---
_id: '8262'
abstract:
- lang: eng
text: "Background: The genus Burkholderia consists of species that occupy remarkably
diverse ecological niches. Its best known members are important pathogens, B.
mallei and B. pseudomallei, which cause glanders and melioidosis, respectively.
Burkholderia genomes are unusual due to their multichromosomal organization, generally
comprised of 2-3 chromosomes.\r\n\r\nResults: We performed integrated genomic
analysis of 127 Burkholderia strains. The pan-genome is open with the saturation
to be reached between 86,000 and 88,000 genes. The reconstructed rearrangements
indicate a strong avoidance of intra-replichore inversions that is likely caused
by selection against the transfer of large groups of genes between the leading
and the lagging strands. Translocated genes also tend to retain their position
in the leading or the lagging strand, and this selection is stronger for large
syntenies. Integrated reconstruction of chromosome rearrangements in the context
of strains phylogeny reveals parallel rearrangements that may indicate inversion-based
phase variation and integration of new genomic islands. In particular, we detected
parallel inversions in the second chromosomes of B. pseudomallei with breakpoints
formed by genes encoding membrane components of multidrug resistance complex,
that may be linked to a phase variation mechanism. Two genomic islands, spreading
horizontally between chromosomes, were detected in the B. cepacia group.\r\n\r\nConclusions:
This study demonstrates the power of integrated analysis of pan-genomes, chromosome
rearrangements, and selection regimes. Non-random inversion patterns indicate
selective pressure, inversions are particularly frequent in a recent pathogen
B. mallei, and, together with periods of positive selection at other branches,
may indicate adaptation to new niches. One such adaptation could be a possible
phase variation mechanism in B. pseudomallei."
article_number: '965'
article_processing_charge: No
article_type: original
author:
- first_name: Olga
full_name: Bochkareva, Olga
id: C4558D3C-6102-11E9-A62E-F418E6697425
last_name: Bochkareva
orcid: 0000-0003-1006-6639
- first_name: Elena V.
full_name: Moroz, Elena V.
last_name: Moroz
- first_name: Iakov I.
full_name: Davydov, Iakov I.
last_name: Davydov
- first_name: Mikhail S.
full_name: Gelfand, Mikhail S.
last_name: Gelfand
citation:
ama: Bochkareva O, Moroz EV, Davydov II, Gelfand MS. Genome rearrangements and selection
in multi-chromosome bacteria Burkholderia spp. BMC Genomics. 2018;19. doi:10.1186/s12864-018-5245-1
apa: Bochkareva, O., Moroz, E. V., Davydov, I. I., & Gelfand, M. S. (2018).
Genome rearrangements and selection in multi-chromosome bacteria Burkholderia
spp. BMC Genomics. Springer Nature. https://doi.org/10.1186/s12864-018-5245-1
chicago: Bochkareva, Olga, Elena V. Moroz, Iakov I. Davydov, and Mikhail S. Gelfand.
“Genome Rearrangements and Selection in Multi-Chromosome Bacteria Burkholderia
Spp.” BMC Genomics. Springer Nature, 2018. https://doi.org/10.1186/s12864-018-5245-1.
ieee: O. Bochkareva, E. V. Moroz, I. I. Davydov, and M. S. Gelfand, “Genome rearrangements
and selection in multi-chromosome bacteria Burkholderia spp.,” BMC Genomics,
vol. 19. Springer Nature, 2018.
ista: Bochkareva O, Moroz EV, Davydov II, Gelfand MS. 2018. Genome rearrangements
and selection in multi-chromosome bacteria Burkholderia spp. BMC Genomics. 19,
965.
mla: Bochkareva, Olga, et al. “Genome Rearrangements and Selection in Multi-Chromosome
Bacteria Burkholderia Spp.” BMC Genomics, vol. 19, 965, Springer Nature,
2018, doi:10.1186/s12864-018-5245-1.
short: O. Bochkareva, E.V. Moroz, I.I. Davydov, M.S. Gelfand, BMC Genomics 19 (2018).
date_created: 2020-08-15T11:02:08Z
date_published: 2018-12-27T00:00:00Z
date_updated: 2023-02-23T13:28:52Z
day: '27'
doi: 10.1186/s12864-018-5245-1
extern: '1'
intvolume: ' 19'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1186/s12864-018-5245-1
month: '12'
oa: 1
oa_version: Published Version
publication: BMC Genomics
publication_identifier:
issn:
- 1471-2164
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Genome rearrangements and selection in multi-chromosome bacteria Burkholderia
spp.
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2018'
...
---
_id: '8265'
abstract:
- lang: eng
text: Genome rearrangements have played an important role in the evolution of Yersinia
pestis from its progenitor Yersinia pseudotuberculosis. Traditional phylogenetic
trees for Y. pestis based on sequence comparison have short internal branches
and low bootstrap supports as only a small number of nucleotide substitutions
have occurred. On the other hand, even a small number of genome rearrangements
may resolve topological ambiguities in a phylogenetic tree. We reconstructed phylogenetic
trees based on genome rearrangements using several popular approaches such as
Maximum likelihood for Gene Order and the Bayesian model of genome rearrangements
by inversions. We also reconciled phylogenetic trees for each of the three CRISPR
loci to obtain an integrated scenario of the CRISPR cassette evolution. Analysis
of contradictions between the obtained evolutionary trees yielded numerous parallel
inversions and gain/loss events. Our data indicate that an integrated analysis
of sequence-based and inversion-based trees enhances the resolution of phylogenetic
reconstruction. In contrast, reconstructions of strain relationships based on
solely CRISPR loci may not be reliable, as the history is obscured by large deletions,
obliterating the order of spacer gains. Similarly, numerous parallel gene losses
preclude reconstruction of phylogeny based on gene content.
article_number: e4545
article_processing_charge: No
article_type: original
author:
- first_name: Olga
full_name: Bochkareva, Olga
id: C4558D3C-6102-11E9-A62E-F418E6697425
last_name: Bochkareva
orcid: 0000-0003-1006-6639
- first_name: Natalia O.
full_name: Dranenko, Natalia O.
last_name: Dranenko
- first_name: Elena S.
full_name: Ocheredko, Elena S.
last_name: Ocheredko
- first_name: German M.
full_name: Kanevsky, German M.
last_name: Kanevsky
- first_name: Yaroslav N.
full_name: Lozinsky, Yaroslav N.
last_name: Lozinsky
- first_name: Vera A.
full_name: Khalaycheva, Vera A.
last_name: Khalaycheva
- first_name: Irena I.
full_name: Artamonova, Irena I.
last_name: Artamonova
- first_name: Mikhail S.
full_name: Gelfand, Mikhail S.
last_name: Gelfand
citation:
ama: Bochkareva O, Dranenko NO, Ocheredko ES, et al. Genome rearrangements and phylogeny
reconstruction in Yersinia pestis. PeerJ. 2018;6. doi:10.7717/peerj.4545
apa: Bochkareva, O., Dranenko, N. O., Ocheredko, E. S., Kanevsky, G. M., Lozinsky,
Y. N., Khalaycheva, V. A., … Gelfand, M. S. (2018). Genome rearrangements and
phylogeny reconstruction in Yersinia pestis. PeerJ. PeerJ. https://doi.org/10.7717/peerj.4545
chicago: Bochkareva, Olga, Natalia O. Dranenko, Elena S. Ocheredko, German M. Kanevsky,
Yaroslav N. Lozinsky, Vera A. Khalaycheva, Irena I. Artamonova, and Mikhail S.
Gelfand. “Genome Rearrangements and Phylogeny Reconstruction in Yersinia Pestis.”
PeerJ. PeerJ, 2018. https://doi.org/10.7717/peerj.4545.
ieee: O. Bochkareva et al., “Genome rearrangements and phylogeny reconstruction
in Yersinia pestis,” PeerJ, vol. 6. PeerJ, 2018.
ista: Bochkareva O, Dranenko NO, Ocheredko ES, Kanevsky GM, Lozinsky YN, Khalaycheva
VA, Artamonova II, Gelfand MS. 2018. Genome rearrangements and phylogeny reconstruction
in Yersinia pestis. PeerJ. 6, e4545.
mla: Bochkareva, Olga, et al. “Genome Rearrangements and Phylogeny Reconstruction
in Yersinia Pestis.” PeerJ, vol. 6, e4545, PeerJ, 2018, doi:10.7717/peerj.4545.
short: O. Bochkareva, N.O. Dranenko, E.S. Ocheredko, G.M. Kanevsky, Y.N. Lozinsky,
V.A. Khalaycheva, I.I. Artamonova, M.S. Gelfand, PeerJ 6 (2018).
date_created: 2020-08-15T11:08:23Z
date_published: 2018-03-27T00:00:00Z
date_updated: 2023-02-23T13:28:57Z
day: '27'
doi: 10.7717/peerj.4545
extern: '1'
external_id:
pmid:
- '29607260'
intvolume: ' 6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.7717/peerj.4545
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
publication: PeerJ
publication_identifier:
issn:
- 2167-8359
publication_status: published
publisher: PeerJ
quality_controlled: '1'
status: public
title: Genome rearrangements and phylogeny reconstruction in Yersinia pestis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 6
year: '2018'
...
---
_id: '8274'
abstract:
- lang: eng
text: 'Background/Aim: Our aim was to investigate the crosstalk between tumor and
immune cells (M2 macrophages) and its effects on cyclo-oxygenase-2 (COX2) regulation
in canine mammary tumors (CMT). Materials and Methods: Sh1b CMT cells and human
BT474 mammary or HT29 colon cancer cells were co-cultured with canine peripheral
blood mononuclear cells (PBMCs) or with macrophage-like differentiated THP1 monocytes
(dTHP1). Intracellular COX2 expression by PBMCs, dTHP1 and cancer cells was evaluated
by flow cytometry. Results: Co-culturing of Sh1b and canine PBMCs induced COX2
overexpression in CMT cells. In turn, COX2 expression by PBMCs, mostly CD68+ macrophages,
was attenuated by co-culture with Sh1b (p=0.0001). In accordance, co-culture with
dTHP1 prompted intracellular production of COX2 in both Sh1b CMT cells and HT29
human colon cancer cells and reduced production of COX2 in BT474 human mammary
cancer cells. The intracellular COX2 expression from dTHP1 decreased when treated
with conditioned medium from cultured Sh1b and HT29 cancer cells. Conclusion:
Bidirectional COX2 regulation between cancer and monocytes/macrophages might shape
a tolerogenic tumor microenvironment in CMT.'
article_processing_charge: No
article_type: original
author:
- first_name: Maria Isabel
full_name: Carvalho, Maria Isabel
last_name: Carvalho
- first_name: Rodolfo
full_name: Bianchini, Rodolfo
last_name: Bianchini
- first_name: Judit
full_name: Fazekas-Singer, Judit
id: 36432834-F248-11E8-B48F-1D18A9856A87
last_name: Fazekas-Singer
orcid: 0000-0002-8777-3502
- first_name: Ina
full_name: Herrmann, Ina
last_name: Herrmann
- first_name: Irene
full_name: Flickinger, Irene
last_name: Flickinger
- first_name: Johann G.
full_name: Thalhammer, Johann G.
last_name: Thalhammer
- first_name: Isabel
full_name: Pires, Isabel
last_name: Pires
- first_name: Erika
full_name: Jensen-Jarolim, Erika
last_name: Jensen-Jarolim
- first_name: Felisbina L.
full_name: Queiroga, Felisbina L.
last_name: Queiroga
citation:
ama: Carvalho MI, Bianchini R, Singer J, et al. Bidirectional regulation of COX-2
expression between cancer cells and macrophages. Anticancer Research. 2018;38(5):2811-2817.
doi:10.21873/anticanres.12525
apa: Carvalho, M. I., Bianchini, R., Singer, J., Herrmann, I., Flickinger, I., Thalhammer,
J. G., … Queiroga, F. L. (2018). Bidirectional regulation of COX-2 expression
between cancer cells and macrophages. Anticancer Research. International
Institute of Anticancer Research. https://doi.org/10.21873/anticanres.12525
chicago: Carvalho, Maria Isabel, Rodolfo Bianchini, Judit Singer, Ina Herrmann,
Irene Flickinger, Johann G. Thalhammer, Isabel Pires, Erika Jensen-Jarolim, and
Felisbina L. Queiroga. “Bidirectional Regulation of COX-2 Expression between Cancer
Cells and Macrophages.” Anticancer Research. International Institute of
Anticancer Research, 2018. https://doi.org/10.21873/anticanres.12525.
ieee: M. I. Carvalho et al., “Bidirectional regulation of COX-2 expression
between cancer cells and macrophages,” Anticancer Research, vol. 38, no.
5. International Institute of Anticancer Research, pp. 2811–2817, 2018.
ista: Carvalho MI, Bianchini R, Singer J, Herrmann I, Flickinger I, Thalhammer JG,
Pires I, Jensen-Jarolim E, Queiroga FL. 2018. Bidirectional regulation of COX-2
expression between cancer cells and macrophages. Anticancer Research. 38(5), 2811–2817.
mla: Carvalho, Maria Isabel, et al. “Bidirectional Regulation of COX-2 Expression
between Cancer Cells and Macrophages.” Anticancer Research, vol. 38, no.
5, International Institute of Anticancer Research, 2018, pp. 2811–17, doi:10.21873/anticanres.12525.
short: M.I. Carvalho, R. Bianchini, J. Singer, I. Herrmann, I. Flickinger, J.G.
Thalhammer, I. Pires, E. Jensen-Jarolim, F.L. Queiroga, Anticancer Research 38
(2018) 2811–2817.
date_created: 2020-08-17T07:13:55Z
date_published: 2018-05-01T00:00:00Z
date_updated: 2021-01-12T08:17:52Z
day: '01'
doi: 10.21873/anticanres.12525
extern: '1'
intvolume: ' 38'
issue: '5'
language:
- iso: eng
month: '05'
oa_version: None
page: 2811-2817
publication: Anticancer Research
publication_identifier:
eissn:
- 1791-7530
issn:
- 0250-7005
publication_status: published
publisher: International Institute of Anticancer Research
quality_controlled: '1'
status: public
title: Bidirectional regulation of COX-2 expression between cancer cells and macrophages
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 38
year: '2018'
...
---
_id: '8297'
abstract:
- lang: eng
text: "Designing a secure permissionless distributed ledger (blockchain) that performs
on par with centralized payment\r\nprocessors, such as Visa, is a challenging
task. Most existing distributed ledgers are unable to scale-out, i.e., to grow
their totalprocessing capacity with the number of validators; and those that do,
compromise security or decentralization. We present OmniLedger, a novel scale-out
distributed ledger that preserves longterm security under permissionless operation.
It ensures security and correctness by using a bias-resistant public-randomness
protocol for choosing large, statistically representative shards that process
transactions, and by introducing an efficient crossshard commit protocol that
atomically handles transactions affecting multiple shards. OmniLedger also optimizes
performance via parallel intra-shard transaction processing, ledger pruning via
collectively-signed state blocks, and low-latency “trust-butverify” \r\nvalidation
for low-value transactions. An evaluation ofour experimental prototype shows that
OmniLedger’s throughput\r\nscales linearly in the number of active validators,
supporting Visa-level workloads and beyond, while confirming typical transactions
in under two seconds."
article_processing_charge: No
author:
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
- first_name: Philipp
full_name: Jovanovic, Philipp
last_name: Jovanovic
- first_name: Linus
full_name: Gasser, Linus
last_name: Gasser
- first_name: Nicolas
full_name: Gailly, Nicolas
last_name: Gailly
- first_name: Ewa
full_name: Syta, Ewa
last_name: Syta
- first_name: Bryan
full_name: Ford, Bryan
last_name: Ford
citation:
ama: 'Kokoris Kogias E, Jovanovic P, Gasser L, Gailly N, Syta E, Ford B. OmniLedger:
A secure, scale-out, decentralized ledger via sharding. In: 2018 IEEE Symposium
on Security and Privacy. IEEE; 2018:583-598. doi:10.1109/sp.2018.000-5'
apa: 'Kokoris Kogias, E., Jovanovic, P., Gasser, L., Gailly, N., Syta, E., &
Ford, B. (2018). OmniLedger: A secure, scale-out, decentralized ledger via sharding.
In 2018 IEEE Symposium on Security and Privacy (pp. 583–598). San Francisco,
CA, United States: IEEE. https://doi.org/10.1109/sp.2018.000-5'
chicago: 'Kokoris Kogias, Eleftherios, Philipp Jovanovic, Linus Gasser, Nicolas
Gailly, Ewa Syta, and Bryan Ford. “OmniLedger: A Secure, Scale-out, Decentralized
Ledger via Sharding.” In 2018 IEEE Symposium on Security and Privacy, 583–98.
IEEE, 2018. https://doi.org/10.1109/sp.2018.000-5.'
ieee: 'E. Kokoris Kogias, P. Jovanovic, L. Gasser, N. Gailly, E. Syta, and B. Ford,
“OmniLedger: A secure, scale-out, decentralized ledger via sharding,” in 2018
IEEE Symposium on Security and Privacy, San Francisco, CA, United States,
2018, pp. 583–598.'
ista: 'Kokoris Kogias E, Jovanovic P, Gasser L, Gailly N, Syta E, Ford B. 2018.
OmniLedger: A secure, scale-out, decentralized ledger via sharding. 2018 IEEE
Symposium on Security and Privacy. SP: Symposium on Security and Privacy, 583–598.'
mla: 'Kokoris Kogias, Eleftherios, et al. “OmniLedger: A Secure, Scale-out, Decentralized
Ledger via Sharding.” 2018 IEEE Symposium on Security and Privacy, IEEE,
2018, pp. 583–98, doi:10.1109/sp.2018.000-5.'
short: E. Kokoris Kogias, P. Jovanovic, L. Gasser, N. Gailly, E. Syta, B. Ford,
in:, 2018 IEEE Symposium on Security and Privacy, IEEE, 2018, pp. 583–598.
conference:
end_date: 2018-05-24
location: San Francisco, CA, United States
name: 'SP: Symposium on Security and Privacy'
start_date: 2018-05-20
date_created: 2020-08-26T11:46:35Z
date_published: 2018-07-26T00:00:00Z
date_updated: 2021-01-12T08:17:56Z
day: '26'
doi: 10.1109/sp.2018.000-5
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://eprint.iacr.org/2017/406
month: '07'
oa: 1
oa_version: Preprint
page: 583-598
publication: 2018 IEEE Symposium on Security and Privacy
publication_identifier:
isbn:
- '9781538643532'
issn:
- 2375-1207
publication_status: published
publisher: IEEE
quality_controlled: '1'
status: public
title: 'OmniLedger: A secure, scale-out, decentralized ledger via sharding'
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2018'
...
---
_id: '8298'
abstract:
- lang: eng
text: Sharding, or partitioning the system’s state so that different subsets of
participants handle it, is a proven approach to building distributed systems whose
total capacity scales horizontally with the number of participants. Many distributed
ledgers have adopted this approach to increase their performance, however, they
focus on the permissionless setting that assumes the existence of a strong adversary.
In this paper, we deploy channels for permissioned blockchains. Our first contribution
is to adapt sharding on asset-management applications for the permissioned setting,
while preserving liveness and safety even on transactions spanning across-channels.
Our second contribution is to leverage channels as a confidentiality boundary,
enabling different organizations and consortia to preserve their privacy within
their channels and still be part of a bigger collaborative ecosystem. To make
our system concrete we map it on top of Hyperledger Fabric.
alternative_title:
- LNCS
article_processing_charge: No
author:
- first_name: Elli
full_name: Androulaki, Elli
last_name: Androulaki
- first_name: Christian
full_name: Cachin, Christian
last_name: Cachin
- first_name: Angelo
full_name: De Caro, Angelo
last_name: De Caro
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
citation:
ama: 'Androulaki E, Cachin C, De Caro A, Kokoris Kogias E. Channels: Horizontal
scaling and confidentiality on permissioned blockchains. In: Computer Security.
Vol 11098. Springer Nature; 2018:111-131. doi:10.1007/978-3-319-99073-6_6'
apa: 'Androulaki, E., Cachin, C., De Caro, A., & Kokoris Kogias, E. (2018).
Channels: Horizontal scaling and confidentiality on permissioned blockchains.
In Computer Security (Vol. 11098, pp. 111–131). Barcelona, Spain: Springer
Nature. https://doi.org/10.1007/978-3-319-99073-6_6'
chicago: 'Androulaki, Elli, Christian Cachin, Angelo De Caro, and Eleftherios Kokoris
Kogias. “Channels: Horizontal Scaling and Confidentiality on Permissioned Blockchains.”
In Computer Security, 11098:111–31. Springer Nature, 2018. https://doi.org/10.1007/978-3-319-99073-6_6.'
ieee: 'E. Androulaki, C. Cachin, A. De Caro, and E. Kokoris Kogias, “Channels: Horizontal
scaling and confidentiality on permissioned blockchains,” in Computer Security,
Barcelona, Spain, 2018, vol. 11098, pp. 111–131.'
ista: 'Androulaki E, Cachin C, De Caro A, Kokoris Kogias E. 2018. Channels: Horizontal
scaling and confidentiality on permissioned blockchains. Computer Security. ESORICS:
European Symposium on Research in Computer Security, LNCS, vol. 11098, 111–131.'
mla: 'Androulaki, Elli, et al. “Channels: Horizontal Scaling and Confidentiality
on Permissioned Blockchains.” Computer Security, vol. 11098, Springer Nature,
2018, pp. 111–31, doi:10.1007/978-3-319-99073-6_6.'
short: E. Androulaki, C. Cachin, A. De Caro, E. Kokoris Kogias, in:, Computer Security,
Springer Nature, 2018, pp. 111–131.
conference:
end_date: 2018-09-07
location: Barcelona, Spain
name: 'ESORICS: European Symposium on Research in Computer Security'
start_date: 2018-09-03
date_created: 2020-08-26T11:47:34Z
date_published: 2018-08-08T00:00:00Z
date_updated: 2021-01-12T08:17:57Z
day: '08'
doi: 10.1007/978-3-319-99073-6_6
extern: '1'
intvolume: ' 11098'
language:
- iso: eng
month: '08'
oa_version: None
page: 111-131
publication: Computer Security
publication_identifier:
eisbn:
- '9783319990736'
isbn:
- '9783319990729'
issn:
- 0302-9743
- 1611-3349
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Channels: Horizontal scaling and confidentiality on permissioned blockchains'
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 11098
year: '2018'
...
---
_id: '83'
abstract:
- lang: eng
text: "A proof system is a protocol between a prover and a verifier over a common
input in which an honest prover convinces the verifier of the validity of true
statements. Motivated by the success of decentralized cryptocurrencies, exemplified
by Bitcoin, the focus of this thesis will be on proof systems which found applications
in some sustainable alternatives to Bitcoin, such as the Spacemint and Chia cryptocurrencies.
In particular, we focus on proofs of space and proofs of sequential work.\r\nProofs
of space (PoSpace) were suggested as more ecological, economical, and egalitarian
alternative to the energy-wasteful proof-of-work mining of Bitcoin. However, the
state-of-the-art constructions of PoSpace are based on sophisticated graph pebbling
lower bounds, and are therefore complex. Moreover, when these PoSpace are used
in cryptocurrencies like Spacemint, miners can only start mining after ensuring
that a commitment to their space is already added in a special transaction to
the blockchain. Proofs of sequential work (PoSW) are proof systems in which a
prover, upon receiving a statement x and a time parameter T, computes a proof
which convinces the verifier that T time units had passed since x was received.
Whereas Spacemint assumes synchrony to retain some interesting Bitcoin dynamics,
Chia requires PoSW with unique proofs, i.e., PoSW in which it is hard to come
up with more than one accepting proof for any true statement. In this thesis we
construct simple and practically-efficient PoSpace and PoSW. When using our PoSpace
in cryptocurrencies, miners can start mining on the fly, like in Bitcoin, and
unlike current constructions of PoSW, which either achieve efficient verification
of sequential work, or faster-than-recomputing verification of correctness of
proofs, but not both at the same time, ours achieve the best of these two worlds."
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Hamza M
full_name: Abusalah, Hamza M
id: 40297222-F248-11E8-B48F-1D18A9856A87
last_name: Abusalah
citation:
ama: Abusalah HM. Proof systems for sustainable decentralized cryptocurrencies.
2018. doi:10.15479/AT:ISTA:TH_1046
apa: Abusalah, H. M. (2018). Proof systems for sustainable decentralized cryptocurrencies.
Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:TH_1046
chicago: Abusalah, Hamza M. “Proof Systems for Sustainable Decentralized Cryptocurrencies.”
Institute of Science and Technology Austria, 2018. https://doi.org/10.15479/AT:ISTA:TH_1046.
ieee: H. M. Abusalah, “Proof systems for sustainable decentralized cryptocurrencies,”
Institute of Science and Technology Austria, 2018.
ista: Abusalah HM. 2018. Proof systems for sustainable decentralized cryptocurrencies.
Institute of Science and Technology Austria.
mla: Abusalah, Hamza M. Proof Systems for Sustainable Decentralized Cryptocurrencies.
Institute of Science and Technology Austria, 2018, doi:10.15479/AT:ISTA:TH_1046.
short: H.M. Abusalah, Proof Systems for Sustainable Decentralized Cryptocurrencies,
Institute of Science and Technology Austria, 2018.
date_created: 2018-12-11T11:44:32Z
date_published: 2018-09-05T00:00:00Z
date_updated: 2023-09-07T12:30:23Z
day: '05'
ddc:
- '004'
degree_awarded: PhD
department:
- _id: KrPi
doi: 10.15479/AT:ISTA:TH_1046
ec_funded: 1
file:
- access_level: open_access
checksum: c4b5f7d111755d1396787f41886fc674
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creator: dernst
date_created: 2019-04-09T06:43:41Z
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file_size: 2029190
relation: source_file
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has_accepted_license: '1'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: '59'
project:
- _id: 258C570E-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '259668'
name: Provable Security for Physical Cryptography
- _id: 258AA5B2-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '682815'
name: Teaching Old Crypto New Tricks
publication_identifier:
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
publist_id: '7971'
pubrep_id: '1046'
related_material:
record:
- id: '1229'
relation: part_of_dissertation
status: public
- id: '1235'
relation: part_of_dissertation
status: public
- id: '1236'
relation: part_of_dissertation
status: public
- id: '559'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Krzysztof Z
full_name: Pietrzak, Krzysztof Z
id: 3E04A7AA-F248-11E8-B48F-1D18A9856A87
last_name: Pietrzak
orcid: 0000-0002-9139-1654
title: Proof systems for sustainable decentralized cryptocurrencies
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2018'
...
---
_id: '8417'
abstract:
- lang: eng
text: The restricted planar elliptic three body problem (RPETBP) describes the motion
of a massless particle (a comet or an asteroid) under the gravitational field
of two massive bodies (the primaries, say the Sun and Jupiter) revolving around
their center of mass on elliptic orbits with some positive eccentricity. The aim
of this paper is to show the existence of orbits whose angular momentum performs
arbitrary excursions in a large region. In particular, there exist diffusive orbits,
that is, with a large variation of angular momentum. The leading idea of the proof
consists in analyzing parabolic motions of the comet. By a well-known result of
McGehee, the union of future (resp. past) parabolic orbits is an analytic manifold
P+ (resp. P−). In a properly chosen coordinate system these manifolds are stable
(resp. unstable) manifolds of a manifold at infinity P∞, which we call the manifold
at parabolic infinity. On P∞ it is possible to define two scattering maps, which
contain the map structure of the homoclinic trajectories to it, i.e. orbits parabolic
both in the future and the past. Since the inner dynamics inside P∞ is trivial,
two different scattering maps are used. The combination of these two scattering
maps permits the design of the desired diffusive pseudo-orbits. Using shadowing
techniques and these pseudo orbits we show the existence of true trajectories
of the RPETBP whose angular momentum varies in any predetermined fashion.
article_processing_charge: No
article_type: original
author:
- first_name: Amadeu
full_name: Delshams, Amadeu
last_name: Delshams
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Abraham
full_name: de la Rosa, Abraham
last_name: de la Rosa
- first_name: Tere M.
full_name: Seara, Tere M.
last_name: Seara
citation:
ama: Delshams A, Kaloshin V, de la Rosa A, Seara TM. Global instability in the restricted
planar elliptic three body problem. Communications in Mathematical Physics.
2018;366(3):1173-1228. doi:10.1007/s00220-018-3248-z
apa: Delshams, A., Kaloshin, V., de la Rosa, A., & Seara, T. M. (2018). Global
instability in the restricted planar elliptic three body problem. Communications
in Mathematical Physics. Springer Nature. https://doi.org/10.1007/s00220-018-3248-z
chicago: Delshams, Amadeu, Vadim Kaloshin, Abraham de la Rosa, and Tere M. Seara.
“Global Instability in the Restricted Planar Elliptic Three Body Problem.” Communications
in Mathematical Physics. Springer Nature, 2018. https://doi.org/10.1007/s00220-018-3248-z.
ieee: A. Delshams, V. Kaloshin, A. de la Rosa, and T. M. Seara, “Global instability
in the restricted planar elliptic three body problem,” Communications in Mathematical
Physics, vol. 366, no. 3. Springer Nature, pp. 1173–1228, 2018.
ista: Delshams A, Kaloshin V, de la Rosa A, Seara TM. 2018. Global instability in
the restricted planar elliptic three body problem. Communications in Mathematical
Physics. 366(3), 1173–1228.
mla: Delshams, Amadeu, et al. “Global Instability in the Restricted Planar Elliptic
Three Body Problem.” Communications in Mathematical Physics, vol. 366,
no. 3, Springer Nature, 2018, pp. 1173–228, doi:10.1007/s00220-018-3248-z.
short: A. Delshams, V. Kaloshin, A. de la Rosa, T.M. Seara, Communications in Mathematical
Physics 366 (2018) 1173–1228.
date_created: 2020-09-17T10:41:43Z
date_published: 2018-09-05T00:00:00Z
date_updated: 2021-01-12T08:19:08Z
day: '05'
doi: 10.1007/s00220-018-3248-z
extern: '1'
intvolume: ' 366'
issue: '3'
keyword:
- Mathematical Physics
- Statistical and Nonlinear Physics
language:
- iso: eng
month: '09'
oa_version: None
page: 1173-1228
publication: Communications in Mathematical Physics
publication_identifier:
issn:
- 0010-3616
- 1432-0916
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Global instability in the restricted planar elliptic three body problem
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 366
year: '2018'
...
---
_id: '8419'
abstract:
- lang: eng
text: "In this survey, we provide a concise introduction to convex billiards and
describe some recent results, obtained by the authors and collaborators, on the
classification of integrable billiards, namely the so-called Birkhoff conjecture.\r\n\r\nThis
article is part of the theme issue ‘Finite dimensional integrable systems: new
trends and methods’."
article_number: '20170419'
article_processing_charge: No
article_type: original
author:
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Alfonso
full_name: Sorrentino, Alfonso
last_name: Sorrentino
citation:
ama: 'Kaloshin V, Sorrentino A. On the integrability of Birkhoff billiards. Philosophical
Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences.
2018;376(2131). doi:10.1098/rsta.2017.0419'
apa: 'Kaloshin, V., & Sorrentino, A. (2018). On the integrability of Birkhoff
billiards. Philosophical Transactions of the Royal Society A: Mathematical,
Physical and Engineering Sciences. The Royal Society. https://doi.org/10.1098/rsta.2017.0419'
chicago: 'Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff
Billiards.” Philosophical Transactions of the Royal Society A: Mathematical,
Physical and Engineering Sciences. The Royal Society, 2018. https://doi.org/10.1098/rsta.2017.0419.'
ieee: 'V. Kaloshin and A. Sorrentino, “On the integrability of Birkhoff billiards,”
Philosophical Transactions of the Royal Society A: Mathematical, Physical and
Engineering Sciences, vol. 376, no. 2131. The Royal Society, 2018.'
ista: 'Kaloshin V, Sorrentino A. 2018. On the integrability of Birkhoff billiards.
Philosophical Transactions of the Royal Society A: Mathematical, Physical and
Engineering Sciences. 376(2131), 20170419.'
mla: 'Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff
Billiards.” Philosophical Transactions of the Royal Society A: Mathematical,
Physical and Engineering Sciences, vol. 376, no. 2131, 20170419, The Royal
Society, 2018, doi:10.1098/rsta.2017.0419.'
short: 'V. Kaloshin, A. Sorrentino, Philosophical Transactions of the Royal Society
A: Mathematical, Physical and Engineering Sciences 376 (2018).'
date_created: 2020-09-17T10:42:01Z
date_published: 2018-10-28T00:00:00Z
date_updated: 2021-01-12T08:19:09Z
day: '28'
doi: 10.1098/rsta.2017.0419
extern: '1'
intvolume: ' 376'
issue: '2131'
keyword:
- General Engineering
- General Physics and Astronomy
- General Mathematics
language:
- iso: eng
month: '10'
oa_version: None
publication: 'Philosophical Transactions of the Royal Society A: Mathematical, Physical
and Engineering Sciences'
publication_identifier:
issn:
- 1364-503X
- 1471-2962
publication_status: published
publisher: The Royal Society
quality_controlled: '1'
status: public
title: On the integrability of Birkhoff billiards
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 376
year: '2018'
...
---
_id: '8420'
abstract:
- lang: eng
text: We show that in the space of all convex billiard boundaries, the set of boundaries
with rational caustics is dense. More precisely, the set of billiard boundaries
with caustics of rotation number 1/q is polynomially sense in the smooth case,
and exponentially dense in the analytic case.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Ke
full_name: Zhang, Ke
last_name: Zhang
citation:
ama: Kaloshin V, Zhang K. Density of convex billiards with rational caustics. Nonlinearity.
2018;31(11):5214-5234. doi:10.1088/1361-6544/aadc12
apa: Kaloshin, V., & Zhang, K. (2018). Density of convex billiards with rational
caustics. Nonlinearity. IOP Publishing. https://doi.org/10.1088/1361-6544/aadc12
chicago: Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational
Caustics.” Nonlinearity. IOP Publishing, 2018. https://doi.org/10.1088/1361-6544/aadc12.
ieee: V. Kaloshin and K. Zhang, “Density of convex billiards with rational caustics,”
Nonlinearity, vol. 31, no. 11. IOP Publishing, pp. 5214–5234, 2018.
ista: Kaloshin V, Zhang K. 2018. Density of convex billiards with rational caustics.
Nonlinearity. 31(11), 5214–5234.
mla: Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational Caustics.”
Nonlinearity, vol. 31, no. 11, IOP Publishing, 2018, pp. 5214–34, doi:10.1088/1361-6544/aadc12.
short: V. Kaloshin, K. Zhang, Nonlinearity 31 (2018) 5214–5234.
date_created: 2020-09-17T10:42:09Z
date_published: 2018-10-15T00:00:00Z
date_updated: 2021-01-12T08:19:10Z
day: '15'
doi: 10.1088/1361-6544/aadc12
extern: '1'
external_id:
arxiv:
- '1706.07968'
intvolume: ' 31'
issue: '11'
keyword:
- Mathematical Physics
- General Physics and Astronomy
- Applied Mathematics
- Statistical and Nonlinear Physics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1706.07968
month: '10'
oa: 1
oa_version: Preprint
page: 5214-5234
publication: Nonlinearity
publication_identifier:
issn:
- 0951-7715
- 1361-6544
publication_status: published
publisher: IOP Publishing
quality_controlled: '1'
status: public
title: Density of convex billiards with rational caustics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 31
year: '2018'
...
---
_id: '8421'
abstract:
- lang: eng
text: 'The classical Birkhoff conjecture claims that the boundary of a strictly
convex integrable billiard table is necessarily an ellipse (or a circle as a special
case). In this article we prove a complete local version of this conjecture: a
small integrable perturbation of an ellipse must be an ellipse. This extends and
completes the result in Avila-De Simoi-Kaloshin, where nearly circular domains
were considered. One of the crucial ideas in the proof is to extend action-angle
coordinates for elliptic billiards into complex domains (with respect to the angle),
and to thoroughly analyze the nature of their complex singularities. As an application,
we are able to prove some spectral rigidity results for elliptic domains.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Alfonso
full_name: Sorrentino, Alfonso
last_name: Sorrentino
citation:
ama: Kaloshin V, Sorrentino A. On the local Birkhoff conjecture for convex billiards.
Annals of Mathematics. 2018;188(1):315-380. doi:10.4007/annals.2018.188.1.6
apa: Kaloshin, V., & Sorrentino, A. (2018). On the local Birkhoff conjecture
for convex billiards. Annals of Mathematics. Annals of Mathematics, Princeton
U. https://doi.org/10.4007/annals.2018.188.1.6
chicago: Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture
for Convex Billiards.” Annals of Mathematics. Annals of Mathematics, Princeton
U, 2018. https://doi.org/10.4007/annals.2018.188.1.6.
ieee: V. Kaloshin and A. Sorrentino, “On the local Birkhoff conjecture for convex
billiards,” Annals of Mathematics, vol. 188, no. 1. Annals of Mathematics,
Princeton U, pp. 315–380, 2018.
ista: Kaloshin V, Sorrentino A. 2018. On the local Birkhoff conjecture for convex
billiards. Annals of Mathematics. 188(1), 315–380.
mla: Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture
for Convex Billiards.” Annals of Mathematics, vol. 188, no. 1, Annals of
Mathematics, Princeton U, 2018, pp. 315–80, doi:10.4007/annals.2018.188.1.6.
short: V. Kaloshin, A. Sorrentino, Annals of Mathematics 188 (2018) 315–380.
date_created: 2020-09-17T10:42:22Z
date_published: 2018-07-01T00:00:00Z
date_updated: 2021-01-12T08:19:10Z
day: '01'
doi: 10.4007/annals.2018.188.1.6
extern: '1'
external_id:
arxiv:
- '1612.09194'
intvolume: ' 188'
issue: '1'
keyword:
- Statistics
- Probability and Uncertainty
- Statistics and Probability
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1612.09194
month: '07'
oa: 1
oa_version: Preprint
page: 315-380
publication: Annals of Mathematics
publication_identifier:
issn:
- 0003-486X
publication_status: published
publisher: Annals of Mathematics, Princeton U
quality_controlled: '1'
status: public
title: On the local Birkhoff conjecture for convex billiards
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 188
year: '2018'
...
---
_id: '8422'
abstract:
- lang: eng
text: 'The Birkhoff conjecture says that the boundary of a strictly convex integrable
billiard table is necessarily an ellipse. In this article, we consider a stronger
notion of integrability, namely integrability close to the boundary, and prove
a local version of this conjecture: a small perturbation of an ellipse of small
eccentricity which preserves integrability near the boundary, is itself an ellipse.
This extends the result in Avila et al. (Ann Math 184:527–558, ADK16), where integrability
was assumed on a larger set. In particular, it shows that (local) integrability
near the boundary implies global integrability. One of the crucial ideas in the
proof consists in analyzing Taylor expansion of the corresponding action-angle
coordinates with respect to the eccentricity parameter, deriving and studying
higher order conditions for the preservation of integrable rational caustics.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Guan
full_name: Huang, Guan
last_name: Huang
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Alfonso
full_name: Sorrentino, Alfonso
last_name: Sorrentino
citation:
ama: Huang G, Kaloshin V, Sorrentino A. Nearly circular domains which are integrable
close to the boundary are ellipses. Geometric and Functional Analysis.
2018;28(2):334-392. doi:10.1007/s00039-018-0440-4
apa: Huang, G., Kaloshin, V., & Sorrentino, A. (2018). Nearly circular domains
which are integrable close to the boundary are ellipses. Geometric and Functional
Analysis. Springer Nature. https://doi.org/10.1007/s00039-018-0440-4
chicago: Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “Nearly Circular Domains
Which Are Integrable Close to the Boundary Are Ellipses.” Geometric and Functional
Analysis. Springer Nature, 2018. https://doi.org/10.1007/s00039-018-0440-4.
ieee: G. Huang, V. Kaloshin, and A. Sorrentino, “Nearly circular domains which are
integrable close to the boundary are ellipses,” Geometric and Functional Analysis,
vol. 28, no. 2. Springer Nature, pp. 334–392, 2018.
ista: Huang G, Kaloshin V, Sorrentino A. 2018. Nearly circular domains which are
integrable close to the boundary are ellipses. Geometric and Functional Analysis.
28(2), 334–392.
mla: Huang, Guan, et al. “Nearly Circular Domains Which Are Integrable Close to
the Boundary Are Ellipses.” Geometric and Functional Analysis, vol. 28,
no. 2, Springer Nature, 2018, pp. 334–92, doi:10.1007/s00039-018-0440-4.
short: G. Huang, V. Kaloshin, A. Sorrentino, Geometric and Functional Analysis 28
(2018) 334–392.
date_created: 2020-09-17T10:42:30Z
date_published: 2018-03-18T00:00:00Z
date_updated: 2021-01-12T08:19:11Z
day: '18'
doi: 10.1007/s00039-018-0440-4
extern: '1'
external_id:
arxiv:
- '1705.10601'
intvolume: ' 28'
issue: '2'
keyword:
- Geometry and Topology
- Analysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1705.10601
month: '03'
oa: 1
oa_version: Preprint
page: 334-392
publication: Geometric and Functional Analysis
publication_identifier:
issn:
- 1016-443X
- 1420-8970
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Nearly circular domains which are integrable close to the boundary are ellipses
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 28
year: '2018'
...
---
_id: '8426'
abstract:
- lang: eng
text: For any strictly convex planar domain Ω ⊂ R2 with a C∞ boundary one can associate
an infinite sequence of spectral invariants introduced by Marvizi–Merlose [5].
These invariants can generically be determined using the spectrum of the Dirichlet
problem of the Laplace operator. A natural question asks if this collection is
sufficient to determine Ω up to isometry. In this paper we give a counterexample,
namely, we present two nonisometric domains Ω and Ω¯ with the same collection
of Marvizi–Melrose invariants. Moreover, each domain has countably many periodic
orbits {Sn}n≥1 (resp. {S¯n}n⩾1) of period going to infinity such that Sn and S¯n
have the same period and perimeter for each n.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Lev
full_name: Buhovsky, Lev
last_name: Buhovsky
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
citation:
ama: Buhovsky L, Kaloshin V. Nonisometric domains with the same Marvizi-Melrose
invariants. Regular and Chaotic Dynamics. 2018;23:54-59. doi:10.1134/s1560354718010057
apa: Buhovsky, L., & Kaloshin, V. (2018). Nonisometric domains with the same
Marvizi-Melrose invariants. Regular and Chaotic Dynamics. Springer Nature.
https://doi.org/10.1134/s1560354718010057
chicago: Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same
Marvizi-Melrose Invariants.” Regular and Chaotic Dynamics. Springer Nature,
2018. https://doi.org/10.1134/s1560354718010057.
ieee: L. Buhovsky and V. Kaloshin, “Nonisometric domains with the same Marvizi-Melrose
invariants,” Regular and Chaotic Dynamics, vol. 23. Springer Nature, pp.
54–59, 2018.
ista: Buhovsky L, Kaloshin V. 2018. Nonisometric domains with the same Marvizi-Melrose
invariants. Regular and Chaotic Dynamics. 23, 54–59.
mla: Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose
Invariants.” Regular and Chaotic Dynamics, vol. 23, Springer Nature, 2018,
pp. 54–59, doi:10.1134/s1560354718010057.
short: L. Buhovsky, V. Kaloshin, Regular and Chaotic Dynamics 23 (2018) 54–59.
date_created: 2020-09-17T10:43:21Z
date_published: 2018-02-05T00:00:00Z
date_updated: 2021-01-12T08:19:11Z
day: '05'
doi: 10.1134/s1560354718010057
extern: '1'
external_id:
arxiv:
- '1801.00952'
intvolume: ' 23'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1801.00952
month: '02'
oa: 1
oa_version: Preprint
page: 54-59
publication: Regular and Chaotic Dynamics
publication_identifier:
issn:
- 1560-3547
- 1468-4845
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Nonisometric domains with the same Marvizi-Melrose invariants
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2018'
...
---
_id: '8436'
abstract:
- lang: eng
text: The exchange of metabolites between the mitochondrial matrix and the cytosol
depends on β-barrel channels in the outer membrane and α-helical carrier proteins
in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones
escort these proteins through the intermembrane space, but the structural and
mechanistic details remain elusive. We have used an integrated structural biology
approach to reveal the functional principle of TIM chaperones. Multiple clamp-like
binding sites hold the mitochondrial membrane proteins in a translocation-competent
elongated form, thus mimicking characteristics of co-translational membrane insertion.
The bound preprotein undergoes conformational dynamics within the chaperone binding
clefts, pointing to a multitude of dynamic local binding events. Mutations in
these binding sites cause cell death or growth defects associated with impairment
of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial
“transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins
in a “nascent chain-like” conformation through a ribosome-free compartment.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Caroline
full_name: Lindau, Caroline
last_name: Lindau
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Yong
full_name: Wang, Yong
last_name: Wang
- first_name: Conny
full_name: Schütze, Conny
last_name: Schütze
- first_name: Tobias
full_name: Jores, Tobias
last_name: Jores
- first_name: Laura
full_name: Melchionda, Laura
last_name: Melchionda
- first_name: Birgit
full_name: Schönfisch, Birgit
last_name: Schönfisch
- first_name: Hubert
full_name: Kalbacher, Hubert
last_name: Kalbacher
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Doron
full_name: Rapaport, Doron
last_name: Rapaport
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Kresten
full_name: Lindorff-Larsen, Kresten
last_name: Lindorff-Larsen
- first_name: Nils
full_name: Wiedemann, Nils
last_name: Wiedemann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein
chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25.
doi:10.1016/j.cell.2018.10.039
apa: Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., …
Schanda, P. (2018). Structural basis of membrane protein chaperoning through the
mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039
chicago: Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny
Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane
Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell.
Elsevier, 2018. https://doi.org/10.1016/j.cell.2018.10.039.
ieee: K. Weinhäupl et al., “Structural basis of membrane protein chaperoning
through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5.
Elsevier, p. 1365–1379.e25, 2018.
ista: Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L,
Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K,
Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning
through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.
mla: Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning
through the Mitochondrial Intermembrane Space.” Cell, vol. 175, no. 5,
Elsevier, 2018, p. 1365–1379.e25, doi:10.1016/j.cell.2018.10.039.
short: K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda,
B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen,
N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.
date_created: 2020-09-18T10:04:39Z
date_published: 2018-11-15T00:00:00Z
date_updated: 2021-01-12T08:19:15Z
day: '15'
doi: 10.1016/j.cell.2018.10.039
extern: '1'
intvolume: ' 175'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '11'
oa_version: None
page: 1365-1379.e25
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Structural basis of membrane protein chaperoning through the mitochondrial
intermembrane space
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 175
year: '2018'
...
---
_id: '8437'
abstract:
- lang: eng
text: Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota,
and archaea, facilitating the folding of proteins, preventing protein aggregation,
and thus participating in maintaining protein homeostasis in the cell. During
their functional cycle, they bind unfolded client proteins inside their double
ring structure and promote protein folding by closing the ring chamber in an adenosine
5′-triphosphate (ATP)–dependent manner. Although the static structures of fully
open and closed forms of chaperonins were solved by x-ray crystallography or electron
microscopy, elucidating the mechanisms of such ATP-driven molecular events requires
studying the proteins at the structural level under working conditions. We introduce
an approach that combines site-specific nuclear magnetic resonance observation
of very large proteins, enabled by advanced isotope labeling methods, with an
in situ ATP regeneration system. Using this method, we provide functional insight
into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal
how nucleotide binding, hydrolysis, and release control switching between closed
and open states. While the open conformation stabilizes the unfolded state of
client proteins, the internalization of the client protein inside the chaperonin
cavity speeds up its functional cycle. This approach opens new perspectives to
study structures and mechanisms of various ATP-driven biological machineries in
the heat of action.
article_number: eaau4196
article_processing_charge: No
article_type: original
author:
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jia-Ying
full_name: Guan, Jia-Ying
last_name: Guan
- first_name: Elodie
full_name: Crublet, Elodie
last_name: Crublet
- first_name: Elisa Colas
full_name: Debled, Elisa Colas
last_name: Debled
- first_name: Christine
full_name: Moriscot, Christine
last_name: Moriscot
- first_name: Pierre
full_name: Gans, Pierre
last_name: Gans
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin
in action reveals how nucleotide binding regulates the functional cycle. Science
Advances. 2018;4(9). doi:10.1126/sciadv.aau4196
apa: Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., …
Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals
how nucleotide binding regulates the functional cycle. Science Advances.
American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aau4196
chicago: Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine
Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier.
“Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding
Regulates the Functional Cycle.” Science Advances. American Association
for the Advancement of Science, 2018. https://doi.org/10.1126/sciadv.aau4196.
ieee: G. Mas et al., “Structural investigation of a chaperonin in action
reveals how nucleotide binding regulates the functional cycle,” Science Advances,
vol. 4, no. 9. American Association for the Advancement of Science, 2018.
ista: Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek
P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in
action reveals how nucleotide binding regulates the functional cycle. Science
Advances. 4(9), eaau4196.
mla: Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action
Reveals How Nucleotide Binding Regulates the Functional Cycle.” Science Advances,
vol. 4, no. 9, eaau4196, American Association for the Advancement of Science,
2018, doi:10.1126/sciadv.aau4196.
short: G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn,
P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).
date_created: 2020-09-18T10:04:51Z
date_published: 2018-09-19T00:00:00Z
date_updated: 2022-08-26T09:11:06Z
day: '19'
doi: 10.1126/sciadv.aau4196
extern: '1'
intvolume: ' 4'
issue: '9'
language:
- iso: eng
month: '09'
oa_version: None
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Structural investigation of a chaperonin in action reveals how nucleotide binding
regulates the functional cycle
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 4
year: '2018'
...
---
_id: '8438'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and
interactions of AAC3 in DPC are not functionally relevant. Nature Structural
& Molecular Biology. 2018;25(9):745-747. doi:10.1038/s41594-018-0127-4
apa: Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., & Schanda,
P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant.
Nature Structural & Molecular Biology. Springer Nature. https://doi.org/10.1038/s41594-018-0127-4
chicago: Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate
Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally
Relevant.” Nature Structural & Molecular Biology. Springer Nature,
2018. https://doi.org/10.1038/s41594-018-0127-4.
ieee: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics
and interactions of AAC3 in DPC are not functionally relevant,” Nature Structural
& Molecular Biology, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.
ista: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics
and interactions of AAC3 in DPC are not functionally relevant. Nature Structural
& Molecular Biology. 25(9), 745–747.
mla: Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not
Functionally Relevant.” Nature Structural & Molecular Biology, vol.
25, no. 9, Springer Nature, 2018, pp. 745–47, doi:10.1038/s41594-018-0127-4.
short: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature
Structural & Molecular Biology 25 (2018) 745–747.
date_created: 2020-09-18T10:04:59Z
date_published: 2018-09-03T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '03'
doi: 10.1038/s41594-018-0127-4
extern: '1'
intvolume: ' 25'
issue: '9'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 745-747
publication: Nature Structural & Molecular Biology
publication_identifier:
issn:
- 1545-9993
- 1545-9985
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Dynamics and interactions of AAC3 in DPC are not functionally relevant
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 25
year: '2018'
...
---
_id: '8439'
abstract:
- lang: eng
text: Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer
of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly
hampers their structural study in an environment similar to the bacterial surface.
We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long
O-antigen polysaccharides assembled in solution as vesicles or elongated micelles.
Solid-state NMR with magic-angle spinning permitted the identification of NMR
signals arising from regions with different flexibilities in the LPS, from the
lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS
enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa
LPS, for which we could confirm that a specific oligosaccharide is involved in
the antibiotic binding. The possibility to study LPS alone and bound to a ligand
when it is assembled in membrane-like structures opens great prospects for the
investigation of proteins and antibiotics that specifically target such an important
molecule at the surface of Gram-negative bacteria.
article_processing_charge: No
article_type: original
author:
- first_name: Cedric
full_name: Laguri, Cedric
last_name: Laguri
- first_name: Alba
full_name: Silipo, Alba
last_name: Silipo
- first_name: Alessandra M.
full_name: Martorana, Alessandra M.
last_name: Martorana
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Roberta
full_name: Marchetti, Roberta
last_name: Marchetti
- first_name: Alessandra
full_name: Polissi, Alessandra
last_name: Polissi
- first_name: Antonio
full_name: Molinaro, Antonio
last_name: Molinaro
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
citation:
ama: Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact
lipopolysaccharide endotoxin. ACS Chemical Biology. 2018;13(8):2106-2113.
doi:10.1021/acschembio.8b00271
apa: Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi,
A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide
endotoxin. ACS Chemical Biology. American Chemical Society. https://doi.org/10.1021/acschembio.8b00271
chicago: Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta
Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid
State NMR Studies of Intact Lipopolysaccharide Endotoxin.” ACS Chemical Biology.
American Chemical Society, 2018. https://doi.org/10.1021/acschembio.8b00271.
ieee: C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide
endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society,
pp. 2106–2113, 2018.
ista: Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro
A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin.
ACS Chemical Biology. 13(8), 2106–2113.
mla: Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide
Endotoxin.” ACS Chemical Biology, vol. 13, no. 8, American Chemical Society,
2018, pp. 2106–13, doi:10.1021/acschembio.8b00271.
short: C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi,
A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.
date_created: 2020-09-18T10:05:09Z
date_published: 2018-07-02T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '02'
doi: 10.1021/acschembio.8b00271
extern: '1'
intvolume: ' 13'
issue: '8'
keyword:
- Molecular Medicine
- Biochemistry
- General Medicine
language:
- iso: eng
month: '07'
oa_version: None
page: 2106-2113
publication: ACS Chemical Biology
publication_identifier:
issn:
- 1554-8929
- 1554-8937
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Solid state NMR studies of intact lipopolysaccharide endotoxin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2018'
...
---
_id: '8440'
abstract:
- lang: eng
text: Mycobacterium tuberculosis can remain dormant in the host, an ability that
explains the failure of many current tuberculosis treatments. Recently, the natural
products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill
Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of
the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein
substrates, such as proteins containing phosphorylated arginine residues, to the
ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit
ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using
NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding
to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these
dynamics are caused by conformational changes and do not result from unfolding
or oligomerization of this domain. Cyclomarin binding to this domain specifically
blocked these N-terminal dynamics. On the basis of these results, we propose a
mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics,
which modulates the chaperone enzymatic activity leading eventually to cell death.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Uli
full_name: Kazmaier, Uli
last_name: Kazmaier
- first_name: Joel
full_name: Lelievre, Joel
last_name: Lelievre
- first_name: Lluis
full_name: Ballell, Lluis
last_name: Ballell
- first_name: Alfred
full_name: Goldberg, Alfred
last_name: Goldberg
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
citation:
ama: Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks
arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1
from Mycobacterium tuberculosis. Journal of Biological Chemistry. 2018;293(22):8379-8393.
doi:10.1074/jbc.ra118.002251
apa: Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg,
A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
Journal of Biological Chemistry. American Society for Biochemistry &
Molecular Biology. https://doi.org/10.1074/jbc.ra118.002251
chicago: Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis
Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin
Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain
of ClpC1 from Mycobacterium Tuberculosis.” Journal of Biological Chemistry.
American Society for Biochemistry & Molecular Biology, 2018. https://doi.org/10.1074/jbc.ra118.002251.
ieee: K. Weinhäupl et al., “The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,”
Journal of Biological Chemistry, vol. 293, no. 22. American Society for
Biochemistry & Molecular Biology, pp. 8379–8393, 2018.
ista: Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda
P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
Journal of Biological Chemistry. 293(22), 8379–8393.
mla: Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced
Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.”
Journal of Biological Chemistry, vol. 293, no. 22, American Society for
Biochemistry & Molecular Biology, 2018, pp. 8379–93, doi:10.1074/jbc.ra118.002251.
short: K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg,
P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
date_created: 2020-09-18T10:05:18Z
date_published: 2018-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '01'
doi: 10.1074/jbc.ra118.002251
extern: '1'
intvolume: ' 293'
issue: '22'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 8379-8393
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
- 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics
in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 293
year: '2018'
...
---
_id: '8441'
abstract:
- lang: eng
text: Solid-state near-rotary-resonance measurements of the spin–lattice relaxation
rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular
dynamics in the microsecond time scale. The small difference between the spin-lock
(SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions,
at the same time it brings up some methodological challenges. In this work, several
issues affecting correct measurements and analysis of 15N R1ρ data are considered
in detail. Among them are signal amplitude as a function of the difference between
SL and MAS frequencies, “dead time” in the initial part of the relaxation decay
caused by transient spin-dynamic oscillations, measurements under HORROR condition
and proper treatment of the multi-exponential relaxation decays. The multiple
15N R1ρ measurements at different SL fields and temperatures have been conducted
in 1D mode (i.e. without site-specific resolution) for a set of four different
microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin)
to study the overall protein rocking in a crystal. While the amplitude of this
motion varies very significantly, its correlation time for all four sample is
practically the same, 30–50 μs. The amplitude of the rocking motion correlates
with the packing density of a protein crystal. It has been suggested that the
rocking motion is not diffusive but likely a jump-like dynamic process.
article_processing_charge: No
article_type: original
author:
- first_name: Alexey
full_name: Krushelnitsky, Alexey
last_name: Krushelnitsky
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Diana C.
full_name: Rodriguez Camargo, Diana C.
last_name: Rodriguez Camargo
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Kay
full_name: Saalwächter, Kay
last_name: Saalwächter
citation:
ama: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 2018;71(1):53-67. doi:10.1007/s10858-018-0191-4'
apa: 'Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &
Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ
15N MAS NMR experiments: The model case of protein overall-rocking in crystals.
Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4'
chicago: 'Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda,
and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ
15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR. Springer Nature, 2018. https://doi.org/10.1007/s10858-018-0191-4.'
ieee: 'A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter,
“Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals,” Journal of Biomolecular
NMR, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.'
ista: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 71(1), 53–67.'
mla: 'Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance
R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR, vol. 71, no. 1, Springer Nature, 2018, pp.
53–67, doi:10.1007/s10858-018-0191-4.'
short: A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter,
Journal of Biomolecular NMR 71 (2018) 53–67.
date_created: 2020-09-18T10:05:28Z
date_published: 2018-05-30T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '30'
doi: 10.1007/s10858-018-0191-4
extern: '1'
intvolume: ' 71'
issue: '1'
language:
- iso: eng
month: '05'
oa_version: Published Version
page: 53-67
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 71
year: '2018'
...
---
_id: '8442'
abstract:
- lang: eng
text: Membrane proteins perform a host of vital cellular functions. Deciphering
the molecular mechanisms whereby they fulfill these functions requires detailed
biophysical and structural investigations. Detergents have proven pivotal to extract
the protein from its native surroundings. Yet, they provide a milieu that departs
significantly from that of the biological membrane, to the extent that the structure,
the dynamics, and the interactions of membrane proteins in detergents may considerably
vary, as compared to the native environment. Understanding the impact of detergents
on membrane proteins is, therefore, crucial to assess the biological relevance
of results obtained in detergents. Here, we review the strengths and weaknesses
of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR
studies of membrane proteins. While this class of detergents is often successful
for membrane protein solubilization, a growing list of examples points to destabilizing
and denaturing properties, in particular for α-helical membrane proteins. Our
comprehensive analysis stresses the importance of stringent controls when working
with this class of detergents and when analyzing the structure and dynamics of
membrane proteins in alkyl phosphocholine detergents.
article_processing_charge: No
article_type: original
author:
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Jason R.
full_name: Schnell, Jason R.
last_name: Schnell
- first_name: Nicole
full_name: Zitzmann, Nicole
last_name: Zitzmann
- first_name: Eva
full_name: Pebay-Peyroula, Eva
last_name: Pebay-Peyroula
- first_name: Laurent J.
full_name: Catoire, Laurent J.
last_name: Catoire
- first_name: Bruno
full_name: Miroux, Bruno
last_name: Miroux
- first_name: Edmund R. S.
full_name: Kunji, Edmund R. S.
last_name: Kunji
- first_name: Gianluigi
full_name: Veglia, Gianluigi
last_name: Veglia
- first_name: Timothy A.
full_name: Cross, Timothy A.
last_name: Cross
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein
structure in alkyl phosphocholine detergents: A critical assessment of NMR and
biophysical studies. Chemical Reviews. 2018;118(7):3559-3607. doi:10.1021/acs.chemrev.7b00570'
apa: 'Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire,
L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies. Chemical Reviews. American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00570'
chicago: 'Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann,
Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of
Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical
Assessment of NMR and Biophysical Studies.” Chemical Reviews. American
Chemical Society, 2018. https://doi.org/10.1021/acs.chemrev.7b00570.'
ieee: 'C. Chipot et al., “Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society,
pp. 3559–3607, 2018.'
ista: 'Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ,
Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native
membrane protein structure in alkyl phosphocholine detergents: A critical assessment
of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.'
mla: 'Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure
in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical
Studies.” Chemical Reviews, vol. 118, no. 7, American Chemical Society,
2018, pp. 3559–607, doi:10.1021/acs.chemrev.7b00570.'
short: C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire,
B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118
(2018) 3559–3607.
date_created: 2020-09-18T10:05:35Z
date_published: 2018-02-28T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '28'
doi: 10.1021/acs.chemrev.7b00570
extern: '1'
intvolume: ' 118'
issue: '7'
keyword:
- General Chemistry
language:
- iso: eng
month: '02'
oa_version: None
page: 3559-3607
publication: Chemical Reviews
publication_identifier:
issn:
- 0009-2665
- 1520-6890
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Perturbations of native membrane protein structure in alkyl phosphocholine
detergents: A critical assessment of NMR and biophysical studies'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 118
year: '2018'
...
---
_id: '8443'
abstract:
- lang: eng
text: Characterizing the structure of membrane proteins (MPs) generally requires
extraction from their native environment, most commonly with detergents. Yet,
the physicochemical properties of detergent micelles and lipid bilayers differ
markedly and could alter the structural organization of MPs, albeit without general
rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure
determination by NMR, but the physiological relevance of several prominent structures
has been questioned, though indirectly, by other biophysical techniques, e.g.,
functional/thermostability assay (TSA) and molecular dynamics (MD) simulations.
Here, we resolve unambiguously this controversy by probing the functional relevance
of three different mitochondrial carriers (MCs) in DPC at the atomic level, using
an exhaustive set of solution-NMR experiments, complemented by functional/TSA
and MD data. Our results provide atomic-level insight into the structure, substrate
interaction and dynamics of the detergent–membrane protein complexes and demonstrates
cogently that, while high-resolution NMR signals can be obtained for MCs in DPC,
they systematically correspond to nonfunctional states.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Peixiang
full_name: Ma, Peixiang
last_name: Ma
- first_name: Paola
full_name: Lunetti, Paola
last_name: Lunetti
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Lionel
full_name: Imbert, Lionel
last_name: Imbert
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Martin S.
full_name: King, Martin S.
last_name: King
- first_name: Rémy
full_name: Sounier, Rémy
last_name: Sounier
- first_name: Vincenza
full_name: Dolce, Vincenza
last_name: Dolce
- first_name: Edmund R. S.
full_name: Kunji, Edmund R. S.
last_name: Kunji
- first_name: Loredana
full_name: Capobianco, Loredana
last_name: Capobianco
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins:
Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The
Journal of Physical Chemistry Letters. 2018;9(5):933-938. doi:10.1021/acs.jpclett.8b00269'
apa: 'Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L.,
… Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views
of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical
Chemistry Letters. American Chemical Society. https://doi.org/10.1021/acs.jpclett.8b00269'
chicago: 'Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina
Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane
Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.”
The Journal of Physical Chemistry Letters. American Chemical Society, 2018.
https://doi.org/10.1021/acs.jpclett.8b00269.'
ieee: 'V. Kurauskas et al., “How detergent impacts membrane proteins: Atomic-level
views of mitochondrial carriers in dodecylphosphocholine,” The Journal of Physical
Chemistry Letters, vol. 9, no. 5. American Chemical Society, pp. 933–938,
2018.'
ista: 'Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher
B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch
B, Schanda P. 2018. How detergent impacts membrane proteins: Atomic-level views
of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry
Letters. 9(5), 933–938.'
mla: 'Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level
Views of Mitochondrial Carriers in Dodecylphosphocholine.” The Journal of Physical
Chemistry Letters, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38,
doi:10.1021/acs.jpclett.8b00269.'
short: V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher,
M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez,
B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.
date_created: 2020-09-18T10:05:45Z
date_published: 2018-02-03T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '03'
doi: 10.1021/acs.jpclett.8b00269
extern: '1'
intvolume: ' 9'
issue: '5'
keyword:
- General Materials Science
language:
- iso: eng
month: '02'
oa_version: None
page: 933-938
publication: The Journal of Physical Chemistry Letters
publication_identifier:
issn:
- 1948-7185
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'How detergent impacts membrane proteins: Atomic-level views of mitochondrial
carriers in dodecylphosphocholine'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...