---
_id: '1867'
abstract:
- lang: eng
text: Cultured mammalian cells essential are model systems in basic biology research,
production platforms of proteins for medical use, and testbeds in synthetic biology.
Flavin cofactors, in particular flavin mononucleotide (FMN) and flavin adenine
dinucleotide (FAD), are critical for cellular redox reactions and sense light
in naturally occurring photoreceptors and optogenetic tools. Here, we quantified
flavin contents of commonly used mammalian cell lines. We first compared three
procedures for extraction of free and noncovalently protein-bound flavins and
verified extraction using fluorescence spectroscopy. For separation, two CE methods
with different BGEs were established, and detection was performed by LED-induced
fluorescence with limit of detections (LODs 0.5-3.8 nM). We found that riboflavin
(RF), FMN, and FAD contents varied significantly between cell lines. RF (3.1-14
amol/cell) and FAD (2.2-17.0 amol/cell) were the predominant flavins, while FMN
(0.46-3.4 amol/cell) was found at markedly lower levels. Observed flavin contents
agree with those previously extracted from mammalian tissues, yet reduced forms
of RF were detected that were not described previously. Quantification of flavins
in mammalian cell lines will allow a better understanding of cellular redox reactions
and optogenetic tools.
author:
- first_name: Jens
full_name: Hühner, Jens
last_name: Hühner
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Christian
full_name: Neusüß, Christian
last_name: Neusüß
- first_name: Michael
full_name: Lämmerhofer, Michael
last_name: Lämmerhofer
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis.
2015;36(4):518-525. doi:10.1002/elps.201400451
apa: Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak,
H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin
adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence
detection. Electrophoresis. Wiley. https://doi.org/10.1002/elps.201400451
chicago: Hühner, Jens, Álvaro Inglés Prieto, Christian Neusüß, Michael Lämmerhofer,
and Harald L Janovjak. “Quantification of Riboflavin, Flavin Mononucleotide, and
Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence
Detection.” Electrophoresis. Wiley, 2015. https://doi.org/10.1002/elps.201400451.
ieee: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, and H. L. Janovjak,
“Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection,” Electrophoresis,
vol. 36, no. 4. Wiley, pp. 518–525, 2015.
ista: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. 2015. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis. 36(4),
518–525.
mla: Hühner, Jens, et al. “Quantification of Riboflavin, Flavin Mononucleotide,
and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced
Fluorescence Detection.” Electrophoresis, vol. 36, no. 4, Wiley, 2015,
pp. 518–25, doi:10.1002/elps.201400451.
short: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, H.L. Janovjak, Electrophoresis
36 (2015) 518–525.
date_created: 2018-12-11T11:54:26Z
date_published: 2015-02-01T00:00:00Z
date_updated: 2021-01-12T06:53:43Z
day: '01'
department:
- _id: HaJa
doi: 10.1002/elps.201400451
ec_funded: 1
intvolume: ' 36'
issue: '4'
language:
- iso: eng
month: '02'
oa_version: None
page: 518 - 525
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
publication: Electrophoresis
publication_status: published
publisher: Wiley
publist_id: '5230'
pubrep_id: '836'
quality_controlled: '1'
scopus_import: 1
status: public
title: Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 36
year: '2015'
...
---
_id: '1549'
abstract:
- lang: eng
text: Nature has incorporated small photochromic molecules, colloquially termed
'photoswitches', in photoreceptor proteins to sense optical cues in photo-taxis
and vision. While Nature's ability to employ light-responsive functionalities
has long been recognized, it was not until recently that scientists designed,
synthesized and applied synthetic photochromes to manipulate many of which open
rapidly and locally in their native cell types, biological processes with the
temporal and spatial resolution of light. Ion channels in particular have come
to the forefront of proteins that can be put under the designer control of synthetic
photochromes. Photochromic ion channel controllers are comprised of three classes,
photochromic soluble ligands (PCLs), photochromic tethered ligands (PTLs) and
photochromic crosslinkers (PXs), and in each class ion channel functionality is
controlled through reversible changes in photochrome structure. By acting as light-dependent
ion channel agonists, antagonist or modulators, photochromic controllers effectively
converted a wide range of ion channels, including voltage-gated ion channels,
'leak channels', tri-, tetra- and pentameric ligand-gated ion channels, and temperaturesensitive
ion channels, into man-made photoreceptors. Control by photochromes can be reversible,
unlike in the case of 'caged' compounds, and non-invasive with high spatial precision,
unlike pharmacology and electrical manipulation. Here, we introduce design principles
of emerging photochromic molecules that act on ion channels and discuss the impact
that these molecules are beginning to have on ion channel biophysics and neuronal
physiology.
author:
- first_name: Catherine
full_name: Mckenzie, Catherine
id: 3EEDE19A-F248-11E8-B48F-1D18A9856A87
last_name: Mckenzie
- first_name: Inmaculada
full_name: Sanchez Romero, Inmaculada
id: 3D9C5D30-F248-11E8-B48F-1D18A9856A87
last_name: Sanchez Romero
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: 'Mckenzie C, Sanchez-Romero I, Janovjak HL. Flipping the photoswitch: Ion channels
under light control. In: Novel Chemical Tools to Study Ion Channel Biology.
Vol 869. Advances in Experimental Medicine and Biology. Springer; 2015:101-117.
doi:10.1007/978-1-4939-2845-3_6'
apa: 'Mckenzie, C., Sanchez-Romero, I., & Janovjak, H. L. (2015). Flipping the
photoswitch: Ion channels under light control. In Novel chemical tools to study
ion channel biology (Vol. 869, pp. 101–117). Springer. https://doi.org/10.1007/978-1-4939-2845-3_6'
chicago: 'Mckenzie, Catherine, Inmaculada Sanchez-Romero, and Harald L Janovjak.
“Flipping the Photoswitch: Ion Channels under Light Control.” In Novel Chemical
Tools to Study Ion Channel Biology, 869:101–17. Advances in Experimental Medicine
and Biology. Springer, 2015. https://doi.org/10.1007/978-1-4939-2845-3_6.'
ieee: 'C. Mckenzie, I. Sanchez-Romero, and H. L. Janovjak, “Flipping the photoswitch:
Ion channels under light control,” in Novel chemical tools to study ion channel
biology, vol. 869, Springer, 2015, pp. 101–117.'
ista: 'Mckenzie C, Sanchez-Romero I, Janovjak HL. 2015.Flipping the photoswitch:
Ion channels under light control. In: Novel chemical tools to study ion channel
biology. vol. 869, 101–117.'
mla: 'Mckenzie, Catherine, et al. “Flipping the Photoswitch: Ion Channels under
Light Control.” Novel Chemical Tools to Study Ion Channel Biology, vol.
869, Springer, 2015, pp. 101–17, doi:10.1007/978-1-4939-2845-3_6.'
short: C. Mckenzie, I. Sanchez-Romero, H.L. Janovjak, in:, Novel Chemical Tools
to Study Ion Channel Biology, Springer, 2015, pp. 101–117.
date_created: 2018-12-11T11:52:39Z
date_published: 2015-09-18T00:00:00Z
date_updated: 2021-01-12T06:51:32Z
day: '18'
ddc:
- '571'
- '576'
department:
- _id: HaJa
doi: 10.1007/978-1-4939-2845-3_6
file:
- access_level: open_access
checksum: bd1bfdf2423a0c3b6e7cabfa8b44bc0f
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:11:02Z
date_updated: 2020-07-14T12:45:01Z
file_id: '4854'
file_name: IST-2017-839-v1+1_mckenzie.pdf
file_size: 1919655
relation: main_file
file_date_updated: 2020-07-14T12:45:01Z
has_accepted_license: '1'
intvolume: ' 869'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Submitted Version
page: 101 - 117
publication: Novel chemical tools to study ion channel biology
publication_identifier:
isbn:
- 978-1-4939-2844-6
publication_status: published
publisher: Springer
publist_id: '5622'
pubrep_id: '839'
quality_controlled: '1'
scopus_import: 1
series_title: Advances in Experimental Medicine and Biology
status: public
title: 'Flipping the photoswitch: Ion channels under light control'
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 869
year: '2015'
...
---
_id: '1611'
abstract:
- lang: eng
text: Biosensors for signaling molecules allow the study of physiological processes
by bringing together the fields of protein engineering, fluorescence imaging,
and cell biology. Construction of genetically encoded biosensors generally relies
on the availability of a binding "core" that is both specific and stable,
which can then be combined with fluorescent molecules to create a sensor. However,
binding proteins with the desired properties are often not available in nature
and substantial improvement to sensors can be required, particularly with regard
to their durability. Ancestral protein reconstruction is a powerful protein-engineering
tool able to generate highly stable and functional proteins. In this work, we
sought to establish the utility of ancestral protein reconstruction to biosensor
development, beginning with the construction of an l-arginine biosensor. l-arginine,
as the immediate precursor to nitric oxide, is an important molecule in many physiological
contexts including brain function. Using a combination of ancestral reconstruction
and circular permutation, we constructed a Förster resonance energy transfer (FRET)
biosensor for l-arginine (cpFLIPR). cpFLIPR displays high sensitivity and specificity,
with a Kd of ∼14 μM and a maximal dynamic range of 35%. Importantly, cpFLIPR was
highly robust, enabling accurate l-arginine measurement at physiological temperatures.
We established that cpFLIPR is compatible with two-photon excitation fluorescence
microscopy and report l-arginine concentrations in brain tissue.
author:
- first_name: Jason
full_name: Whitfield, Jason
last_name: Whitfield
- first_name: William
full_name: Zhang, William
last_name: Zhang
- first_name: Michel
full_name: Herde, Michel
last_name: Herde
- first_name: Ben
full_name: Clifton, Ben
last_name: Clifton
- first_name: Johanna
full_name: Radziejewski, Johanna
last_name: Radziejewski
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Christian
full_name: Henneberger, Christian
last_name: Henneberger
- first_name: Colin
full_name: Jackson, Colin
last_name: Jackson
citation:
ama: Whitfield J, Zhang W, Herde M, et al. Construction of a robust and sensitive
arginine biosensor through ancestral protein reconstruction. Protein Science.
2015;24(9):1412-1422. doi:10.1002/pro.2721
apa: Whitfield, J., Zhang, W., Herde, M., Clifton, B., Radziejewski, J., Janovjak,
H. L., … Jackson, C. (2015). Construction of a robust and sensitive arginine biosensor
through ancestral protein reconstruction. Protein Science. Wiley. https://doi.org/10.1002/pro.2721
chicago: Whitfield, Jason, William Zhang, Michel Herde, Ben Clifton, Johanna Radziejewski,
Harald L Janovjak, Christian Henneberger, and Colin Jackson. “Construction of
a Robust and Sensitive Arginine Biosensor through Ancestral Protein Reconstruction.”
Protein Science. Wiley, 2015. https://doi.org/10.1002/pro.2721.
ieee: J. Whitfield et al., “Construction of a robust and sensitive arginine
biosensor through ancestral protein reconstruction,” Protein Science, vol.
24, no. 9. Wiley, pp. 1412–1422, 2015.
ista: Whitfield J, Zhang W, Herde M, Clifton B, Radziejewski J, Janovjak HL, Henneberger
C, Jackson C. 2015. Construction of a robust and sensitive arginine biosensor
through ancestral protein reconstruction. Protein Science. 24(9), 1412–1422.
mla: Whitfield, Jason, et al. “Construction of a Robust and Sensitive Arginine Biosensor
through Ancestral Protein Reconstruction.” Protein Science, vol. 24, no.
9, Wiley, 2015, pp. 1412–22, doi:10.1002/pro.2721.
short: J. Whitfield, W. Zhang, M. Herde, B. Clifton, J. Radziejewski, H.L. Janovjak,
C. Henneberger, C. Jackson, Protein Science 24 (2015) 1412–1422.
date_created: 2018-12-11T11:53:01Z
date_published: 2015-09-01T00:00:00Z
date_updated: 2021-01-12T06:52:00Z
day: '01'
department:
- _id: HaJa
doi: 10.1002/pro.2721
external_id:
pmid:
- '26061224'
intvolume: ' 24'
issue: '9'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4570536/
month: '09'
oa: 1
oa_version: Submitted Version
page: 1412 - 1422
pmid: 1
project:
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
publication: Protein Science
publication_status: published
publisher: Wiley
publist_id: '5555'
quality_controlled: '1'
scopus_import: 1
status: public
title: Construction of a robust and sensitive arginine biosensor through ancestral
protein reconstruction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2015'
...
---
_id: '1844'
abstract:
- lang: eng
text: 'Local protein interactions ("molecular context" effects) dictate
amino acid replacements and can be described in terms of site-specific, energetic
preferences for any different amino acid. It has been recently debated whether
these preferences remain approximately constant during evolution or whether, due
to coevolution of sites, they change strongly. Such research highlights an unresolved
and fundamental issue with far-reaching implications for phylogenetic analysis
and molecular evolution modeling. Here, we take advantage of the recent availability
of phenotypically supported laboratory resurrections of Precambrian thioredoxins
and β-lactamases to experimentally address the change of site-specific amino acid
preferences over long geological timescales. Extensive mutational analyses support
the notion that evolutionary adjustment to a new amino acid may occur, but to
a large extent this is insufficient to erase the primitive preference for amino
acid replacements. Generally, site-specific amino acid preferences appear to remain
conserved throughout evolutionary history despite local sequence divergence. We
show such preference conservation to be readily understandable in molecular terms
and we provide crystallographic evidence for an intriguing structural-switch mechanism:
Energetic preference for an ancestral amino acid in a modern protein can be linked
to reorganization upon mutation to the ancestral local structure around the mutated
site. Finally, we point out that site-specific preference conservation naturally
leads to one plausible evolutionary explanation for the existence of intragenic
global suppressor mutations.'
author:
- first_name: Valeria
full_name: Risso, Valeria
last_name: Risso
- first_name: Fadia
full_name: Manssour Triedo, Fadia
last_name: Manssour Triedo
- first_name: Asuncion
full_name: Delgado Delgado, Asuncion
last_name: Delgado Delgado
- first_name: Rocio
full_name: Arco, Rocio
last_name: Arco
- first_name: Alicia
full_name: Barroso Deljesús, Alicia
last_name: Barroso Deljesús
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Raquel
full_name: Godoy Ruiz, Raquel
last_name: Godoy Ruiz
- first_name: Josè
full_name: Gavira, Josè
last_name: Gavira
- first_name: Eric
full_name: Gaucher, Eric
last_name: Gaucher
- first_name: Beatriz
full_name: Ibarra Molero, Beatriz
last_name: Ibarra Molero
- first_name: Jose
full_name: Sánchez Ruiz, Jose
last_name: Sánchez Ruiz
citation:
ama: Risso V, Manssour Triedo F, Delgado Delgado A, et al. Mutational studies on
resurrected ancestral proteins reveal conservation of site-specific amino acid
preferences throughout evolutionary history. Molecular Biology and Evolution.
2014;32(2):440-455. doi:10.1093/molbev/msu312
apa: Risso, V., Manssour Triedo, F., Delgado Delgado, A., Arco, R., Barroso Deljesús,
A., Inglés Prieto, Á., … Sánchez Ruiz, J. (2014). Mutational studies on resurrected
ancestral proteins reveal conservation of site-specific amino acid preferences
throughout evolutionary history. Molecular Biology and Evolution. Oxford
University Press. https://doi.org/10.1093/molbev/msu312
chicago: Risso, Valeria, Fadia Manssour Triedo, Asuncion Delgado Delgado, Rocio
Arco, Alicia Barroso Deljesús, Álvaro Inglés Prieto, Raquel Godoy Ruiz, et al.
“Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific
Amino Acid Preferences throughout Evolutionary History.” Molecular Biology
and Evolution. Oxford University Press, 2014. https://doi.org/10.1093/molbev/msu312.
ieee: V. Risso et al., “Mutational studies on resurrected ancestral proteins
reveal conservation of site-specific amino acid preferences throughout evolutionary
history,” Molecular Biology and Evolution, vol. 32, no. 2. Oxford University
Press, pp. 440–455, 2014.
ista: Risso V, Manssour Triedo F, Delgado Delgado A, Arco R, Barroso Deljesús A,
Inglés Prieto Á, Godoy Ruiz R, Gavira J, Gaucher E, Ibarra Molero B, Sánchez Ruiz
J. 2014. Mutational studies on resurrected ancestral proteins reveal conservation
of site-specific amino acid preferences throughout evolutionary history. Molecular
Biology and Evolution. 32(2), 440–455.
mla: Risso, Valeria, et al. “Mutational Studies on Resurrected Ancestral Proteins
Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary
History.” Molecular Biology and Evolution, vol. 32, no. 2, Oxford University
Press, 2014, pp. 440–55, doi:10.1093/molbev/msu312.
short: V. Risso, F. Manssour Triedo, A. Delgado Delgado, R. Arco, A. Barroso Deljesús,
Á. Inglés Prieto, R. Godoy Ruiz, J. Gavira, E. Gaucher, B. Ibarra Molero, J. Sánchez
Ruiz, Molecular Biology and Evolution 32 (2014) 440–455.
date_created: 2018-12-11T11:54:19Z
date_published: 2014-11-12T00:00:00Z
date_updated: 2021-01-12T06:53:34Z
day: '12'
ddc:
- '571'
department:
- _id: HaJa
doi: 10.1093/molbev/msu312
file:
- access_level: open_access
checksum: 06215318e66be8f3e0c33abb07e9d3da
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:16:56Z
date_updated: 2020-07-14T12:45:19Z
file_id: '5247'
file_name: IST-2016-430-v1+1_Mol_Biol_Evol-2015-Risso-440-55.pdf
file_size: 1545246
relation: main_file
file_date_updated: 2020-07-14T12:45:19Z
has_accepted_license: '1'
intvolume: ' 32'
issue: '2'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '11'
oa: 1
oa_version: Published Version
page: 440 - 455
publication: Molecular Biology and Evolution
publication_status: published
publisher: Oxford University Press
publist_id: '5257'
pubrep_id: '430'
quality_controlled: '1'
scopus_import: 1
status: public
title: Mutational studies on resurrected ancestral proteins reveal conservation of
site-specific amino acid preferences throughout evolutionary history
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2014'
...
---
_id: '2032'
abstract:
- lang: eng
text: As light-based control of fundamental signaling pathways is becoming a reality,
the field of optogenetics is rapidly moving beyond neuroscience. We have recently
developed receptor tyrosine kinases that are activated by light and control cell
proliferation, epithelial–mesenchymal transition, and angiogenic sprouting—cell
behaviors central to cancer progression.
article_number: e964045
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Karin
full_name: Schelch, Karin
last_name: Schelch
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
citation:
ama: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology.
2014;1(4). doi:10.4161/23723548.2014.964045'
apa: 'Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L.,
& Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular
and Cellular Oncology. Taylor & Francis. https://doi.org/10.4161/23723548.2014.964045'
chicago: 'Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Karin Schelch, Harald
L Janovjak, and Michael Grusch. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology. Taylor & Francis, 2014. https://doi.org/10.4161/23723548.2014.964045.'
ieee: 'Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H. L. Janovjak, and
M. Grusch, “The optogenetic promise for oncology: Episode I,” Molecular and
Cellular Oncology, vol. 1, no. 4. Taylor & Francis, 2014.'
ista: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
2014. The optogenetic promise for oncology: Episode I. Molecular and Cellular
Oncology. 1(4), e964045.'
mla: 'Inglés Prieto, Álvaro, et al. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology, vol. 1, no. 4, e964045, Taylor &
Francis, 2014, doi:10.4161/23723548.2014.964045.'
short: Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H.L. Janovjak, M. Grusch,
Molecular and Cellular Oncology 1 (2014).
date_created: 2018-12-11T11:55:19Z
date_published: 2014-12-31T00:00:00Z
date_updated: 2021-01-12T06:54:51Z
day: '31'
ddc:
- '570'
department:
- _id: HaJa
doi: 10.4161/23723548.2014.964045
file:
- access_level: open_access
checksum: 44e17ad40577ab46eb602e88a8b0b8fd
content_type: application/pdf
creator: kschuh
date_created: 2019-05-16T13:39:11Z
date_updated: 2020-07-14T12:45:26Z
file_id: '6464'
file_name: 2014_Taylor_Alvaro.pdf
file_size: 1765933
relation: main_file
file_date_updated: 2020-07-14T12:45:26Z
has_accepted_license: '1'
intvolume: ' 1'
issue: '4'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
publication: Molecular and Cellular Oncology
publication_status: published
publisher: Taylor & Francis
publist_id: '5040'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'The optogenetic promise for oncology: Episode I'
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 1
year: '2014'
...
---
_id: '2084'
abstract:
- lang: eng
text: Receptor tyrosine kinases (RTKs) are a large family of cell surface receptors
that sense growth factors and hormones and regulate a variety of cell behaviours
in health and disease. Contactless activation of RTKs with spatial and temporal
precision is currently not feasible. Here, we generated RTKs that are insensitive
to endogenous ligands but can be selectively activated by low-intensity blue light.
We screened light-oxygen-voltage (LOV)-sensing domains for their ability to activate
RTKs by light-activated dimerization. Incorporation of LOV domains found in aureochrome
photoreceptors of stramenopiles resulted in robust activation of the fibroblast
growth factor receptor 1 (FGFR1), epidermal growth factor receptor (EGFR) and
rearranged during transfection (RET). In human cancer and endothelial cells, light
induced cellular signalling with spatial and temporal precision. Furthermore,
light faithfully mimicked complex mitogenic and morphogenic cell behaviour induced
by growth factors. RTKs under optical control (Opto-RTKs) provide a powerful optogenetic
approach to actuate cellular signals and manipulate cell behaviour.
acknowledgement: European Union Seventh Framework Programme; Human Frontier Science
Program; Oesterreichische Nationalbank Anniversary Fund 14211; Austrian Research
Promotion Agency; FemTech
author:
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
- first_name: Karin
full_name: Schelch, Karin
last_name: Schelch
- first_name: Robert
full_name: Riedler, Robert
last_name: Riedler
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Christopher
full_name: Differ, Christopher
last_name: Differ
- first_name: Walter
full_name: Berger, Walter
last_name: Berger
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Grusch M, Schelch K, Riedler R, et al. Spatio-temporally precise activation
of engineered receptor tyrosine kinases by light. EMBO Journal. 2014;33(15):1713-1726.
doi:10.15252/embj.201387695
apa: Grusch, M., Schelch, K., Riedler, R., Gschaider-Reichhart, E., Differ, C.,
Berger, W., … Janovjak, H. L. (2014). Spatio-temporally precise activation of
engineered receptor tyrosine kinases by light. EMBO Journal. Wiley-Blackwell.
https://doi.org/10.15252/embj.201387695
chicago: Grusch, Michael, Karin Schelch, Robert Riedler, Eva Gschaider-Reichhart,
Christopher Differ, Walter Berger, Álvaro Inglés Prieto, and Harald L Janovjak.
“Spatio-Temporally Precise Activation of Engineered Receptor Tyrosine Kinases
by Light.” EMBO Journal. Wiley-Blackwell, 2014. https://doi.org/10.15252/embj.201387695.
ieee: M. Grusch et al., “Spatio-temporally precise activation of engineered
receptor tyrosine kinases by light,” EMBO Journal, vol. 33, no. 15. Wiley-Blackwell,
pp. 1713–1726, 2014.
ista: Grusch M, Schelch K, Riedler R, Gschaider-Reichhart E, Differ C, Berger W,
Inglés Prieto Á, Janovjak HL. 2014. Spatio-temporally precise activation of engineered
receptor tyrosine kinases by light. EMBO Journal. 33(15), 1713–1726.
mla: Grusch, Michael, et al. “Spatio-Temporally Precise Activation of Engineered
Receptor Tyrosine Kinases by Light.” EMBO Journal, vol. 33, no. 15, Wiley-Blackwell,
2014, pp. 1713–26, doi:10.15252/embj.201387695.
short: M. Grusch, K. Schelch, R. Riedler, E. Gschaider-Reichhart, C. Differ, W.
Berger, Á. Inglés Prieto, H.L. Janovjak, EMBO Journal 33 (2014) 1713–1726.
date_created: 2018-12-11T11:55:37Z
date_published: 2014-07-01T00:00:00Z
date_updated: 2023-09-07T12:49:09Z
day: '01'
department:
- _id: HaJa
doi: 10.15252/embj.201387695
intvolume: ' 33'
issue: '15'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4194103/
month: '07'
oa: 1
oa_version: Submitted Version
page: 1713 - 1726
publication: EMBO Journal
publication_status: published
publisher: Wiley-Blackwell
publist_id: '4953'
quality_controlled: '1'
related_material:
record:
- id: '418'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: Spatio-temporally precise activation of engineered receptor tyrosine kinases
by light
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 33
year: '2014'
...
---
_id: '2471'
abstract:
- lang: eng
text: The impact of disulfide bonds on protein stability goes beyond simple equilibrium
thermodynamics effects associated with the conformational entropy of the unfolded
state. Indeed, disulfide crosslinks may play a role in the prevention of dysfunctional
association and strongly affect the rates of irreversible enzyme inactivation,
highly relevant in biotechnological applications. While these kinetic-stability
effects remain poorly understood, by analogy with proposed mechanisms for processes
of protein aggregation and fibrillogenesis, we propose that they may be determined
by the properties of sparsely-populated, partially-unfolded intermediates. Here
we report the successful design, on the basis of high temperature molecular-dynamics
simulations, of six thermodynamically and kinetically stabilized variants of phytase
from Citrobacter braakii (a biotechnologically important enzyme) with one, two
or three engineered disulfides. Activity measurements and 3D crystal structure
determination demonstrate that the engineered crosslinks do not cause dramatic
alterations in the native structure. The inactivation kinetics for all the variants
displays a strongly non-Arrhenius temperature dependence, with the time-scale
for the irreversible denaturation process reaching a minimum at a given temperature
within the range of the denaturation transition. We show this striking feature
to be a signature of a key role played by a partially unfolded, intermediate state/ensemble.
Energetic and mutational analyses confirm that the intermediate is highly unfolded
(akin to a proposed critical intermediate in the misfolding of the prion protein),
a result that explains the observed kinetic stabilization. Our results provide
a rationale for the kinetic-stability consequences of disulfide-crosslink engineering
and an experimental methodology to arrive at energetic/structural descriptions
of the sparsely populated and elusive intermediates that play key roles in irreversible
protein denaturation.
article_number: e70013
author:
- first_name: Inmaculada
full_name: Sanchez Romero, Inmaculada
id: 3D9C5D30-F248-11E8-B48F-1D18A9856A87
last_name: Sanchez Romero
- first_name: Antonio
full_name: Ariza, Antonio
last_name: Ariza
- first_name: Keith
full_name: Wilson, Keith
last_name: Wilson
- first_name: Michael
full_name: Skjøt, Michael
last_name: Skjøt
- first_name: Jesper
full_name: Vind, Jesper
last_name: Vind
- first_name: Leonardo
full_name: De Maria, Leonardo
last_name: De Maria
- first_name: Lars
full_name: Skov, Lars
last_name: Skov
- first_name: Jose
full_name: Sánchez Ruiz, Jose
last_name: Sánchez Ruiz
citation:
ama: Sanchez-Romero I, Ariza A, Wilson K, et al. Mechanism of protein kinetic stabilization
by engineered disulfide crosslinks. PLoS One. 2013;8(7). doi:10.1371/journal.pone.0070013
apa: Sanchez-Romero, I., Ariza, A., Wilson, K., Skjøt, M., Vind, J., De Maria, L.,
… Sánchez Ruiz, J. (2013). Mechanism of protein kinetic stabilization by engineered
disulfide crosslinks. PLoS One. Public Library of Science. https://doi.org/10.1371/journal.pone.0070013
chicago: Sanchez-Romero, Inmaculada, Antonio Ariza, Keith Wilson, Michael Skjøt,
Jesper Vind, Leonardo De Maria, Lars Skov, and Jose Sánchez Ruiz. “Mechanism of
Protein Kinetic Stabilization by Engineered Disulfide Crosslinks.” PLoS One.
Public Library of Science, 2013. https://doi.org/10.1371/journal.pone.0070013.
ieee: I. Sanchez-Romero et al., “Mechanism of protein kinetic stabilization
by engineered disulfide crosslinks,” PLoS One, vol. 8, no. 7. Public Library
of Science, 2013.
ista: Sanchez-Romero I, Ariza A, Wilson K, Skjøt M, Vind J, De Maria L, Skov L,
Sánchez Ruiz J. 2013. Mechanism of protein kinetic stabilization by engineered
disulfide crosslinks. PLoS One. 8(7), e70013.
mla: Sanchez-Romero, Inmaculada, et al. “Mechanism of Protein Kinetic Stabilization
by Engineered Disulfide Crosslinks.” PLoS One, vol. 8, no. 7, e70013, Public
Library of Science, 2013, doi:10.1371/journal.pone.0070013.
short: I. Sanchez-Romero, A. Ariza, K. Wilson, M. Skjøt, J. Vind, L. De Maria, L.
Skov, J. Sánchez Ruiz, PLoS One 8 (2013).
date_created: 2018-12-11T11:57:51Z
date_published: 2013-07-30T00:00:00Z
date_updated: 2021-01-12T06:57:41Z
day: '30'
ddc:
- '570'
department:
- _id: HaJa
doi: 10.1371/journal.pone.0070013
file:
- access_level: open_access
checksum: c0c96cc76ed7ef0d036a31a7e33c9a37
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:15:07Z
date_updated: 2020-07-14T12:45:41Z
file_id: '5124'
file_name: IST-2016-414-v1+1_journal.pone.0070013.pdf
file_size: 1323666
relation: main_file
file_date_updated: 2020-07-14T12:45:41Z
has_accepted_license: '1'
intvolume: ' 8'
issue: '7'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
publication: PLoS One
publication_status: published
publisher: Public Library of Science
publist_id: '4430'
pubrep_id: '414'
quality_controlled: '1'
scopus_import: 1
status: public
title: Mechanism of protein kinetic stabilization by engineered disulfide crosslinks
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2013'
...
---
_id: '2856'
abstract:
- lang: eng
text: 'G protein–coupled receptors (GPCRs), the largest family of membrane signaling
proteins, respond to neurotransmitters, hormones and small environmental molecules.
The neuronal function of many GPCRs has been difficult to resolve because of an
inability to gate them with subtype specificity, spatial precision, speed and
reversibility. To address this, we developed an approach for opto-chemical engineering
of native GPCRs. We applied this to the metabotropic glutamate receptors (mGluRs)
to generate light-agonized and light-antagonized mGluRs (LimGluRs). The light-agonized
LimGluR2, on which we focused, was fast, bistable and supported multiple rounds
of on/off switching. Light gated two of the primary neuronal functions of mGluR2:
suppression of excitability and inhibition of neurotransmitter release. We found
that the light-antagonized tool LimGluR2-block was able to manipulate negative
feedback of synaptically released glutamate on transmitter release. We generalized
the optical control to two additional family members: mGluR3 and mGluR6. This
system worked in rodent brain slices and in zebrafish in vivo, where we found
that mGluR2 modulated the threshold for escape behavior. These light-gated mGluRs
pave the way for determining the roles of mGluRs in synaptic plasticity, memory
and disease.'
acknowledgement: National Science Foundation grants CHE-0233882 and CHE-0840505 (to
the College of Chemistry at the University of California, Berkeley), a postdoctoral
fellowship of the European Molecular Biology Organization (H.J.)
author:
- first_name: Joshua
full_name: Levitz, Joshua
last_name: Levitz
- first_name: Carlos
full_name: Pantoja, Carlos
last_name: Pantoja
- first_name: Benjamin
full_name: Gaub, Benjamin
last_name: Gaub
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Andreas
full_name: Reiner, Andreas
last_name: Reiner
- first_name: Adam
full_name: Hoagland, Adam
last_name: Hoagland
- first_name: David
full_name: Schoppik, David
last_name: Schoppik
- first_name: Brian
full_name: Kane, Brian
last_name: Kane
- first_name: Philipp
full_name: Stawski, Philipp
last_name: Stawski
- first_name: Alexander
full_name: Schier, Alexander
last_name: Schier
- first_name: Dirk
full_name: Trauner, Dirk
last_name: Trauner
- first_name: Ehud
full_name: Isacoff, Ehud
last_name: Isacoff
citation:
ama: Levitz J, Pantoja C, Gaub B, et al. Optical control of metabotropic glutamate
receptors. Nature Neuroscience. 2013;16:507-516. doi:10.1038/nn.3346
apa: Levitz, J., Pantoja, C., Gaub, B., Janovjak, H. L., Reiner, A., Hoagland, A.,
… Isacoff, E. (2013). Optical control of metabotropic glutamate receptors. Nature
Neuroscience. Nature Publishing Group. https://doi.org/10.1038/nn.3346
chicago: Levitz, Joshua, Carlos Pantoja, Benjamin Gaub, Harald L Janovjak, Andreas
Reiner, Adam Hoagland, David Schoppik, et al. “Optical Control of Metabotropic
Glutamate Receptors.” Nature Neuroscience. Nature Publishing Group, 2013.
https://doi.org/10.1038/nn.3346.
ieee: J. Levitz et al., “Optical control of metabotropic glutamate receptors,”
Nature Neuroscience, vol. 16. Nature Publishing Group, pp. 507–516, 2013.
ista: Levitz J, Pantoja C, Gaub B, Janovjak HL, Reiner A, Hoagland A, Schoppik D,
Kane B, Stawski P, Schier A, Trauner D, Isacoff E. 2013. Optical control of metabotropic
glutamate receptors. Nature Neuroscience. 16, 507–516.
mla: Levitz, Joshua, et al. “Optical Control of Metabotropic Glutamate Receptors.”
Nature Neuroscience, vol. 16, Nature Publishing Group, 2013, pp. 507–16,
doi:10.1038/nn.3346.
short: J. Levitz, C. Pantoja, B. Gaub, H.L. Janovjak, A. Reiner, A. Hoagland, D.
Schoppik, B. Kane, P. Stawski, A. Schier, D. Trauner, E. Isacoff, Nature Neuroscience
16 (2013) 507–516.
date_created: 2018-12-11T11:59:57Z
date_published: 2013-03-03T00:00:00Z
date_updated: 2021-01-12T07:00:16Z
day: '03'
department:
- _id: HaJa
doi: 10.1038/nn.3346
external_id:
pmid:
- '23455609'
intvolume: ' 16'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681425/
month: '03'
oa: 1
oa_version: Submitted Version
page: 507 - 516
pmid: 1
publication: Nature Neuroscience
publication_status: published
publisher: Nature Publishing Group
publist_id: '3936'
quality_controlled: '1'
scopus_import: 1
status: public
title: Optical control of metabotropic glutamate receptors
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2013'
...
---
_id: '2857'
abstract:
- lang: eng
text: In the vibrant field of optogenetics, optics and genetic targeting are combined
to commandeer cellular functions, such as the neuronal action potential, by optically
stimulating light-sensitive ion channels expressed in the cell membrane. One broadly
applicable manifestation of this approach are covalently attached photochromic
tethered ligands (PTLs) that allow activating ligand-gated ion channels with outstanding
spatial and temporal resolution. Here, we describe all steps towards the successful
development and application of PTL-gated ion channels in cell lines and primary
cells. The basis for these experiments forms a combination of molecular modeling,
genetic engineering, cell culture, and electrophysiology. The light-gated glutamate
receptor (LiGluR), which consists of the PTL-functionalized GluK2 receptor, serves
as a model.
alternative_title:
- MIMB
author:
- first_name: Stephanie
full_name: Szobota, Stephanie
last_name: Szobota
- first_name: Catherine
full_name: Mckenzie, Catherine
id: 3EEDE19A-F248-11E8-B48F-1D18A9856A87
last_name: Mckenzie
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Szobota S, Mckenzie C, Janovjak HL. Optical control of ligand-gated ion channels.
Methods in Molecular Biology. 2013;998:417-435. doi:10.1007/978-1-62703-351-0_32
apa: Szobota, S., Mckenzie, C., & Janovjak, H. L. (2013). Optical control of
ligand-gated ion channels. Methods in Molecular Biology. Springer. https://doi.org/10.1007/978-1-62703-351-0_32
chicago: Szobota, Stephanie, Catherine Mckenzie, and Harald L Janovjak. “Optical
Control of Ligand-Gated Ion Channels.” Methods in Molecular Biology. Springer,
2013. https://doi.org/10.1007/978-1-62703-351-0_32.
ieee: S. Szobota, C. Mckenzie, and H. L. Janovjak, “Optical control of ligand-gated
ion channels,” Methods in Molecular Biology, vol. 998. Springer, pp. 417–435,
2013.
ista: Szobota S, Mckenzie C, Janovjak HL. 2013. Optical control of ligand-gated
ion channels. Methods in Molecular Biology. 998, 417–435.
mla: Szobota, Stephanie, et al. “Optical Control of Ligand-Gated Ion Channels.”
Methods in Molecular Biology, vol. 998, Springer, 2013, pp. 417–35, doi:10.1007/978-1-62703-351-0_32.
short: S. Szobota, C. Mckenzie, H.L. Janovjak, Methods in Molecular Biology 998
(2013) 417–435.
date_created: 2018-12-11T11:59:57Z
date_published: 2013-02-22T00:00:00Z
date_updated: 2021-01-12T07:00:17Z
day: '22'
ddc:
- '570'
department:
- _id: HaJa
doi: 10.1007/978-1-62703-351-0_32
ec_funded: 1
file:
- access_level: open_access
checksum: 1701f0d989f27ddac471b19a894ec0d1
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:12:34Z
date_updated: 2020-07-14T12:45:51Z
file_id: '4952'
file_name: IST-2017-834-v1+1_szobota.pdf
file_size: 336734
relation: main_file
file_date_updated: 2020-07-14T12:45:51Z
has_accepted_license: '1'
intvolume: ' 998'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Submitted Version
page: 417 - 435
project:
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
publication: Methods in Molecular Biology
publication_status: published
publisher: Springer
publist_id: '3932'
pubrep_id: '834'
quality_controlled: '1'
scopus_import: 1
status: public
title: Optical control of ligand-gated ion channels
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 998
year: '2013'
...
---
_id: '505'
abstract:
- lang: eng
text: Alkyd resins are polyesters containing unsaturated fatty acids that are used
as binding agents in paints and coatings. Chemical drying of these polyesters
is based on heavy metal catalyzed cross-linking of the unsaturated fatty acid
moieties. Among the heavy-metal catalysts, cobalt complexes are the most effective,
yet they have been proven to be carcinogenic. Therefore, strategies to replace
the cobalt-based catalyst by environmentally friendlier and less toxic alternatives
are under development. Here, we demonstrate for the first time that a laccase-mediator
system can effectively replace the heavy-metal catalyst and cross-link alkyd resins.
Interestingly, the biocatalytic reaction does not only work in aqueous media,
but also in a solid film, where enzyme diffusion is limited. Within the catalytic
cycle, the mediator oxidizes the alkyd resin and is regenerated by the laccase,
which is uniformly distributed within the drying film as evidenced by confocal
laser scanning microscopy. During gradual build-up of molecular weight, there
is a concomitant decrease of the oxygen content in the film. A new optical sensor
to follow oxygen consumption during the cross-linking reaction was developed and
validated with state of the art techniques. A remarkable feature is the low sample
amount required, which allows faster screening of new catalysts.
acknowledgement: "This study was performed within the Austrian Centre of Indus-\r\ntrial
Biotechnology ACIB and the COST Action 868. This work\r\nhas been supported by the
Federal Ministry of Economy,\r\nFamily and Youth (BMWFJ), the Federal Ministry of
Tra\r\nffi\r\nc,\r\nInnovation and Technology (bmvit), the Styrian Business\r\nPromotion
Agency SFG, the Standortagentur Tirol and ZIT\r\n–\r\nTechnology Agency of the
\ City of Vienna through the\r\nCOMET-Funding Program managed by the Austrian
Research\r\nPromotion Agency FFG. Dr Massimiliano Cardinale (Institute of\r\nEnvironmental
Biotechnology, TU Graz) is gratefully acknowl-\r\nedged for technical support with
the CLSM measurements."
author:
- first_name: Katrin
full_name: Greimel, Katrin
last_name: Greimel
- first_name: Veronika
full_name: Perz, Veronika
last_name: Perz
- first_name: Klaus
full_name: Koren, Klaus
id: 382FBD6A-F248-11E8-B48F-1D18A9856A87
last_name: Koren
- first_name: Roland
full_name: Feola, Roland
last_name: Feola
- first_name: Armin
full_name: Temel, Armin
last_name: Temel
- first_name: Christian
full_name: Sohar, Christian
last_name: Sohar
- first_name: Enrique
full_name: Herrero Acero, Enrique
last_name: Herrero Acero
- first_name: Ingo
full_name: Klimant, Ingo
last_name: Klimant
- first_name: Georg
full_name: Guebitz, Georg
last_name: Guebitz
citation:
ama: 'Greimel K, Perz V, Koren K, et al. Banning toxic heavy-metal catalysts from
paints: Enzymatic cross-linking of alkyd resins. Green Chemistry. 2013;15(2):381-388.
doi:10.1039/c2gc36666e'
apa: 'Greimel, K., Perz, V., Koren, K., Feola, R., Temel, A., Sohar, C., … Guebitz,
G. (2013). Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking
of alkyd resins. Green Chemistry. Royal Society of Chemistry. https://doi.org/10.1039/c2gc36666e'
chicago: 'Greimel, Katrin, Veronika Perz, Klaus Koren, Roland Feola, Armin Temel,
Christian Sohar, Enrique Herrero Acero, Ingo Klimant, and Georg Guebitz. “Banning
Toxic Heavy-Metal Catalysts from Paints: Enzymatic Cross-Linking of Alkyd Resins.”
Green Chemistry. Royal Society of Chemistry, 2013. https://doi.org/10.1039/c2gc36666e.'
ieee: 'K. Greimel et al., “Banning toxic heavy-metal catalysts from paints:
Enzymatic cross-linking of alkyd resins,” Green Chemistry, vol. 15, no.
2. Royal Society of Chemistry, pp. 381–388, 2013.'
ista: 'Greimel K, Perz V, Koren K, Feola R, Temel A, Sohar C, Herrero Acero E, Klimant
I, Guebitz G. 2013. Banning toxic heavy-metal catalysts from paints: Enzymatic
cross-linking of alkyd resins. Green Chemistry. 15(2), 381–388.'
mla: 'Greimel, Katrin, et al. “Banning Toxic Heavy-Metal Catalysts from Paints:
Enzymatic Cross-Linking of Alkyd Resins.” Green Chemistry, vol. 15, no.
2, Royal Society of Chemistry, 2013, pp. 381–88, doi:10.1039/c2gc36666e.'
short: K. Greimel, V. Perz, K. Koren, R. Feola, A. Temel, C. Sohar, E. Herrero Acero,
I. Klimant, G. Guebitz, Green Chemistry 15 (2013) 381–388.
date_created: 2018-12-11T11:46:51Z
date_published: 2013-02-01T00:00:00Z
date_updated: 2021-01-12T08:01:11Z
day: '01'
department:
- _id: HaJa
doi: 10.1039/c2gc36666e
intvolume: ' 15'
issue: '2'
language:
- iso: eng
month: '02'
oa_version: None
page: 381 - 388
publication: Green Chemistry
publication_status: published
publisher: Royal Society of Chemistry
publist_id: '7313'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of
alkyd resins'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 15
year: '2013'
...
---
_id: '10896'
abstract:
- lang: eng
text: Under physiological conditions the brain, via the purine salvage pathway,
reuses the preformed purine bases hypoxanthine, derived from ATP degradation,
and adenine (Ade), derived from polyamine synthesis, to restore its ATP pool.
However, the massive degradation of ATP during ischemia, although providing valuable
neuroprotective adenosine, results in the accumulation and loss of diffusible
purine metabolites and thereby leads to a protracted reduction in the post-ischemic
ATP pool size. In vivo, this may both limit the ability to deploy ATP-dependent
reparative mechanisms and reduce the subsequent availability of adenosine, whilst
in brain slices results in tissue with substantially lower levels of ATP than
in vivo. In the present review, we describe the mechanisms by which brain tissue
replenishes its ATP, how this can be improved with the clinically tolerated chemicals
D-ribose and adenine, and the functional, and potential therapeutic, implications
of doing so.
acknowledgement: We are grateful to Research into Ageing/Ageing UK and The Dunhill
Trust for funding SzN’s graduate studies, and to Prof Nicholas Dale for his valuable
input.
article_processing_charge: No
author:
- first_name: Stephanie
full_name: zur Nedden, Stephanie
id: 3C77F464-F248-11E8-B48F-1D18A9856A87
last_name: zur Nedden
- first_name: Alexander S.
full_name: Doney, Alexander S.
last_name: Doney
- first_name: Bruno G.
full_name: Frenguelli, Bruno G.
last_name: Frenguelli
citation:
ama: 'zur Nedden S, Doney AS, Frenguelli BG. The double-edged sword: Gaining Adenosine
at the expense of ATP. How to balance the books. In: Masino S, Boison D, eds.
Adenosine. 1st ed. New York: Springer; 2012:109-129. doi:10.1007/978-1-4614-3903-5_6'
apa: 'zur Nedden, S., Doney, A. S., & Frenguelli, B. G. (2012). The double-edged
sword: Gaining Adenosine at the expense of ATP. How to balance the books. In S.
Masino & D. Boison (Eds.), Adenosine (1st ed., pp. 109–129). New York:
Springer. https://doi.org/10.1007/978-1-4614-3903-5_6'
chicago: 'Nedden, Stephanie zur, Alexander S. Doney, and Bruno G. Frenguelli. “The
Double-Edged Sword: Gaining Adenosine at the Expense of ATP. How to Balance the
Books.” In Adenosine, edited by Susan Masino and Detlev Boison, 1st ed.,
109–29. New York: Springer, 2012. https://doi.org/10.1007/978-1-4614-3903-5_6.'
ieee: 'S. zur Nedden, A. S. Doney, and B. G. Frenguelli, “The double-edged sword:
Gaining Adenosine at the expense of ATP. How to balance the books,” in Adenosine,
1st ed., S. Masino and D. Boison, Eds. New York: Springer, 2012, pp. 109–129.'
ista: 'zur Nedden S, Doney AS, Frenguelli BG. 2012.The double-edged sword: Gaining
Adenosine at the expense of ATP. How to balance the books. In: Adenosine. , 109–129.'
mla: 'zur Nedden, Stephanie, et al. “The Double-Edged Sword: Gaining Adenosine at
the Expense of ATP. How to Balance the Books.” Adenosine, edited by Susan
Masino and Detlev Boison, 1st ed., Springer, 2012, pp. 109–29, doi:10.1007/978-1-4614-3903-5_6.'
short: S. zur Nedden, A.S. Doney, B.G. Frenguelli, in:, S. Masino, D. Boison (Eds.),
Adenosine, 1st ed., Springer, New York, 2012, pp. 109–129.
date_created: 2022-03-21T07:16:12Z
date_published: 2012-07-23T00:00:00Z
date_updated: 2022-06-21T11:51:58Z
day: '23'
department:
- _id: HaJa
doi: 10.1007/978-1-4614-3903-5_6
edition: '1'
editor:
- first_name: Susan
full_name: Masino, Susan
last_name: Masino
- first_name: Detlev
full_name: Boison, Detlev
last_name: Boison
language:
- iso: eng
month: '07'
oa_version: None
page: 109-129
place: New York
publication: Adenosine
publication_identifier:
eisbn:
- '9781461439035'
isbn:
- '9781461439028'
publication_status: published
publisher: Springer
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance
the books'
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2012'
...
---
_id: '3405'
abstract:
- lang: eng
text: Glutamate is the major excitatory neurotransmitter in the mammalian central
nervous system and gates non-selective cation channels. The origins of glutamate
receptors are not well understood as they differ structurally and functionally
from simple bacterial ligand-gated ion channels. Here we report the discovery
of an ionotropic glutamate receptor that combines the typical eukaryotic domain
architecture with the 'TXVGYG' signature sequence of the selectivity filter found
in K+ channels. This receptor exhibits functional properties intermediate between
bacterial and eukaryotic glutamate-gated ion channels, suggesting a link in the
evolution of ionotropic glutamate receptors.
author:
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Guillaume
full_name: Sandoz, Guillaume
last_name: Sandoz
- first_name: Ehud
full_name: Isacoff, Ehud
last_name: Isacoff
citation:
ama: Janovjak HL, Sandoz G, Isacoff E. Modern ionotropic glutamate receptor with
a K+ selectivity signature sequence. Nature Communications. 2011;2(232):1-6.
doi:10.1038/ncomms1231
apa: Janovjak, H. L., Sandoz, G., & Isacoff, E. (2011). Modern ionotropic glutamate
receptor with a K+ selectivity signature sequence. Nature Communications.
Nature Publishing Group. https://doi.org/10.1038/ncomms1231
chicago: Janovjak, Harald L, Guillaume Sandoz, and Ehud Isacoff. “Modern Ionotropic
Glutamate Receptor with a K+ Selectivity Signature Sequence.” Nature Communications.
Nature Publishing Group, 2011. https://doi.org/10.1038/ncomms1231.
ieee: H. L. Janovjak, G. Sandoz, and E. Isacoff, “Modern ionotropic glutamate receptor
with a K+ selectivity signature sequence,” Nature Communications, vol.
2, no. 232. Nature Publishing Group, pp. 1–6, 2011.
ista: Janovjak HL, Sandoz G, Isacoff E. 2011. Modern ionotropic glutamate receptor
with a K+ selectivity signature sequence. Nature Communications. 2(232), 1–6.
mla: Janovjak, Harald L., et al. “Modern Ionotropic Glutamate Receptor with a K+
Selectivity Signature Sequence.” Nature Communications, vol. 2, no. 232,
Nature Publishing Group, 2011, pp. 1–6, doi:10.1038/ncomms1231.
short: H.L. Janovjak, G. Sandoz, E. Isacoff, Nature Communications 2 (2011) 1–6.
date_created: 2018-12-11T12:03:09Z
date_published: 2011-03-08T00:00:00Z
date_updated: 2021-01-12T07:43:15Z
day: '08'
ddc:
- '570'
- '571'
department:
- _id: HaJa
doi: 10.1038/ncomms1231
file:
- access_level: open_access
checksum: 6b68d65aadd97c18d663eb117a0a9d35
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:11:36Z
date_updated: 2020-07-14T12:46:12Z
file_id: '4891'
file_name: IST-2017-832-v1+1_janovjak.pdf
file_size: 387654
relation: main_file
file_date_updated: 2020-07-14T12:46:12Z
has_accepted_license: '1'
intvolume: ' 2'
issue: '232'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Submitted Version
page: 1 - 6
publication: Nature Communications
publication_status: published
publisher: Nature Publishing Group
publist_id: '2997'
pubrep_id: '832'
quality_controlled: '1'
scopus_import: 1
status: public
title: Modern ionotropic glutamate receptor with a K+ selectivity signature sequence
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 2
year: '2011'
...