---
_id: '9477'
abstract:
- lang: eng
text: Cytosine methylation is a DNA modification with important regulatory functions
in eukaryotes. In flowering plants, sexual reproduction is accompanied by extensive
DNA demethylation, which is required for proper gene expression in the endosperm,
a nutritive extraembryonic seed tissue. Endosperm arises from a fusion of a sperm
cell carried in the pollen and a female central cell. Endosperm DNA demethylation
is observed specifically on the chromosomes inherited from the central cell in
Arabidopsis thaliana, rice, and maize, and requires the DEMETER DNA demethylase
in Arabidopsis. DEMETER is expressed in the central cell before fertilization,
suggesting that endosperm demethylation patterns are inherited from the central
cell. Down-regulation of the MET1 DNA methyltransferase has also been proposed
to contribute to central cell demethylation. However, with the exception of three
maize genes, central cell DNA methylation has not been directly measured, leaving
the origin and mechanism of endosperm demethylation uncertain. Here, we report
genome-wide analysis of DNA methylation in the central cells of Arabidopsis and
rice—species that diverged 150 million years ago—as well as in rice egg cells.
We find that DNA demethylation in both species is initiated in central cells,
which requires DEMETER in Arabidopsis. However, we do not observe a global reduction
of CG methylation that would be indicative of lowered MET1 activity; on the contrary,
CG methylation efficiency is elevated in female gametes compared with nonsexual
tissues. Our results demonstrate that locus-specific, active DNA demethylation
in the central cell is the origin of maternal chromosome hypomethylation in the
endosperm.
article_processing_charge: No
article_type: original
author:
- first_name: Kyunghyuk
full_name: Park, Kyunghyuk
last_name: Park
- first_name: M. Yvonne
full_name: Kim, M. Yvonne
last_name: Kim
- first_name: Martin
full_name: Vickers, Martin
last_name: Vickers
- first_name: Jin-Sup
full_name: Park, Jin-Sup
last_name: Park
- first_name: Youbong
full_name: Hyun, Youbong
last_name: Hyun
- first_name: Takashi
full_name: Okamoto, Takashi
last_name: Okamoto
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Yeonhee
full_name: Choi, Yeonhee
last_name: Choi
- first_name: Stefan
full_name: Scholten, Stefan
last_name: Scholten
citation:
ama: Park K, Kim MY, Vickers M, et al. DNA demethylation is initiated in the central
cells of Arabidopsis and rice. Proceedings of the National Academy of Sciences.
2016;113(52):15138-15143. doi:10.1073/pnas.1619047114
apa: Park, K., Kim, M. Y., Vickers, M., Park, J.-S., Hyun, Y., Okamoto, T., … Scholten,
S. (2016). DNA demethylation is initiated in the central cells of Arabidopsis
and rice. Proceedings of the National Academy of Sciences. National Academy
of Sciences. https://doi.org/10.1073/pnas.1619047114
chicago: Park, Kyunghyuk, M. Yvonne Kim, Martin Vickers, Jin-Sup Park, Youbong Hyun,
Takashi Okamoto, Daniel Zilberman, et al. “DNA Demethylation Is Initiated in the
Central Cells of Arabidopsis and Rice.” Proceedings of the National Academy
of Sciences. National Academy of Sciences, 2016. https://doi.org/10.1073/pnas.1619047114.
ieee: K. Park et al., “DNA demethylation is initiated in the central cells
of Arabidopsis and rice,” Proceedings of the National Academy of Sciences,
vol. 113, no. 52. National Academy of Sciences, pp. 15138–15143, 2016.
ista: Park K, Kim MY, Vickers M, Park J-S, Hyun Y, Okamoto T, Zilberman D, Fischer
RL, Feng X, Choi Y, Scholten S. 2016. DNA demethylation is initiated in the central
cells of Arabidopsis and rice. Proceedings of the National Academy of Sciences.
113(52), 15138–15143.
mla: Park, Kyunghyuk, et al. “DNA Demethylation Is Initiated in the Central Cells
of Arabidopsis and Rice.” Proceedings of the National Academy of Sciences,
vol. 113, no. 52, National Academy of Sciences, 2016, pp. 15138–43, doi:10.1073/pnas.1619047114.
short: K. Park, M.Y. Kim, M. Vickers, J.-S. Park, Y. Hyun, T. Okamoto, D. Zilberman,
R.L. Fischer, X. Feng, Y. Choi, S. Scholten, Proceedings of the National Academy
of Sciences 113 (2016) 15138–15143.
date_created: 2021-06-07T07:10:59Z
date_published: 2016-12-27T00:00:00Z
date_updated: 2023-05-08T11:00:07Z
day: '27'
department:
- _id: DaZi
- _id: XiFe
doi: 10.1073/pnas.1619047114
extern: '1'
external_id:
pmid:
- '27956642'
intvolume: ' 113'
issue: '52'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1619047114
month: '12'
oa: 1
oa_version: Published Version
page: 15138-15143
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: DNA demethylation is initiated in the central cells of Arabidopsis and rice
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2016'
...
---
_id: '8021'
abstract:
- lang: eng
text: 'Most excitatory inputs in the mammalian brain are made on dendritic spines,
rather than on dendritic shafts. Spines compartmentalize calcium, and this biochemical
isolation can underlie input-specific synaptic plasticity, providing a raison
d''etre for spines. However, recent results indicate that the spine can experience
a membrane potential different from that in the parent dendrite, as though the
spine neck electrically isolated the spine. Here we use two-photon calcium imaging
of mouse neocortical pyramidal neurons to analyze the correlation between the
morphologies of spines activated under minimal synaptic stimulation and the excitatory
postsynaptic potentials they generate. We find that excitatory postsynaptic potential
amplitudes are inversely correlated with spine neck lengths. Furthermore, a spike
timing-dependent plasticity protocol, in which two-photon glutamate uncaging over
a spine is paired with postsynaptic spikes, produces rapid shrinkage of the spine
neck and concomitant increases in the amplitude of the evoked spine potentials.
Using numerical simulations, we explore the parameter regimes for the spine neck
resistance and synaptic conductance changes necessary to explain our observations.
Our data, directly correlating synaptic and morphological plasticity, imply that
long-necked spines have small or negligible somatic voltage contributions, but
that, upon synaptic stimulation paired with postsynaptic activity, they can shorten
their necks and increase synaptic efficacy, thus changing the input/output gain
of pyramidal neurons. '
article_processing_charge: No
article_type: original
author:
- first_name: R.
full_name: Araya, R.
last_name: Araya
- first_name: Tim P
full_name: Vogels, Tim P
id: CB6FF8D2-008F-11EA-8E08-2637E6697425
last_name: Vogels
orcid: 0000-0003-3295-6181
- first_name: R.
full_name: Yuste, R.
last_name: Yuste
citation:
ama: Araya R, Vogels TP, Yuste R. Activity-dependent dendritic spine neck changes
are correlated with synaptic strength. Proceedings of the National Academy
of Sciences. 2014;111(28):E2895-E2904. doi:10.1073/pnas.1321869111
apa: Araya, R., Vogels, T. P., & Yuste, R. (2014). Activity-dependent dendritic
spine neck changes are correlated with synaptic strength. Proceedings of the
National Academy of Sciences. Proceedings of the National Academy of Sciences.
https://doi.org/10.1073/pnas.1321869111
chicago: Araya, R., Tim P Vogels, and R. Yuste. “Activity-Dependent Dendritic Spine
Neck Changes Are Correlated with Synaptic Strength.” Proceedings of the National
Academy of Sciences. Proceedings of the National Academy of Sciences, 2014.
https://doi.org/10.1073/pnas.1321869111.
ieee: R. Araya, T. P. Vogels, and R. Yuste, “Activity-dependent dendritic spine
neck changes are correlated with synaptic strength,” Proceedings of the National
Academy of Sciences, vol. 111, no. 28. Proceedings of the National Academy
of Sciences, pp. E2895–E2904, 2014.
ista: Araya R, Vogels TP, Yuste R. 2014. Activity-dependent dendritic spine neck
changes are correlated with synaptic strength. Proceedings of the National Academy
of Sciences. 111(28), E2895–E2904.
mla: Araya, R., et al. “Activity-Dependent Dendritic Spine Neck Changes Are Correlated
with Synaptic Strength.” Proceedings of the National Academy of Sciences,
vol. 111, no. 28, Proceedings of the National Academy of Sciences, 2014, pp. E2895–904,
doi:10.1073/pnas.1321869111.
short: R. Araya, T.P. Vogels, R. Yuste, Proceedings of the National Academy of Sciences
111 (2014) E2895–E2904.
date_created: 2020-06-25T13:06:24Z
date_published: 2014-07-15T00:00:00Z
date_updated: 2021-01-12T08:16:34Z
day: '15'
doi: 10.1073/pnas.1321869111
extern: '1'
external_id:
pmid:
- '24982196'
intvolume: ' 111'
issue: '28'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4104910/
month: '07'
oa: 1
oa_version: Published Version
page: E2895-E2904
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
status: public
title: Activity-dependent dendritic spine neck changes are correlated with synaptic
strength
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 111
year: '2014'
...
---
_id: '10382'
abstract:
- lang: eng
text: 'Protein oligomers have been implicated as toxic agents in a wide range of
amyloid-related diseases. However, it has remained unsolved whether the oligomers
are a necessary step in the formation of amyloid fibrils or just a dangerous byproduct.
Analogously, it has not been resolved if the amyloid nucleation process is a classical
one-step nucleation process or a two-step process involving prenucleation clusters.
We use coarse-grained computer simulations to study the effect of nonspecific
attractions between peptides on the primary nucleation process underlying amyloid
fibrillization. We find that, for peptides that do not attract, the classical
one-step nucleation mechanism is possible but only at nonphysiologically high
peptide concentrations. At low peptide concentrations, which mimic the physiologically
relevant regime, attractive interpeptide interactions are essential for fibril
formation. Nucleation then inevitably takes place through a two-step mechanism
involving prefibrillar oligomers. We show that oligomers not only help peptides
meet each other but also, create an environment that facilitates the conversion
of monomers into the β-sheet–rich form characteristic of fibrils. Nucleation typically
does not proceed through the most prevalent oligomers but through an oligomer
size that is only observed in rare fluctuations, which is why such aggregates
might be hard to capture experimentally. Finally, we find that the nucleation
of amyloid fibrils cannot be described by classical nucleation theory: in the
two-step mechanism, the critical nucleus size increases with increases in both
concentration and interpeptide interactions, which is in direct contrast with
predictions from classical nucleation theory.'
acknowledgement: We thank Michele Vendruscolo, Iskra Staneva, and William M. Jacobs,
for helpful discussions. A.Š. acknowledges support from the Human Frontier Science
Program and Emmanuel College. Y.C.C. and D.F. are supported by Engineering and Physical
Sciences Research Council Programme Grant EP/I001352/1. T.P.J.K. acknowledges the
Frances and Augustus Newman Foundation, the European Research Council, and the Biotechnology
and Biological Sciences Research Council. D.F. acknowledges European Research Council
Advanced Grant 227758.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Yassmine C.
full_name: Chebaro, Yassmine C.
last_name: Chebaro
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
citation:
ama: Šarić A, Chebaro YC, Knowles TPJ, Frenkel D. Crucial role of nonspecific interactions
in amyloid nucleation. Proceedings of the National Academy of Sciences.
2014;111(50):17869-17874. doi:10.1073/pnas.1410159111
apa: Šarić, A., Chebaro, Y. C., Knowles, T. P. J., & Frenkel, D. (2014). Crucial
role of nonspecific interactions in amyloid nucleation. Proceedings of the
National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.1410159111
chicago: Šarić, Anđela, Yassmine C. Chebaro, Tuomas P. J. Knowles, and Daan Frenkel.
“Crucial Role of Nonspecific Interactions in Amyloid Nucleation.” Proceedings
of the National Academy of Sciences. National Academy of Sciences, 2014. https://doi.org/10.1073/pnas.1410159111.
ieee: A. Šarić, Y. C. Chebaro, T. P. J. Knowles, and D. Frenkel, “Crucial role of
nonspecific interactions in amyloid nucleation,” Proceedings of the National
Academy of Sciences, vol. 111, no. 50. National Academy of Sciences, pp. 17869–17874,
2014.
ista: Šarić A, Chebaro YC, Knowles TPJ, Frenkel D. 2014. Crucial role of nonspecific
interactions in amyloid nucleation. Proceedings of the National Academy of Sciences.
111(50), 17869–17874.
mla: Šarić, Anđela, et al. “Crucial Role of Nonspecific Interactions in Amyloid
Nucleation.” Proceedings of the National Academy of Sciences, vol. 111,
no. 50, National Academy of Sciences, 2014, pp. 17869–74, doi:10.1073/pnas.1410159111.
short: A. Šarić, Y.C. Chebaro, T.P.J. Knowles, D. Frenkel, Proceedings of the National
Academy of Sciences 111 (2014) 17869–17874.
date_created: 2021-11-29T13:09:53Z
date_published: 2014-12-01T00:00:00Z
date_updated: 2021-11-29T13:29:05Z
day: '01'
doi: 10.1073/pnas.1410159111
extern: '1'
external_id:
arxiv:
- '1412.0897'
pmid:
- '25453085'
intvolume: ' 111'
issue: '50'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.pnas.org/content/111/50/17869
month: '12'
oa: 1
oa_version: Published Version
page: 17869-17874
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Crucial role of nonspecific interactions in amyloid nucleation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 111
year: '2014'
...
---
_id: '9479'
abstract:
- lang: eng
text: Centromeres mediate chromosome segregation and are defined by the centromere-specific
histone H3 variant (CenH3)/centromere protein A (CENP-A). Removal of CenH3 from
centromeres is a general property of terminally differentiated cells, and the
persistence of CenH3 increases the risk of diseases such as cancer. However, active
mechanisms of centromere disassembly are unknown. Nondividing Arabidopsis pollen
vegetative cells, which transport engulfed sperm by extended tip growth, undergo
loss of CenH3; centromeric heterochromatin decondensation; and bulk activation
of silent rRNA genes, accompanied by their translocation into the nucleolus. Here,
we show that these processes are blocked by mutations in the evolutionarily conserved
AAA-ATPase molecular chaperone, CDC48A, homologous to yeast Cdc48 and human p97
proteins, both of which are implicated in ubiquitin/small ubiquitin-like modifier
(SUMO)-targeted protein degradation. We demonstrate that CDC48A physically associates
with its heterodimeric cofactor UFD1-NPL4, known to bind ubiquitin and SUMO, as
well as with SUMO1-modified CenH3 and mutations in NPL4 phenocopy cdc48a mutations.
In WT vegetative cell nuclei, genetically unlinked ribosomal DNA (rDNA) loci are
uniquely clustered together within the nucleolus and all major rRNA gene variants,
including those rDNA variants silenced in leaves, are transcribed. In cdc48a mutant
vegetative cell nuclei, however, these rDNA loci frequently colocalized with condensed
centromeric heterochromatin at the external periphery of the nucleolus. Our results
indicate that the CDC48ANPL4 complex actively removes sumoylated CenH3 from centromeres
and disrupts centromeric heterochromatin to release bulk rRNA genes into the nucleolus
for ribosome production, which fuels single nucleus-driven pollen tube growth
and is essential for plant reproduction.
article_processing_charge: No
article_type: original
author:
- first_name: Zsuzsanna
full_name: Mérai, Zsuzsanna
last_name: Mérai
- first_name: Nina
full_name: Chumak, Nina
last_name: Chumak
- first_name: Marcelina
full_name: García-Aguilar, Marcelina
last_name: García-Aguilar
- first_name: Tzung-Fu
full_name: Hsieh, Tzung-Fu
last_name: Hsieh
- first_name: Toshiro
full_name: Nishimura, Toshiro
last_name: Nishimura
- first_name: Vera K.
full_name: Schoft, Vera K.
last_name: Schoft
- first_name: János
full_name: Bindics, János
last_name: Bindics
- first_name: Lucyna
full_name: Ślusarz, Lucyna
last_name: Ślusarz
- first_name: Stéphanie
full_name: Arnoux, Stéphanie
last_name: Arnoux
- first_name: Susanne
full_name: Opravil, Susanne
last_name: Opravil
- first_name: Karl
full_name: Mechtler, Karl
last_name: Mechtler
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
- first_name: Hisashi
full_name: Tamaru, Hisashi
last_name: Tamaru
citation:
ama: Mérai Z, Chumak N, García-Aguilar M, et al. The AAA-ATPase molecular chaperone
Cdc48/p97 disassembles sumoylated centromeres, decondenses heterochromatin, and
activates ribosomal RNA genes. Proceedings of the National Academy of Sciences.
2014;111(45):16166-16171. doi:10.1073/pnas.1418564111
apa: Mérai, Z., Chumak, N., García-Aguilar, M., Hsieh, T.-F., Nishimura, T., Schoft,
V. K., … Tamaru, H. (2014). The AAA-ATPase molecular chaperone Cdc48/p97 disassembles
sumoylated centromeres, decondenses heterochromatin, and activates ribosomal RNA
genes. Proceedings of the National Academy of Sciences. National Academy
of Sciences. https://doi.org/10.1073/pnas.1418564111
chicago: Mérai, Zsuzsanna, Nina Chumak, Marcelina García-Aguilar, Tzung-Fu Hsieh,
Toshiro Nishimura, Vera K. Schoft, János Bindics, et al. “The AAA-ATPase Molecular
Chaperone Cdc48/P97 Disassembles Sumoylated Centromeres, Decondenses Heterochromatin,
and Activates Ribosomal RNA Genes.” Proceedings of the National Academy of
Sciences. National Academy of Sciences, 2014. https://doi.org/10.1073/pnas.1418564111.
ieee: Z. Mérai et al., “The AAA-ATPase molecular chaperone Cdc48/p97 disassembles
sumoylated centromeres, decondenses heterochromatin, and activates ribosomal RNA
genes,” Proceedings of the National Academy of Sciences, vol. 111, no.
45. National Academy of Sciences, pp. 16166–16171, 2014.
ista: Mérai Z, Chumak N, García-Aguilar M, Hsieh T-F, Nishimura T, Schoft VK, Bindics
J, Ślusarz L, Arnoux S, Opravil S, Mechtler K, Zilberman D, Fischer RL, Tamaru
H. 2014. The AAA-ATPase molecular chaperone Cdc48/p97 disassembles sumoylated
centromeres, decondenses heterochromatin, and activates ribosomal RNA genes. Proceedings
of the National Academy of Sciences. 111(45), 16166–16171.
mla: Mérai, Zsuzsanna, et al. “The AAA-ATPase Molecular Chaperone Cdc48/P97 Disassembles
Sumoylated Centromeres, Decondenses Heterochromatin, and Activates Ribosomal RNA
Genes.” Proceedings of the National Academy of Sciences, vol. 111, no.
45, National Academy of Sciences, 2014, pp. 16166–71, doi:10.1073/pnas.1418564111.
short: Z. Mérai, N. Chumak, M. García-Aguilar, T.-F. Hsieh, T. Nishimura, V.K. Schoft,
J. Bindics, L. Ślusarz, S. Arnoux, S. Opravil, K. Mechtler, D. Zilberman, R.L.
Fischer, H. Tamaru, Proceedings of the National Academy of Sciences 111 (2014)
16166–16171.
date_created: 2021-06-07T07:23:43Z
date_published: 2014-11-11T00:00:00Z
date_updated: 2021-12-14T08:23:26Z
day: '11'
department:
- _id: DaZi
doi: 10.1073/pnas.1418564111
extern: '1'
external_id:
pmid:
- '25344531'
intvolume: ' 111'
issue: '45'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1418564111
month: '11'
oa: 1
oa_version: Published Version
page: 16166-16171
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: The AAA-ATPase molecular chaperone Cdc48/p97 disassembles sumoylated centromeres,
decondenses heterochromatin, and activates ribosomal RNA genes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 111
year: '2014'
...
---
_id: '9481'
abstract:
- lang: eng
text: Arabidopsis thaliana endosperm, a transient tissue that nourishes the embryo,
exhibits extensive localized DNA demethylation on maternally inherited chromosomes.
Demethylation mediates parent-of-origin–specific (imprinted) gene expression but
is apparently unnecessary for the extensive accumulation of maternally biased
small RNA (sRNA) molecules detected in seeds. Endosperm DNA in the distantly related
monocots rice and maize is likewise locally hypomethylated, but whether this hypomethylation
is generally parent-of-origin specific is unknown. Imprinted expression of sRNA
also remains uninvestigated in monocot seeds. Here, we report high-coverage sequencing
of the Kitaake rice cultivar that enabled us to show that localized hypomethylation
in rice endosperm occurs solely on the maternal genome, preferring regions of
high DNA accessibility. Maternally expressed imprinted genes are enriched for
hypomethylation at putative promoter regions and transcriptional termini and paternally
expressed genes at promoters and gene bodies, mirroring our recent results in
A. thaliana. However, unlike in A. thaliana, rice endosperm sRNA populations are
dominated by specific strong sRNA-producing loci, and imprinted 24-nt sRNAs are
expressed from both parental genomes and correlate with hypomethylation. Overlaps
between imprinted sRNA loci and imprinted genes expressed from opposite alleles
suggest that sRNAs may regulate genomic imprinting. Whereas sRNAs in seedling
tissues primarily originate from small class II (cut-and-paste) transposable elements,
those in endosperm are more uniformly derived, including sequences from other
transposon classes, as well as genic and intergenic regions. Our data indicate
that the endosperm exhibits a unique pattern of sRNA expression and suggest that
localized hypomethylation of maternal endosperm DNA is conserved in flowering
plants.
article_processing_charge: No
article_type: original
author:
- first_name: Jessica A.
full_name: Rodrigues, Jessica A.
last_name: Rodrigues
- first_name: Randy
full_name: Ruan, Randy
last_name: Ruan
- first_name: Toshiro
full_name: Nishimura, Toshiro
last_name: Nishimura
- first_name: Manoj K.
full_name: Sharma, Manoj K.
last_name: Sharma
- first_name: Rita
full_name: Sharma, Rita
last_name: Sharma
- first_name: Pamela C
full_name: Ronald, Pamela C
last_name: Ronald
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Rodrigues JA, Ruan R, Nishimura T, et al. Imprinted expression of genes and
small RNA is associated with localized hypomethylation of the maternal genome
in rice endosperm. Proceedings of the National Academy of Sciences. 2013;110(19):7934-7939.
doi:10.1073/pnas.1306164110
apa: Rodrigues, J. A., Ruan, R., Nishimura, T., Sharma, M. K., Sharma, R., Ronald,
P. C., … Zilberman, D. (2013). Imprinted expression of genes and small RNA is
associated with localized hypomethylation of the maternal genome in rice endosperm.
Proceedings of the National Academy of Sciences. National Academy of Sciences.
https://doi.org/10.1073/pnas.1306164110
chicago: Rodrigues, Jessica A., Randy Ruan, Toshiro Nishimura, Manoj K. Sharma,
Rita Sharma, Pamela C Ronald, Robert L. Fischer, and Daniel Zilberman. “Imprinted
Expression of Genes and Small RNA Is Associated with Localized Hypomethylation
of the Maternal Genome in Rice Endosperm.” Proceedings of the National Academy
of Sciences. National Academy of Sciences, 2013. https://doi.org/10.1073/pnas.1306164110.
ieee: J. A. Rodrigues et al., “Imprinted expression of genes and small RNA
is associated with localized hypomethylation of the maternal genome in rice endosperm,”
Proceedings of the National Academy of Sciences, vol. 110, no. 19. National
Academy of Sciences, pp. 7934–7939, 2013.
ista: Rodrigues JA, Ruan R, Nishimura T, Sharma MK, Sharma R, Ronald PC, Fischer
RL, Zilberman D. 2013. Imprinted expression of genes and small RNA is associated
with localized hypomethylation of the maternal genome in rice endosperm. Proceedings
of the National Academy of Sciences. 110(19), 7934–7939.
mla: Rodrigues, Jessica A., et al. “Imprinted Expression of Genes and Small RNA
Is Associated with Localized Hypomethylation of the Maternal Genome in Rice Endosperm.”
Proceedings of the National Academy of Sciences, vol. 110, no. 19, National
Academy of Sciences, 2013, pp. 7934–39, doi:10.1073/pnas.1306164110.
short: J.A. Rodrigues, R. Ruan, T. Nishimura, M.K. Sharma, R. Sharma, P.C. Ronald,
R.L. Fischer, D. Zilberman, Proceedings of the National Academy of Sciences 110
(2013) 7934–7939.
date_created: 2021-06-07T07:31:02Z
date_published: 2013-05-07T00:00:00Z
date_updated: 2021-12-14T08:26:44Z
day: '07'
department:
- _id: DaZi
doi: 10.1073/pnas.1306164110
extern: '1'
external_id:
pmid:
- '23613580'
intvolume: ' 110'
issue: '19'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1306164110
month: '05'
oa: 1
oa_version: Published Version
page: 7934-7939
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Imprinted expression of genes and small RNA is associated with localized hypomethylation
of the maternal genome in rice endosperm
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 110
year: '2013'
...
---
_id: '14305'
abstract:
- lang: eng
text: Understanding the mechanism of protein folding requires a detailed knowledge
of the structural properties of the barriers separating unfolded from native conformations.
The S-peptide from ribonuclease S forms its α-helical structure only upon binding
to the folded S-protein. We characterized the transition state for this binding-induced
folding reaction at high resolution by determining the effect of site-specific
backbone thioxylation and side-chain modifications on the kinetics and thermodynamics
of the reaction, which allows us to monitor formation of backbone hydrogen bonds
and side-chain interactions in the transition state. The experiments reveal that
α-helical structure in the S-peptide is absent in the transition state of binding.
Recognition between the unfolded S-peptide and the S-protein is mediated by loosely
packed hydrophobic side-chain interactions in two well defined regions on the
S-peptide. Close packing and helix formation occurs rapidly after binding. Introducing
hydrophobic residues at positions outside the recognition region can drastically
slow down association.
article_processing_charge: No
article_type: original
author:
- first_name: Annett
full_name: Bachmann, Annett
last_name: Bachmann
- first_name: Dirk
full_name: Wildemann, Dirk
last_name: Wildemann
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Gunter
full_name: Fischer, Gunter
last_name: Fischer
- first_name: Thomas
full_name: Kiefhaber, Thomas
last_name: Kiefhaber
citation:
ama: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. Mapping backbone
and side-chain interactions in the transition state of a coupled protein folding
and binding reaction. PNAS. 2011;108(10):3952-3957. doi:10.1073/pnas.1012668108
apa: Bachmann, A., Wildemann, D., Praetorius, F. M., Fischer, G., & Kiefhaber,
T. (2011). Mapping backbone and side-chain interactions in the transition state
of a coupled protein folding and binding reaction. PNAS. Proceedings of
the National Academy of Sciences. https://doi.org/10.1073/pnas.1012668108
chicago: Bachmann, Annett, Dirk Wildemann, Florian M Praetorius, Gunter Fischer,
and Thomas Kiefhaber. “Mapping Backbone and Side-Chain Interactions in the Transition
State of a Coupled Protein Folding and Binding Reaction.” PNAS. Proceedings
of the National Academy of Sciences, 2011. https://doi.org/10.1073/pnas.1012668108.
ieee: A. Bachmann, D. Wildemann, F. M. Praetorius, G. Fischer, and T. Kiefhaber,
“Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction,” PNAS, vol. 108, no. 10. Proceedings
of the National Academy of Sciences, pp. 3952–3957, 2011.
ista: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. 2011. Mapping
backbone and side-chain interactions in the transition state of a coupled protein
folding and binding reaction. PNAS. 108(10), 3952–3957.
mla: Bachmann, Annett, et al. “Mapping Backbone and Side-Chain Interactions in the
Transition State of a Coupled Protein Folding and Binding Reaction.” PNAS,
vol. 108, no. 10, Proceedings of the National Academy of Sciences, 2011, pp. 3952–57,
doi:10.1073/pnas.1012668108.
short: A. Bachmann, D. Wildemann, F.M. Praetorius, G. Fischer, T. Kiefhaber, PNAS
108 (2011) 3952–3957.
date_created: 2023-09-06T12:54:36Z
date_published: 2011-01-12T00:00:00Z
date_updated: 2023-11-07T11:50:29Z
day: '12'
doi: 10.1073/pnas.1012668108
extern: '1'
external_id:
pmid:
- '21325613'
intvolume: ' 108'
issue: '10'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1012668108
month: '01'
oa: 1
oa_version: Published Version
page: 3952-3957
pmid: 1
publication: PNAS
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 108
year: '2011'
...
---
_id: '9483'
abstract:
- lang: eng
text: Imprinted genes are expressed primarily or exclusively from either the maternal
or paternal allele, a phenomenon that occurs in flowering plants and mammals.
Flowering plant imprinted gene expression has been described primarily in endosperm,
a terminal nutritive tissue consumed by the embryo during seed development or
after germination. Imprinted expression in Arabidopsis thaliana endosperm is orchestrated
by differences in cytosine DNA methylation between the paternal and maternal genomes
as well as by Polycomb group proteins. Currently, only 11 imprinted A. thaliana
genes are known. Here, we use extensive sequencing of cDNA libraries to identify
9 paternally expressed and 34 maternally expressed imprinted genes in A. thaliana
endosperm that are regulated by the DNA-demethylating glycosylase DEMETER, the
DNA methyltransferase MET1, and/or the core Polycomb group protein FIE. These
genes encode transcription factors, proteins involved in hormone signaling, components
of the ubiquitin protein degradation pathway, regulators of histone and DNA methylation,
and small RNA pathway proteins. We also identify maternally expressed genes that
may be regulated by unknown mechanisms or deposited from maternal tissues. We
did not detect any imprinted genes in the embryo. Our results show that imprinted
gene expression is an extensive mechanistically complex phenomenon that likely
affects multiple aspects of seed development.
article_processing_charge: No
article_type: original
author:
- first_name: Tzung-Fu
full_name: Hsieh, Tzung-Fu
last_name: Hsieh
- first_name: Juhyun
full_name: Shin, Juhyun
last_name: Shin
- first_name: Rie
full_name: Uzawa, Rie
last_name: Uzawa
- first_name: Pedro
full_name: Silva, Pedro
last_name: Silva
- first_name: Stephanie
full_name: Cohen, Stephanie
last_name: Cohen
- first_name: Matthew J.
full_name: Bauer, Matthew J.
last_name: Bauer
- first_name: Meryl
full_name: Hashimoto, Meryl
last_name: Hashimoto
- first_name: Ryan C.
full_name: Kirkbride, Ryan C.
last_name: Kirkbride
- first_name: John J.
full_name: Harada, John J.
last_name: Harada
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
citation:
ama: Hsieh T-F, Shin J, Uzawa R, et al. Regulation of imprinted gene expression
in Arabidopsis endosperm. Proceedings of the National Academy of Sciences.
2011;108(5):1755-1762. doi:10.1073/pnas.1019273108
apa: Hsieh, T.-F., Shin, J., Uzawa, R., Silva, P., Cohen, S., Bauer, M. J., … Fischer,
R. L. (2011). Regulation of imprinted gene expression in Arabidopsis endosperm.
Proceedings of the National Academy of Sciences. National Academy of Sciences.
https://doi.org/10.1073/pnas.1019273108
chicago: Hsieh, Tzung-Fu, Juhyun Shin, Rie Uzawa, Pedro Silva, Stephanie Cohen,
Matthew J. Bauer, Meryl Hashimoto, et al. “Regulation of Imprinted Gene Expression
in Arabidopsis Endosperm.” Proceedings of the National Academy of Sciences.
National Academy of Sciences, 2011. https://doi.org/10.1073/pnas.1019273108.
ieee: T.-F. Hsieh et al., “Regulation of imprinted gene expression in Arabidopsis
endosperm,” Proceedings of the National Academy of Sciences, vol. 108,
no. 5. National Academy of Sciences, pp. 1755–1762, 2011.
ista: Hsieh T-F, Shin J, Uzawa R, Silva P, Cohen S, Bauer MJ, Hashimoto M, Kirkbride
RC, Harada JJ, Zilberman D, Fischer RL. 2011. Regulation of imprinted gene expression
in Arabidopsis endosperm. Proceedings of the National Academy of Sciences. 108(5),
1755–1762.
mla: Hsieh, Tzung-Fu, et al. “Regulation of Imprinted Gene Expression in Arabidopsis
Endosperm.” Proceedings of the National Academy of Sciences, vol. 108,
no. 5, National Academy of Sciences, 2011, pp. 1755–62, doi:10.1073/pnas.1019273108.
short: T.-F. Hsieh, J. Shin, R. Uzawa, P. Silva, S. Cohen, M.J. Bauer, M. Hashimoto,
R.C. Kirkbride, J.J. Harada, D. Zilberman, R.L. Fischer, Proceedings of the National
Academy of Sciences 108 (2011) 1755–1762.
date_created: 2021-06-07T07:40:38Z
date_published: 2011-02-01T00:00:00Z
date_updated: 2021-12-14T08:33:49Z
day: '01'
department:
- _id: DaZi
doi: 10.1073/pnas.1019273108
extern: '1'
external_id:
pmid:
- '21257907'
intvolume: ' 108'
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1019273108
month: '02'
oa: 1
oa_version: Published Version
page: 1755-1762
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Regulation of imprinted gene expression in Arabidopsis endosperm
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 108
year: '2011'
...
---
_id: '9485'
abstract:
- lang: eng
text: 'Cytosine methylation silences transposable elements in plants, vertebrates,
and fungi but also regulates gene expression. Plant methylation is catalyzed by
three families of enzymes, each with a preferred sequence context: CG, CHG (H
= A, C, or T), and CHH, with CHH methylation targeted by the RNAi pathway. Arabidopsis
thaliana endosperm, a placenta-like tissue that nourishes the embryo, is globally
hypomethylated in the CG context while retaining high non-CG methylation. Global
methylation dynamics in seeds of cereal crops that provide the bulk of human nutrition
remain unknown. Here, we show that rice endosperm DNA is hypomethylated in all
sequence contexts. Non-CG methylation is reduced evenly across the genome, whereas
CG hypomethylation is localized. CHH methylation of small transposable elements
is increased in embryos, suggesting that endosperm demethylation enhances transposon
silencing. Genes preferentially expressed in endosperm, including those coding
for major storage proteins and starch synthesizing enzymes, are frequently hypomethylated
in endosperm, indicating that DNA methylation is a crucial regulator of rice endosperm
biogenesis. Our data show that genome-wide reshaping of seed DNA methylation is
conserved among angiosperms and has a profound effect on gene expression in cereal
crops.'
article_processing_charge: No
article_type: original
author:
- first_name: Assaf
full_name: Zemach, Assaf
last_name: Zemach
- first_name: M. Yvonne
full_name: Kim, M. Yvonne
last_name: Kim
- first_name: Pedro
full_name: Silva, Pedro
last_name: Silva
- first_name: Jessica A.
full_name: Rodrigues, Jessica A.
last_name: Rodrigues
- first_name: Bradley
full_name: Dotson, Bradley
last_name: Dotson
- first_name: Matthew D.
full_name: Brooks, Matthew D.
last_name: Brooks
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Zemach A, Kim MY, Silva P, et al. Local DNA hypomethylation activates genes
in rice endosperm. Proceedings of the National Academy of Sciences. 2010;107(43):18729-18734.
doi:10.1073/pnas.1009695107
apa: Zemach, A., Kim, M. Y., Silva, P., Rodrigues, J. A., Dotson, B., Brooks, M.
D., & Zilberman, D. (2010). Local DNA hypomethylation activates genes in rice
endosperm. Proceedings of the National Academy of Sciences. National Academy
of Sciences. https://doi.org/10.1073/pnas.1009695107
chicago: Zemach, Assaf, M. Yvonne Kim, Pedro Silva, Jessica A. Rodrigues, Bradley
Dotson, Matthew D. Brooks, and Daniel Zilberman. “Local DNA Hypomethylation Activates
Genes in Rice Endosperm.” Proceedings of the National Academy of Sciences.
National Academy of Sciences, 2010. https://doi.org/10.1073/pnas.1009695107.
ieee: A. Zemach et al., “Local DNA hypomethylation activates genes in rice
endosperm,” Proceedings of the National Academy of Sciences, vol. 107,
no. 43. National Academy of Sciences, pp. 18729–18734, 2010.
ista: Zemach A, Kim MY, Silva P, Rodrigues JA, Dotson B, Brooks MD, Zilberman D.
2010. Local DNA hypomethylation activates genes in rice endosperm. Proceedings
of the National Academy of Sciences. 107(43), 18729–18734.
mla: Zemach, Assaf, et al. “Local DNA Hypomethylation Activates Genes in Rice Endosperm.”
Proceedings of the National Academy of Sciences, vol. 107, no. 43, National
Academy of Sciences, 2010, pp. 18729–34, doi:10.1073/pnas.1009695107.
short: A. Zemach, M.Y. Kim, P. Silva, J.A. Rodrigues, B. Dotson, M.D. Brooks, D.
Zilberman, Proceedings of the National Academy of Sciences 107 (2010) 18729–18734.
date_created: 2021-06-07T09:31:01Z
date_published: 2010-10-26T00:00:00Z
date_updated: 2021-12-14T08:40:02Z
day: '26'
department:
- _id: DaZi
doi: 10.1073/pnas.1009695107
extern: '1'
external_id:
pmid:
- '20937895'
intvolume: ' 107'
issue: '43'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1009695107
month: '10'
oa: 1
oa_version: Published Version
page: 18729-18734
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Local DNA hypomethylation activates genes in rice endosperm
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 107
year: '2010'
...
---
_id: '8483'
abstract:
- lang: eng
text: Atom-resolved real-time studies of kinetic processes in proteins have been
hampered in the past by the lack of experimental techniques that yield sufficient
temporal and atomic resolution. Here we present band-selective optimized flip-angle
short transient (SOFAST) real-time 2D NMR spectroscopy, a method that allows simultaneous
observation of reaction kinetics for a large number of nuclear sites along the
polypeptide chain of a protein with an unprecedented time resolution of a few
seconds. SOFAST real-time 2D NMR spectroscopy combines fast NMR data acquisition
techniques with rapid sample mixing inside the NMR magnet to initiate the kinetic
event. We demonstrate the use of SOFAST real-time 2D NMR to monitor the conformational
transition of α-lactalbumin from a molten globular to the native state for a large
number of amide sites along the polypeptide chain. The kinetic behavior observed
for the disappearance of the molten globule and the appearance of the native state
is monoexponential and uniform along the polypeptide chain. This observation confirms
previous findings that a single transition state ensemble controls folding of
α-lactalbumin from the molten globule to the native state. In a second application,
the spontaneous unfolding of native ubiquitin under nondenaturing conditions is
characterized by amide hydrogen exchange rate constants measured at high pH by
using SOFAST real-time 2D NMR. Our data reveal that ubiquitin unfolds in a gradual
manner with distinct unfolding regimes.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: V.
full_name: Forge, V.
last_name: Forge
- first_name: B.
full_name: Brutscher, B.
last_name: Brutscher
citation:
ama: Schanda P, Forge V, Brutscher B. Protein folding and unfolding studied at atomic
resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National
Academy of Sciences. 2007;104(27):11257-11262. doi:10.1073/pnas.0702069104
apa: Schanda, P., Forge, V., & Brutscher, B. (2007). Protein folding and unfolding
studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings
of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.0702069104
chicago: Schanda, Paul, V. Forge, and B. Brutscher. “Protein Folding and Unfolding
Studied at Atomic Resolution by Fast Two-Dimensional NMR Spectroscopy.” Proceedings
of the National Academy of Sciences. National Academy of Sciences, 2007. https://doi.org/10.1073/pnas.0702069104.
ieee: P. Schanda, V. Forge, and B. Brutscher, “Protein folding and unfolding studied
at atomic resolution by fast two-dimensional NMR spectroscopy,” Proceedings
of the National Academy of Sciences, vol. 104, no. 27. National Academy of
Sciences, pp. 11257–11262, 2007.
ista: Schanda P, Forge V, Brutscher B. 2007. Protein folding and unfolding studied
at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of
the National Academy of Sciences. 104(27), 11257–11262.
mla: Schanda, Paul, et al. “Protein Folding and Unfolding Studied at Atomic Resolution
by Fast Two-Dimensional NMR Spectroscopy.” Proceedings of the National Academy
of Sciences, vol. 104, no. 27, National Academy of Sciences, 2007, pp. 11257–62,
doi:10.1073/pnas.0702069104.
short: P. Schanda, V. Forge, B. Brutscher, Proceedings of the National Academy of
Sciences 104 (2007) 11257–11262.
date_created: 2020-09-18T10:12:54Z
date_published: 2007-07-03T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '03'
doi: 10.1073/pnas.0702069104
extern: '1'
intvolume: ' 104'
issue: '27'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '07'
oa_version: None
page: 11257-11262
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
status: public
title: Protein folding and unfolding studied at atomic resolution by fast two-dimensional
NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 104
year: '2007'
...
---
_id: '13425'
abstract:
- lang: eng
text: Nanoparticles (NPs) decorated with ligands combining photoswitchable dipoles
and covalent cross-linkers can be assembled by light into organized, three-dimensional
suprastructures of various types and sizes. NPs covered with only few photoactive
ligands form metastable crystals that can be assembled and disassembled “on demand”
by using light of different wavelengths. For higher surface concentrations, self-assembly
is irreversible, and the NPs organize into permanently cross-linked structures
including robust supracrystals and plastic spherical aggregates.
article_processing_charge: No
article_type: original
author:
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Kyle J. M.
full_name: Bishop, Kyle J. M.
last_name: Bishop
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Klajn R, Bishop KJM, Grzybowski BA. Light-controlled self-assembly of reversible
and irreversible nanoparticle suprastructures. Proceedings of the National
Academy of Sciences. 2007;104(25):10305-10309. doi:10.1073/pnas.0611371104
apa: Klajn, R., Bishop, K. J. M., & Grzybowski, B. A. (2007). Light-controlled
self-assembly of reversible and irreversible nanoparticle suprastructures. Proceedings
of the National Academy of Sciences. Proceedings of the National Academy of
Sciences. https://doi.org/10.1073/pnas.0611371104
chicago: Klajn, Rafal, Kyle J. M. Bishop, and Bartosz A. Grzybowski. “Light-Controlled
Self-Assembly of Reversible and Irreversible Nanoparticle Suprastructures.” Proceedings
of the National Academy of Sciences. Proceedings of the National Academy of
Sciences, 2007. https://doi.org/10.1073/pnas.0611371104.
ieee: R. Klajn, K. J. M. Bishop, and B. A. Grzybowski, “Light-controlled self-assembly
of reversible and irreversible nanoparticle suprastructures,” Proceedings of
the National Academy of Sciences, vol. 104, no. 25. Proceedings of the National
Academy of Sciences, pp. 10305–10309, 2007.
ista: Klajn R, Bishop KJM, Grzybowski BA. 2007. Light-controlled self-assembly of
reversible and irreversible nanoparticle suprastructures. Proceedings of the National
Academy of Sciences. 104(25), 10305–10309.
mla: Klajn, Rafal, et al. “Light-Controlled Self-Assembly of Reversible and Irreversible
Nanoparticle Suprastructures.” Proceedings of the National Academy of Sciences,
vol. 104, no. 25, Proceedings of the National Academy of Sciences, 2007, pp. 10305–09,
doi:10.1073/pnas.0611371104.
short: R. Klajn, K.J.M. Bishop, B.A. Grzybowski, Proceedings of the National Academy
of Sciences 104 (2007) 10305–10309.
date_created: 2023-08-01T10:31:19Z
date_published: 2007-06-19T00:00:00Z
date_updated: 2023-08-08T11:24:51Z
day: '19'
doi: 10.1073/pnas.0611371104
extern: '1'
external_id:
pmid:
- '17563381'
intvolume: ' 104'
issue: '25'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.0611371104
month: '06'
oa: 1
oa_version: Published Version
page: 10305-10309
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Light-controlled self-assembly of reversible and irreversible nanoparticle
suprastructures
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 104
year: '2007'
...
---
_id: '9487'
abstract:
- lang: eng
text: Cytosine DNA methylation is considered to be a stable epigenetic mark, but
active demethylation has been observed in both plants and animals. In Arabidopsis
thaliana, DNA glycosylases of the DEMETER (DME) family remove methylcytosines
from DNA. Demethylation by DME is necessary for genomic imprinting, and demethylation
by a related protein, REPRESSOR OF SILENCING1, prevents gene silencing in a transgenic
background. However, the extent and function of demethylation by DEMETER-LIKE
(DML) proteins in WT plants is not known. Using genome-tiling microarrays, we
mapped DNA methylation in mutant and WT plants and identified 179 loci actively
demethylated by DML enzymes. Mutations in DML genes lead to locus-specific DNA
hypermethylation. Reintroducing WT DML genes restores most loci to the normal
pattern of methylation, although at some loci, hypermethylated epialleles persist.
Of loci demethylated by DML enzymes, >80% are near or overlap genes. Genic demethylation
by DML enzymes primarily occurs at the 5′ and 3′ ends, a pattern opposite to the
overall distribution of WT DNA methylation. Our results show that demethylation
by DML DNA glycosylases edits the patterns of DNA methylation within the Arabidopsis
genome to protect genes from potentially deleterious methylation.
article_processing_charge: No
article_type: original
author:
- first_name: Jon
full_name: Penterman, Jon
last_name: Penterman
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Jin Hoe
full_name: Huh, Jin Hoe
last_name: Huh
- first_name: Tracy
full_name: Ballinger, Tracy
last_name: Ballinger
- first_name: Steven
full_name: Henikoff, Steven
last_name: Henikoff
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
citation:
ama: Penterman J, Zilberman D, Huh JH, Ballinger T, Henikoff S, Fischer RL. DNA
demethylation in the Arabidopsis genome. Proceedings of the National Academy
of Sciences. 2007;104(16):6752-6757. doi:10.1073/pnas.0701861104
apa: Penterman, J., Zilberman, D., Huh, J. H., Ballinger, T., Henikoff, S., &
Fischer, R. L. (2007). DNA demethylation in the Arabidopsis genome. Proceedings
of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.0701861104
chicago: Penterman, Jon, Daniel Zilberman, Jin Hoe Huh, Tracy Ballinger, Steven
Henikoff, and Robert L. Fischer. “DNA Demethylation in the Arabidopsis Genome.”
Proceedings of the National Academy of Sciences. National Academy of Sciences,
2007. https://doi.org/10.1073/pnas.0701861104.
ieee: J. Penterman, D. Zilberman, J. H. Huh, T. Ballinger, S. Henikoff, and R. L.
Fischer, “DNA demethylation in the Arabidopsis genome,” Proceedings of the
National Academy of Sciences, vol. 104, no. 16. National Academy of Sciences,
pp. 6752–6757, 2007.
ista: Penterman J, Zilberman D, Huh JH, Ballinger T, Henikoff S, Fischer RL. 2007.
DNA demethylation in the Arabidopsis genome. Proceedings of the National Academy
of Sciences. 104(16), 6752–6757.
mla: Penterman, Jon, et al. “DNA Demethylation in the Arabidopsis Genome.” Proceedings
of the National Academy of Sciences, vol. 104, no. 16, National Academy of
Sciences, 2007, pp. 6752–57, doi:10.1073/pnas.0701861104.
short: J. Penterman, D. Zilberman, J.H. Huh, T. Ballinger, S. Henikoff, R.L. Fischer,
Proceedings of the National Academy of Sciences 104 (2007) 6752–6757.
date_created: 2021-06-07T09:38:21Z
date_published: 2007-04-17T00:00:00Z
date_updated: 2021-12-14T08:55:12Z
day: '17'
department:
- _id: DaZi
doi: 10.1073/pnas.0701861104
extern: '1'
external_id:
pmid:
- '17409185'
intvolume: ' 104'
issue: '16'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.0701861104
month: '04'
oa: 1
oa_version: Published Version
page: 6752-6757
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: DNA demethylation in the Arabidopsis genome
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 104
year: '2007'
...
---
_id: '11877'
abstract:
- lang: eng
text: The World Wide Web provides a unprecedented opportunity to automatically analyze
a large sample of interests and activity in the world. We discuss methods for
extracting knowledge from the web by randomly sampling and analyzing hosts and
pages, and by analyzing the link structure of the web and how links accumulate
over time. A variety of interesting and valuable information can be extracted,
such as the distribution of web pages over domains, the distribution of interest
in different areas, communities related to different topics, the nature of competition
in different categories of sites, and the degree of communication between different
communities or countries.
article_processing_charge: No
article_type: original
author:
- first_name: Monika H
full_name: Henzinger, Monika H
id: 540c9bbd-f2de-11ec-812d-d04a5be85630
last_name: Henzinger
orcid: 0000-0002-5008-6530
- first_name: Steve
full_name: Lawrence, Steve
last_name: Lawrence
citation:
ama: Henzinger MH, Lawrence S. Extracting knowledge from the World Wide Web. Proceedings
of the National Academy of Sciences. 2004;101(suppl_1):5186-5191. doi:10.1073/pnas.0307528100
apa: Henzinger, M. H., & Lawrence, S. (2004). Extracting knowledge from the
World Wide Web. Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences. https://doi.org/10.1073/pnas.0307528100
chicago: Henzinger, Monika H, and Steve Lawrence. “Extracting Knowledge from the
World Wide Web.” Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences, 2004. https://doi.org/10.1073/pnas.0307528100.
ieee: M. H. Henzinger and S. Lawrence, “Extracting knowledge from the World Wide
Web,” Proceedings of the National Academy of Sciences, vol. 101, no. suppl_1.
Proceedings of the National Academy of Sciences, pp. 5186–5191, 2004.
ista: Henzinger MH, Lawrence S. 2004. Extracting knowledge from the World Wide Web.
Proceedings of the National Academy of Sciences. 101(suppl_1), 5186–5191.
mla: Henzinger, Monika H., and Steve Lawrence. “Extracting Knowledge from the World
Wide Web.” Proceedings of the National Academy of Sciences, vol. 101, no.
suppl_1, Proceedings of the National Academy of Sciences, 2004, pp. 5186–91, doi:10.1073/pnas.0307528100.
short: M.H. Henzinger, S. Lawrence, Proceedings of the National Academy of Sciences
101 (2004) 5186–5191.
date_created: 2022-08-16T13:06:10Z
date_published: 2004-04-06T00:00:00Z
date_updated: 2023-02-17T12:21:43Z
day: '06'
doi: 10.1073/pnas.0307528100
extern: '1'
external_id:
pmid:
- '14745041'
intvolume: ' 101'
issue: suppl_1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC387294/
month: '04'
oa: 1
oa_version: Published Version
page: 5186-5191
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Extracting knowledge from the World Wide Web
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 101
year: '2004'
...
---
_id: '3466'
abstract:
- lang: eng
text: Amphibian myelinated nerve fibers were treated with collagenase and protease.
Axons with retraction of the myelin sheath were patch-clamped in the nodal and
paranodal region. One type of Na channel was found. It has a single-channel conductance
of 11 pS (15 degrees C) and is blocked by tetrodotoxin. Averaged events show the
typical activation and inactivation kinetics of macroscopic Na current. Three
potential-dependent K channels were identified (I, F, and S channel). The I channel,
being the most frequent type, has a single-channel conductance of 23 pS (inward
current, 105 mM K on both sides of the membrane), activates between -60 and -30
mV, deactivates with intermediate kinetics, and is sensitive to dendrotoxin. The
F channel has a conductance of 30 pS, activates between -40 and 60 mV, and deactivates
with fast kinetics. The former inactivates within tens of seconds; the latter
inactivates within seconds. The third type, the S channel, has a conductance of
7 pS and deactivates slowly. All three channels can be blocked by external tetraethylammonium
chloride. We suggest that these distinct K channel types form the basis for the
different components of macroscopic K current described previously.
acknowledgement: We thank Drs. C. Baumann, D. Siemen, and W. Stuhmer for reading the
manuscript and Dr. F. Dreyer for the generous gift of DTX. The study was supported
by the Deutsche Forschungsgemeinschaft.
article_processing_charge: No
article_type: original
author:
- first_name: Peter M
full_name: Jonas, Peter M
id: 353C1B58-F248-11E8-B48F-1D18A9856A87
last_name: Jonas
orcid: 0000-0001-5001-4804
- first_name: Michael
full_name: Bräu, Michael
last_name: Bräu
- first_name: Markus
full_name: Hermsteiner, Markus
last_name: Hermsteiner
- first_name: Werner
full_name: Vogel, Werner
last_name: Vogel
citation:
ama: Jonas PM, Bräu M, Hermsteiner M, Vogel W. Single-channel recording in myelinated
nerve fibers reveals one type of Na channel but different K channels. PNAS.
1989;86(18):7238-7242. doi:10.1073/pnas.86.18.7238
apa: Jonas, P. M., Bräu, M., Hermsteiner, M., & Vogel, W. (1989). Single-channel
recording in myelinated nerve fibers reveals one type of Na channel but different
K channels. PNAS. National Academy of Sciences. https://doi.org/10.1073/pnas.86.18.7238
chicago: Jonas, Peter M, Michael Bräu, Markus Hermsteiner, and Werner Vogel. “Single-Channel
Recording in Myelinated Nerve Fibers Reveals One Type of Na Channel but Different
K Channels.” PNAS. National Academy of Sciences, 1989. https://doi.org/10.1073/pnas.86.18.7238.
ieee: P. M. Jonas, M. Bräu, M. Hermsteiner, and W. Vogel, “Single-channel recording
in myelinated nerve fibers reveals one type of Na channel but different K channels,”
PNAS, vol. 86, no. 18. National Academy of Sciences, pp. 7238–7242, 1989.
ista: Jonas PM, Bräu M, Hermsteiner M, Vogel W. 1989. Single-channel recording in
myelinated nerve fibers reveals one type of Na channel but different K channels.
PNAS. 86(18), 7238–7242.
mla: Jonas, Peter M., et al. “Single-Channel Recording in Myelinated Nerve Fibers
Reveals One Type of Na Channel but Different K Channels.” PNAS, vol. 86,
no. 18, National Academy of Sciences, 1989, pp. 7238–42, doi:10.1073/pnas.86.18.7238.
short: P.M. Jonas, M. Bräu, M. Hermsteiner, W. Vogel, PNAS 86 (1989) 7238–7242.
date_created: 2018-12-11T12:03:28Z
date_published: 1989-09-01T00:00:00Z
date_updated: 2022-02-14T16:12:33Z
day: '01'
doi: 10.1073/pnas.86.18.7238
extern: '1'
external_id:
pmid:
- '2550937 '
intvolume: ' 86'
issue: '18'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC298032/?tool=pubmed
month: '09'
oa: 1
oa_version: Published Version
page: 7238 - 7242
pmid: 1
publication: PNAS
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
publist_id: '2921'
quality_controlled: '1'
status: public
title: Single-channel recording in myelinated nerve fibers reveals one type of Na
channel but different K channels
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 86
year: '1989'
...