---
_id: '9713'
abstract:
- lang: eng
text: Additional analyses of the trajectories
article_processing_charge: No
author:
- first_name: Chitrak
full_name: Gupta, Chitrak
last_name: Gupta
- first_name: Umesh
full_name: Khaniya, Umesh
last_name: Khaniya
- first_name: Chun Kit
full_name: Chan, Chun Kit
last_name: Chan
- first_name: Francois
full_name: Dehez, Francois
last_name: Dehez
- first_name: Mrinal
full_name: Shekhar, Mrinal
last_name: Shekhar
- first_name: M.R.
full_name: Gunner, M.R.
last_name: Gunner
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: Abhishek
full_name: Singharoy, Abhishek
last_name: Singharoy
citation:
ama: Gupta C, Khaniya U, Chan CK, et al. Supporting information. 2020. doi:10.1021/jacs.9b13450.s001
apa: Gupta, C., Khaniya, U., Chan, C. K., Dehez, F., Shekhar, M., Gunner, M. R.,
… Singharoy, A. (2020). Supporting information. American Chemical Society . https://doi.org/10.1021/jacs.9b13450.s001
chicago: Gupta, Chitrak, Umesh Khaniya, Chun Kit Chan, Francois Dehez, Mrinal Shekhar,
M.R. Gunner, Leonid A Sazanov, Christophe Chipot, and Abhishek Singharoy. “Supporting
Information.” American Chemical Society , 2020. https://doi.org/10.1021/jacs.9b13450.s001.
ieee: C. Gupta et al., “Supporting information.” American Chemical Society
, 2020.
ista: Gupta C, Khaniya U, Chan CK, Dehez F, Shekhar M, Gunner MR, Sazanov LA, Chipot
C, Singharoy A. 2020. Supporting information, American Chemical Society , 10.1021/jacs.9b13450.s001.
mla: Gupta, Chitrak, et al. Supporting Information. American Chemical Society
, 2020, doi:10.1021/jacs.9b13450.s001.
short: C. Gupta, U. Khaniya, C.K. Chan, F. Dehez, M. Shekhar, M.R. Gunner, L.A.
Sazanov, C. Chipot, A. Singharoy, (2020).
date_created: 2021-07-23T12:02:39Z
date_published: 2020-05-20T00:00:00Z
date_updated: 2023-08-22T07:49:38Z
day: '20'
department:
- _id: LeSa
doi: 10.1021/jacs.9b13450.s001
month: '05'
oa_version: Published Version
publisher: 'American Chemical Society '
related_material:
record:
- id: '8040'
relation: used_in_publication
status: public
status: public
title: Supporting information
type: research_data_reference
user_id: 6785fbc1-c503-11eb-8a32-93094b40e1cf
year: '2020'
...
---
_id: '9878'
article_processing_charge: No
author:
- first_name: Chitrak
full_name: Gupta, Chitrak
last_name: Gupta
- first_name: Umesh
full_name: Khaniya, Umesh
last_name: Khaniya
- first_name: Chun Kit
full_name: Chan, Chun Kit
last_name: Chan
- first_name: Francois
full_name: Dehez, Francois
last_name: Dehez
- first_name: Mrinal
full_name: Shekhar, Mrinal
last_name: Shekhar
- first_name: M.R.
full_name: Gunner, M.R.
last_name: Gunner
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: Abhishek
full_name: Singharoy, Abhishek
last_name: Singharoy
citation:
ama: Gupta C, Khaniya U, Chan CK, et al. Movies. 2020. doi:10.1021/jacs.9b13450.s002
apa: Gupta, C., Khaniya, U., Chan, C. K., Dehez, F., Shekhar, M., Gunner, M. R.,
… Singharoy, A. (2020). Movies. American Chemical Society. https://doi.org/10.1021/jacs.9b13450.s002
chicago: Gupta, Chitrak, Umesh Khaniya, Chun Kit Chan, Francois Dehez, Mrinal Shekhar,
M.R. Gunner, Leonid A Sazanov, Christophe Chipot, and Abhishek Singharoy. “Movies.”
American Chemical Society, 2020. https://doi.org/10.1021/jacs.9b13450.s002.
ieee: C. Gupta et al., “Movies.” American Chemical Society, 2020.
ista: Gupta C, Khaniya U, Chan CK, Dehez F, Shekhar M, Gunner MR, Sazanov LA, Chipot
C, Singharoy A. 2020. Movies, American Chemical Society, 10.1021/jacs.9b13450.s002.
mla: Gupta, Chitrak, et al. Movies. American Chemical Society, 2020, doi:10.1021/jacs.9b13450.s002.
short: C. Gupta, U. Khaniya, C.K. Chan, F. Dehez, M. Shekhar, M.R. Gunner, L.A.
Sazanov, C. Chipot, A. Singharoy, (2020).
date_created: 2021-08-11T09:18:54Z
date_published: 2020-05-20T00:00:00Z
date_updated: 2023-08-22T07:49:38Z
day: '20'
department:
- _id: LeSa
doi: 10.1021/jacs.9b13450.s002
month: '05'
oa_version: Published Version
publisher: American Chemical Society
related_material:
record:
- id: '8040'
relation: used_in_publication
status: public
status: public
title: Movies
type: research_data_reference
user_id: 6785fbc1-c503-11eb-8a32-93094b40e1cf
year: '2020'
...
---
_id: '8318'
abstract:
- lang: eng
text: Complex I is the first and the largest enzyme of respiratory chains in bacteria
and mitochondria. The mechanism which couples spatially separated transfer of
electrons to proton translocation in complex I is not known. Here we report five
crystal structures of T. thermophilus enzyme in complex with NADH or quinone-like
compounds. We also determined cryo-EM structures of major and minor native states
of the complex, differing in the position of the peripheral arm. Crystal structures
show that binding of quinone-like compounds (but not of NADH) leads to a related
global conformational change, accompanied by local re-arrangements propagating
from the quinone site to the nearest proton channel. Normal mode and molecular
dynamics analyses indicate that these are likely to represent the first steps
in the proton translocation mechanism. Our results suggest that quinone binding
and chemistry play a key role in the coupling mechanism of complex I.
acknowledgement: This work was funded by the Medical Research Council, UK and IST
Austria. We thank the European Synchrotron Radiation Facility and the Diamond Light
Source for provision of synchrotron radiation facilities. We are grateful to the
staff of beamlines ID29, ID23-2 (ESRF, Grenoble, France) and I03 (Diamond Light
Source, Didcot, UK) for assistance. Data processing was performed at the IST high-performance
computing cluster.
article_number: '4135'
article_processing_charge: No
article_type: original
author:
- first_name: Javier
full_name: Gutierrez-Fernandez, Javier
id: 3D9511BA-F248-11E8-B48F-1D18A9856A87
last_name: Gutierrez-Fernandez
- first_name: Karol
full_name: Kaszuba, Karol
id: 3FDF9472-F248-11E8-B48F-1D18A9856A87
last_name: Kaszuba
- first_name: Gurdeep S.
full_name: Minhas, Gurdeep S.
last_name: Minhas
- first_name: Rozbeh
full_name: Baradaran, Rozbeh
last_name: Baradaran
- first_name: Margherita
full_name: Tambalo, Margherita
id: 4187dfe4-ec23-11ea-ae46-f08ab378313a
last_name: Tambalo
- first_name: David T.
full_name: Gallagher, David T.
last_name: Gallagher
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Gutierrez-Fernandez J, Kaszuba K, Minhas GS, et al. Key role of quinone in
the mechanism of respiratory complex I. Nature Communications. 2020;11(1).
doi:10.1038/s41467-020-17957-0
apa: Gutierrez-Fernandez, J., Kaszuba, K., Minhas, G. S., Baradaran, R., Tambalo,
M., Gallagher, D. T., & Sazanov, L. A. (2020). Key role of quinone in the
mechanism of respiratory complex I. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-020-17957-0
chicago: Gutierrez-Fernandez, Javier, Karol Kaszuba, Gurdeep S. Minhas, Rozbeh Baradaran,
Margherita Tambalo, David T. Gallagher, and Leonid A Sazanov. “Key Role of Quinone
in the Mechanism of Respiratory Complex I.” Nature Communications. Springer
Nature, 2020. https://doi.org/10.1038/s41467-020-17957-0.
ieee: J. Gutierrez-Fernandez et al., “Key role of quinone in the mechanism
of respiratory complex I,” Nature Communications, vol. 11, no. 1. Springer
Nature, 2020.
ista: Gutierrez-Fernandez J, Kaszuba K, Minhas GS, Baradaran R, Tambalo M, Gallagher
DT, Sazanov LA. 2020. Key role of quinone in the mechanism of respiratory complex
I. Nature Communications. 11(1), 4135.
mla: Gutierrez-Fernandez, Javier, et al. “Key Role of Quinone in the Mechanism of
Respiratory Complex I.” Nature Communications, vol. 11, no. 1, 4135, Springer
Nature, 2020, doi:10.1038/s41467-020-17957-0.
short: J. Gutierrez-Fernandez, K. Kaszuba, G.S. Minhas, R. Baradaran, M. Tambalo,
D.T. Gallagher, L.A. Sazanov, Nature Communications 11 (2020).
date_created: 2020-08-30T22:01:10Z
date_published: 2020-08-18T00:00:00Z
date_updated: 2023-08-22T09:03:00Z
day: '18'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1038/s41467-020-17957-0
external_id:
isi:
- '000607072900001'
pmid:
- '32811817'
file:
- access_level: open_access
checksum: 52b96f41d7d0db9728064c08da00d030
content_type: application/pdf
creator: cziletti
date_created: 2020-08-31T13:40:00Z
date_updated: 2020-08-31T13:40:00Z
file_id: '8326'
file_name: 2020_NatComm_Gutierrez-Fernandez.pdf
file_size: 7527373
relation: main_file
success: 1
file_date_updated: 2020-08-31T13:40:00Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
issue: '1'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
eissn:
- '20411723'
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/mystery-of-giant-proton-pump-solved/
scopus_import: '1'
status: public
title: Key role of quinone in the mechanism of respiratory complex I
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 11
year: '2020'
...
---
_id: '8579'
abstract:
- lang: eng
text: Copper (Cu) is an essential trace element for all living organisms and used
as cofactor in key enzymes of important biological processes, such as aerobic
respiration or superoxide dismutation. However, due to its toxicity, cells have
developed elaborate mechanisms for Cu homeostasis, which balance Cu supply for
cuproprotein biogenesis with the need to remove excess Cu. This review summarizes
our current knowledge on bacterial Cu homeostasis with a focus on Gram-negative
bacteria and describes the multiple strategies that bacteria use for uptake, storage
and export of Cu. We furthermore describe general mechanistic principles that
aid the bacterial response to toxic Cu concentrations and illustrate dedicated
Cu relay systems that facilitate Cu delivery for cuproenzyme biogenesis. Progress
in understanding how bacteria avoid Cu poisoning while maintaining a certain Cu
quota for cell proliferation is of particular importance for microbial pathogens
because Cu is utilized by the host immune system for attenuating pathogen survival
in host cells.
article_number: '242'
article_processing_charge: No
article_type: original
author:
- first_name: Andreea
full_name: Andrei, Andreea
last_name: Andrei
- first_name: Yavuz
full_name: Öztürk, Yavuz
last_name: Öztürk
- first_name: Bahia
full_name: Khalfaoui-Hassani, Bahia
last_name: Khalfaoui-Hassani
- first_name: Juna
full_name: Rauch, Juna
last_name: Rauch
- first_name: Dorian
full_name: Marckmann, Dorian
last_name: Marckmann
- first_name: Petru Iulian
full_name: Trasnea, Petru Iulian
id: D560034C-10C4-11EA-ABF4-A4B43DDC885E
last_name: Trasnea
- first_name: Fevzi
full_name: Daldal, Fevzi
last_name: Daldal
- first_name: Hans-Georg
full_name: Koch, Hans-Georg
last_name: Koch
citation:
ama: 'Andrei A, Öztürk Y, Khalfaoui-Hassani B, et al. Cu homeostasis in bacteria:
The ins and outs. Membranes. 2020;10(9). doi:10.3390/membranes10090242'
apa: 'Andrei, A., Öztürk, Y., Khalfaoui-Hassani, B., Rauch, J., Marckmann, D., Trasnea,
P. I., … Koch, H.-G. (2020). Cu homeostasis in bacteria: The ins and outs. Membranes.
MDPI. https://doi.org/10.3390/membranes10090242'
chicago: 'Andrei, Andreea, Yavuz Öztürk, Bahia Khalfaoui-Hassani, Juna Rauch, Dorian
Marckmann, Petru Iulian Trasnea, Fevzi Daldal, and Hans-Georg Koch. “Cu Homeostasis
in Bacteria: The Ins and Outs.” Membranes. MDPI, 2020. https://doi.org/10.3390/membranes10090242.'
ieee: 'A. Andrei et al., “Cu homeostasis in bacteria: The ins and outs,”
Membranes, vol. 10, no. 9. MDPI, 2020.'
ista: 'Andrei A, Öztürk Y, Khalfaoui-Hassani B, Rauch J, Marckmann D, Trasnea PI,
Daldal F, Koch H-G. 2020. Cu homeostasis in bacteria: The ins and outs. Membranes.
10(9), 242.'
mla: 'Andrei, Andreea, et al. “Cu Homeostasis in Bacteria: The Ins and Outs.” Membranes,
vol. 10, no. 9, 242, MDPI, 2020, doi:10.3390/membranes10090242.'
short: A. Andrei, Y. Öztürk, B. Khalfaoui-Hassani, J. Rauch, D. Marckmann, P.I.
Trasnea, F. Daldal, H.-G. Koch, Membranes 10 (2020).
date_created: 2020-09-28T08:59:26Z
date_published: 2020-09-01T00:00:00Z
date_updated: 2023-08-22T09:34:06Z
day: '01'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.3390/membranes10090242
external_id:
isi:
- '000581446000001'
file:
- access_level: open_access
checksum: ceb43d7554e712dea6f36f9287271737
content_type: application/pdf
creator: dernst
date_created: 2020-09-28T11:36:50Z
date_updated: 2020-09-28T11:36:50Z
file_id: '8583'
file_name: 2020_Membranes_Andrei.pdf
file_size: 4612258
relation: main_file
success: 1
file_date_updated: 2020-09-28T11:36:50Z
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: Membranes
publication_identifier:
eissn:
- '20770375'
publication_status: published
publisher: MDPI
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Cu homeostasis in bacteria: The ins and outs'
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 10
year: '2020'
...
---
_id: '8581'
abstract:
- lang: eng
text: The majority of adenosine triphosphate (ATP) powering cellular processes in
eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present
the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo,
determined by cryo-electron microscopy. Subunits in the membrane domain are arranged
in the ‘proton translocation cluster’ attached to the c-ring and a more distant
‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to
a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation
pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM
maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled
c-ring, suggesting permeability transition pore opening. We propose a model for
the permeability transition pore opening, whereby subunit e pulls the lipid plug
out of the c-ring. Our structure will allow the design of drugs for many emerging
applications in medicine.
acknowledged_ssus:
- _id: EM-Fac
- _id: ScienComp
acknowledgement: We thank J. Novacek from CEITEC (Brno, Czech Republic) for assistance
with collecting the FEI Krios dataset and iNEXT for providing access to CEITEC.
We thank the IST Austria EM facility for access and assistance with collecting the
FEI Glacios dataset. Data processing was performed at the IST high-performance computing
cluster. This work has been supported by iNEXT EM HEDC (proposal 4506), funded by
the Horizon 2020 Programme of the European Commission.
article_processing_charge: No
article_type: original
author:
- first_name: Gergely
full_name: Pinke, Gergely
id: 4D5303E6-F248-11E8-B48F-1D18A9856A87
last_name: Pinke
- first_name: Long
full_name: Zhou, Long
id: 3E751364-F248-11E8-B48F-1D18A9856A87
last_name: Zhou
orcid: 0000-0002-1864-8951
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Pinke G, Zhou L, Sazanov LA. Cryo-EM structure of the entire mammalian F-type
ATP synthase. Nature Structural and Molecular Biology. 2020;27(11):1077-1085.
doi:10.1038/s41594-020-0503-8
apa: Pinke, G., Zhou, L., & Sazanov, L. A. (2020). Cryo-EM structure of the
entire mammalian F-type ATP synthase. Nature Structural and Molecular Biology.
Springer Nature. https://doi.org/10.1038/s41594-020-0503-8
chicago: Pinke, Gergely, Long Zhou, and Leonid A Sazanov. “Cryo-EM Structure of
the Entire Mammalian F-Type ATP Synthase.” Nature Structural and Molecular
Biology. Springer Nature, 2020. https://doi.org/10.1038/s41594-020-0503-8.
ieee: G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian
F-type ATP synthase,” Nature Structural and Molecular Biology, vol. 27,
no. 11. Springer Nature, pp. 1077–1085, 2020.
ista: Pinke G, Zhou L, Sazanov LA. 2020. Cryo-EM structure of the entire mammalian
F-type ATP synthase. Nature Structural and Molecular Biology. 27(11), 1077–1085.
mla: Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP
Synthase.” Nature Structural and Molecular Biology, vol. 27, no. 11, Springer
Nature, 2020, pp. 1077–85, doi:10.1038/s41594-020-0503-8.
short: G. Pinke, L. Zhou, L.A. Sazanov, Nature Structural and Molecular Biology
27 (2020) 1077–1085.
date_created: 2020-09-28T08:59:27Z
date_published: 2020-11-01T00:00:00Z
date_updated: 2023-08-22T09:33:09Z
day: '01'
department:
- _id: LeSa
doi: 10.1038/s41594-020-0503-8
external_id:
isi:
- '000569299400004'
pmid:
- '32929284'
intvolume: ' 27'
isi: 1
issue: '11'
language:
- iso: eng
month: '11'
oa_version: None
page: 1077-1085
pmid: 1
publication: Nature Structural and Molecular Biology
publication_identifier:
eissn:
- '15459985'
issn:
- '15459993'
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/structure-of-atpase-solved/
scopus_import: '1'
status: public
title: Cryo-EM structure of the entire mammalian F-type ATP synthase
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 27
year: '2020'
...
---
_id: '8737'
abstract:
- lang: eng
text: Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping
by an unknown mechanism. Here, we present cryo-electron microscopy structures
of ovine complex I in five different conditions, including turnover, at resolutions
up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally
define the proton translocation pathways. Quinone binds at three positions along
the quinone cavity, as does the inhibitor rotenone that also binds within subunit
ND4. Dramatic conformational changes around the quinone cavity couple the redox
reaction to proton translocation during open-to-closed state transitions of the
enzyme. In the induced deactive state, the open conformation is arrested by the
ND6 subunit. We propose a detailed molecular coupling mechanism of complex I,
which is an unexpected combination of conformational changes and electrostatic
interactions.
acknowledged_ssus:
- _id: LifeSc
- _id: EM-Fac
acknowledgement: We thank J. Novacek (CEITEC Brno) and V.-V. Hodirnau (IST Austria)
for their help with collecting cryo-EM datasets. We thank the IST Life Science and
Electron Microscopy Facilities for providing equipment. This work has been supported
by iNEXT,project number 653706, funded by the Horizon 2020 program of the European
Union. This article reflects only the authors’view,and the European Commission is
not responsible for any use that may be made of the information it contains. CIISB
research infrastructure project LM2015043 funded by MEYS CR is gratefully acknowledged
for the financial support of the measurements at the CF Cryo-electron Microscopy
and Tomography CEITEC MU.This project has received funding from the European Union’s
Horizon 2020 research and innovation program under the Marie Skłodowska-Curie Grant
Agreement no. 665385
article_number: eabc4209
article_processing_charge: No
article_type: original
author:
- first_name: Domen
full_name: Kampjut, Domen
id: 37233050-F248-11E8-B48F-1D18A9856A87
last_name: Kampjut
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Kampjut D, Sazanov LA. The coupling mechanism of mammalian respiratory complex
I. Science. 2020;370(6516). doi:10.1126/science.abc4209
apa: Kampjut, D., & Sazanov, L. A. (2020). The coupling mechanism of mammalian
respiratory complex I. Science. American Association for the Advancement
of Science. https://doi.org/10.1126/science.abc4209
chicago: Kampjut, Domen, and Leonid A Sazanov. “The Coupling Mechanism of Mammalian
Respiratory Complex I.” Science. American Association for the Advancement
of Science, 2020. https://doi.org/10.1126/science.abc4209.
ieee: D. Kampjut and L. A. Sazanov, “The coupling mechanism of mammalian respiratory
complex I,” Science, vol. 370, no. 6516. American Association for the Advancement
of Science, 2020.
ista: Kampjut D, Sazanov LA. 2020. The coupling mechanism of mammalian respiratory
complex I. Science. 370(6516), eabc4209.
mla: Kampjut, Domen, and Leonid A. Sazanov. “The Coupling Mechanism of Mammalian
Respiratory Complex I.” Science, vol. 370, no. 6516, eabc4209, American
Association for the Advancement of Science, 2020, doi:10.1126/science.abc4209.
short: D. Kampjut, L.A. Sazanov, Science 370 (2020).
date_created: 2020-11-08T23:01:23Z
date_published: 2020-10-30T00:00:00Z
date_updated: 2023-08-22T12:35:38Z
day: '30'
ddc:
- '572'
department:
- _id: LeSa
doi: 10.1126/science.abc4209
ec_funded: 1
external_id:
isi:
- '000583031800004'
pmid:
- '32972993'
file:
- access_level: open_access
checksum: 658ba90979ca9528a2efdfac8547047a
content_type: application/pdf
creator: lsazanov
date_created: 2020-11-26T18:47:58Z
date_updated: 2020-11-26T18:47:58Z
file_id: '8820'
file_name: Full_manuscript_with_SI_opt_red.pdf
file_size: 7618987
relation: main_file
success: 1
file_date_updated: 2020-11-26T18:47:58Z
has_accepted_license: '1'
intvolume: ' 370'
isi: 1
issue: '6516'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
pmid: 1
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
publication: Science
publication_identifier:
eissn:
- '10959203'
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: The coupling mechanism of mammalian respiratory complex I
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 370
year: '2020'
...
---
_id: '8353'
abstract:
- lang: eng
text: "Mrp (Multi resistance and pH adaptation) are broadly distributed secondary
active antiporters that catalyze the transport of monovalent ions such as sodium
and potassium outside of the cell coupled to the inward translocation of protons.
Mrp antiporters are unique in a way that they are composed of seven subunits (MrpABCDEFG)
encoded in a single operon, whereas other antiporters catalyzing the same reaction
are mostly encoded by a single gene. Mrp exchangers are crucial for intracellular
pH homeostasis and Na+ efflux, essential mechanisms for H+ uptake under alkaline
environments and for reduction of the intracellular concentration of toxic cations.
Mrp displays no homology to any other monovalent Na+(K+)/H+ antiporters but Mrp
subunits have primary sequence similarity to essential redox-driven proton pumps,
such as respiratory complex I and membrane-bound hydrogenases. This similarity
reinforces the hypothesis that these present day redox-driven proton pumps are
descended from the Mrp antiporter. The Mrp structure serves as a model to understand
the yet obscure coupling mechanism between ion or electron transfer and proton
translocation in this large group of proteins. In the thesis, I am presenting
the purification, biochemical analysis, cryo-EM analysis and molecular structure
of the Mrp complex from Anoxybacillus flavithermus solved by cryo-EM at 3.0 Å
resolution. Numerous conditions were screened to purify Mrp to high homogeneity
and to obtain an appropriate distribution of single particles on cryo-EM grids
covered with a continuous layer of ultrathin carbon. A preferred particle orientation
problem was solved by performing a tilted data collection. The activity assays
showed the specific pH-dependent\r\nprofile of secondary active antiporters. The
molecular structure shows that Mrp is a dimer of seven-subunit protomers with
50 trans-membrane helices each. The dimer interface is built by many short and
tilted transmembrane helices, probably causing a thinning of the bacterial membrane.
The surface charge distribution shows an extraordinary asymmetry within each monomer,
revealing presumable proton and sodium translocation pathways. The two largest\r\nand
homologous Mrp subunits MrpA and MrpD probably translocate one proton each into
the cell. The sodium ion is likely being translocated in the opposite direction
within the small subunits along a ladder of charged and conserved residues. Based
on the structure, we propose a mechanism were the antiport activity is accomplished
via electrostatic interactions between the charged cations and key charged residues.
The flexible key TM helices coordinate these\r\nelectrostatic interactions, while
the membrane thinning between the monomers enables the translocation of sodium
across the charged membrane. The entire family of redox-driven proton pumps is
likely to perform their mechanism in a likewise manner."
acknowledged_ssus:
- _id: LifeSc
- _id: EM-Fac
- _id: ScienComp
acknowledgement: "I acknowledge the scientific service units of the IST Austria for
providing resources by the Life Science Facility, the Electron Microscopy Facility
and the high-performance computer cluster. Special thanks to the cryo-EM specialists
Valentin Hodirnau and Daniel Johann Gütl for spending many hours with me in front
of the microscope and for supporting me to collect the data presented here. I also
want to thank Professor Masahiro Ito for providing plasmid DNA\r\nencoding Mrp from
Anoxybacillus flavithermus WK1. I am a recipient of a DOC Fellowship of the Austrian
Academy of Sciences."
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Julia
full_name: Steiner, Julia
id: 3BB67EB0-F248-11E8-B48F-1D18A9856A87
last_name: Steiner
orcid: 0000-0003-0493-3775
citation:
ama: Steiner J. Biochemical and structural investigation of the Mrp antiporter,
an ancestor of complex I. 2020. doi:10.15479/AT:ISTA:8353
apa: Steiner, J. (2020). Biochemical and structural investigation of the Mrp
antiporter, an ancestor of complex I. Institute of Science and Technology
Austria. https://doi.org/10.15479/AT:ISTA:8353
chicago: Steiner, Julia. “Biochemical and Structural Investigation of the Mrp Antiporter,
an Ancestor of Complex I.” Institute of Science and Technology Austria, 2020.
https://doi.org/10.15479/AT:ISTA:8353.
ieee: J. Steiner, “Biochemical and structural investigation of the Mrp antiporter,
an ancestor of complex I,” Institute of Science and Technology Austria, 2020.
ista: Steiner J. 2020. Biochemical and structural investigation of the Mrp antiporter,
an ancestor of complex I. Institute of Science and Technology Austria.
mla: Steiner, Julia. Biochemical and Structural Investigation of the Mrp Antiporter,
an Ancestor of Complex I. Institute of Science and Technology Austria, 2020,
doi:10.15479/AT:ISTA:8353.
short: J. Steiner, Biochemical and Structural Investigation of the Mrp Antiporter,
an Ancestor of Complex I, Institute of Science and Technology Austria, 2020.
date_created: 2020-09-09T14:27:01Z
date_published: 2020-09-09T00:00:00Z
date_updated: 2023-09-07T13:14:09Z
day: '09'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: LeSa
doi: 10.15479/AT:ISTA:8353
file:
- access_level: open_access
checksum: 2388d7e6e7a4d364c096fa89f305c3de
content_type: application/pdf
creator: jsteiner
date_created: 2020-09-09T14:22:35Z
date_updated: 2021-09-16T12:40:56Z
file_id: '8354'
file_name: Thesis_Julia_Steiner_pdfA.pdf
file_size: 117547589
relation: main_file
- access_level: closed
checksum: ba112f957b7145462d0ab79044873ee9
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: jsteiner
date_created: 2020-09-09T14:23:25Z
date_updated: 2020-09-15T08:48:37Z
file_id: '8355'
file_name: Thesis_Julia_Steiner.docx
file_size: 223328668
relation: source_file
file_date_updated: 2021-09-16T12:40:56Z
has_accepted_license: '1'
language:
- iso: eng
month: '09'
oa: 1
oa_version: None
page: '191'
project:
- _id: 26169496-B435-11E9-9278-68D0E5697425
grant_number: '24741'
name: Revealing the functional mechanism of Mrp antiporter, an ancestor of complex
I
publication_identifier:
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '8284'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
title: Biochemical and structural investigation of the Mrp antiporter, an ancestor
of complex I
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2020'
...
---
_id: '8284'
abstract:
- lang: eng
text: Multiple resistance and pH adaptation (Mrp) antiporters are multi-subunit
Na+ (or K+)/H+ exchangers representing an ancestor of many essential redox-driven
proton pumps, such as respiratory complex I. The mechanism of coupling between
ion or electron transfer and proton translocation in this large protein family
is unknown. Here, we present the structure of the Mrp complex from Anoxybacillus
flavithermus solved by cryo-EM at 3.0 Å resolution. It is a dimer of seven-subunit
protomers with 50 trans-membrane helices each. Surface charge distribution within
each monomer is remarkably asymmetric, revealing probable proton and sodium translocation
pathways. On the basis of the structure we propose a mechanism where the coupling
between sodium and proton translocation is facilitated by a series of electrostatic
interactions between a cation and key charged residues. This mechanism is likely
to be applicable to the entire family of redox proton pumps, where electron transfer
to substrates replaces cation movements.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
acknowledgement: This research was supported by the Scientific Service Units (SSU)
of IST Austria through resources provided by the Electron Microscopy Facility (EMF),
the Life Science Facility (LSF) and the IST high-performance computing cluster.
We thank Dr Victor-Valentin Hodirnau and Daniel Johann Gütl from IST Austria for
assistance with collecting cryo-EM data. We thank Prof. Masahiro Ito (Graduate School
of Life Sciences, Toyo University, Japan) for a kind provision of plasmid DNA encoding
Mrp from A. flavithermus WK1. JS is a recipient of a DOC Fellowship of the Austrian
Academy of Sciences at the Institute of Science and Technology, Austria.
article_number: e59407
article_processing_charge: No
article_type: original
author:
- first_name: Julia
full_name: Steiner, Julia
id: 3BB67EB0-F248-11E8-B48F-1D18A9856A87
last_name: Steiner
orcid: 0000-0003-0493-3775
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Steiner J, Sazanov LA. Structure and mechanism of the Mrp complex, an ancient
cation/proton antiporter. eLife. 2020;9. doi:10.7554/eLife.59407
apa: Steiner, J., & Sazanov, L. A. (2020). Structure and mechanism of the Mrp
complex, an ancient cation/proton antiporter. ELife. eLife Sciences Publications.
https://doi.org/10.7554/eLife.59407
chicago: Steiner, Julia, and Leonid A Sazanov. “Structure and Mechanism of the Mrp
Complex, an Ancient Cation/Proton Antiporter.” ELife. eLife Sciences Publications,
2020. https://doi.org/10.7554/eLife.59407.
ieee: J. Steiner and L. A. Sazanov, “Structure and mechanism of the Mrp complex,
an ancient cation/proton antiporter,” eLife, vol. 9. eLife Sciences Publications,
2020.
ista: Steiner J, Sazanov LA. 2020. Structure and mechanism of the Mrp complex, an
ancient cation/proton antiporter. eLife. 9, e59407.
mla: Steiner, Julia, and Leonid A. Sazanov. “Structure and Mechanism of the Mrp
Complex, an Ancient Cation/Proton Antiporter.” ELife, vol. 9, e59407, eLife
Sciences Publications, 2020, doi:10.7554/eLife.59407.
short: J. Steiner, L.A. Sazanov, ELife 9 (2020).
date_created: 2020-08-24T06:24:04Z
date_published: 2020-07-31T00:00:00Z
date_updated: 2023-09-07T13:14:08Z
day: '31'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.7554/eLife.59407
external_id:
isi:
- '000562123600001'
pmid:
- '32735215'
file:
- access_level: open_access
checksum: b3656d14d5ddbb9d26e3074eea2d0c15
content_type: application/pdf
creator: cziletti
date_created: 2020-08-24T13:31:53Z
date_updated: 2020-08-24T13:31:53Z
file_id: '8289'
file_name: 2020_eLife_Steiner.pdf
file_size: 7320493
relation: main_file
success: 1
file_date_updated: 2020-08-24T13:31:53Z
has_accepted_license: '1'
intvolume: ' 9'
isi: 1
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26169496-B435-11E9-9278-68D0E5697425
grant_number: '24741'
name: Revealing the functional mechanism of Mrp antiporter, an ancestor of complex
I
publication: eLife
publication_identifier:
eissn:
- 2050084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/mystery-of-giant-proton-pump-solved/
record:
- id: '8353'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 9
year: '2020'
...
---
_id: '8340'
abstract:
- lang: eng
text: Mitochondria are sites of oxidative phosphorylation in eukaryotic cells. Oxidative
phosphorylation operates by a chemiosmotic mechanism made possible by redox-driven
proton pumping machines which establish a proton motive force across the inner
mitochondrial membrane. This electrochemical proton gradient is used to drive
ATP synthesis, which powers the majority of cellular processes such as protein
synthesis, locomotion and signalling. In this thesis I investigate the structures
and molecular mechanisms of two inner mitochondrial proton pumping enzymes, respiratory
complex I and transhydrogenase. I present the first high-resolution structure
of the full transhydrogenase from any species, and a significantly improved structure
of complex I. Improving the resolution from 3.3 Å available previously to up to
2.3 Å in this thesis allowed us to model bound water molecules, crucial in the
proton pumping mechanism. For both enzymes, up to five cryo-EM datasets with different
substrates and inhibitors bound were solved to delineate the catalytic cycle and
understand the proton pumping mechanism. In transhydrogenase, the proton channel
is gated by reversible detachment of the NADP(H)-binding domain which opens the
proton channel to the opposite sites of the membrane. In complex I, the proton
channels are gated by reversible protonation of key glutamate and lysine residues
and breaking of the water wire connecting the proton pumps with the quinone reduction
site. The tight coupling between the redox and the proton pumping reactions in
transhydrogenase is achieved by controlling the NADP(H) exchange which can only
happen when the NADP(H)-binding domain interacts with the membrane domain. In
complex I, coupling is achieved by cycling of the whole complex between the closed
state, in which quinone can get reduced, and the open state, in which NADH can
induce quinol ejection from the binding pocket. On the basis of these results
I propose detailed mechanisms for catalytic cycles of transhydrogenase and complex
I that are consistent with a large amount of previous work. In both enzymes, conformational
and electrostatic mechanisms contribute to the overall catalytic process. Results
presented here could be used for better understanding of the human pathologies
arising from deficiencies of complex I or transhydrogenase and could be used to
develop novel therapies.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: 'I acknowledge the support of IST facilities, especially the Electron
Miscroscopy facility for providing training and resources. Special thanks also go
to cryo-EM specialists who helped me to collect the data present here: Dr Valentin
Hodirnau (IST Austria), Dr Tom Heuser (IMBA, Vienna), Dr Rebecca Thompson (Uni.
of Leeds) and Dr Jirka Nováček (CEITEC). This work has been supported by iNEXT,
project number 653706, funded by the Horizon 2020 programme of the European Union.
This project has received funding from the European Union’s Horizon 2020 research
and innovation programme under the Marie Skłodowska-Curie Grant Agreement No. 665385.'
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Domen
full_name: Kampjut, Domen
id: 37233050-F248-11E8-B48F-1D18A9856A87
last_name: Kampjut
citation:
ama: Kampjut D. Molecular mechanisms of mitochondrial redox-coupled proton pumping
enzymes. 2020. doi:10.15479/AT:ISTA:8340
apa: Kampjut, D. (2020). Molecular mechanisms of mitochondrial redox-coupled
proton pumping enzymes. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:8340
chicago: Kampjut, Domen. “Molecular Mechanisms of Mitochondrial Redox-Coupled Proton
Pumping Enzymes.” Institute of Science and Technology Austria, 2020. https://doi.org/10.15479/AT:ISTA:8340.
ieee: D. Kampjut, “Molecular mechanisms of mitochondrial redox-coupled proton pumping
enzymes,” Institute of Science and Technology Austria, 2020.
ista: Kampjut D. 2020. Molecular mechanisms of mitochondrial redox-coupled proton
pumping enzymes. Institute of Science and Technology Austria.
mla: Kampjut, Domen. Molecular Mechanisms of Mitochondrial Redox-Coupled Proton
Pumping Enzymes. Institute of Science and Technology Austria, 2020, doi:10.15479/AT:ISTA:8340.
short: D. Kampjut, Molecular Mechanisms of Mitochondrial Redox-Coupled Proton Pumping
Enzymes, Institute of Science and Technology Austria, 2020.
date_created: 2020-09-07T18:42:23Z
date_published: 2020-09-09T00:00:00Z
date_updated: 2023-09-07T13:26:17Z
day: '09'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: LeSa
doi: 10.15479/AT:ISTA:8340
ec_funded: 1
file:
- access_level: closed
checksum: dd270baf82121eb4472ad19d77bf227c
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: dkampjut
date_created: 2020-09-08T13:32:06Z
date_updated: 2021-09-11T22:30:04Z
embargo_to: open_access
file_id: '8345'
file_name: ThesisFull20200908.docx
file_size: 166146359
relation: source_file
- access_level: open_access
checksum: 82fce6f95ffa47ecc4ebca67ea2cc38c
content_type: application/pdf
creator: dernst
date_created: 2020-09-14T15:02:20Z
date_updated: 2021-09-11T22:30:04Z
embargo: 2021-09-10
file_id: '8393'
file_name: 2020_Thesis_Kampjut.pdf
file_size: 13873769
relation: main_file
file_date_updated: 2021-09-11T22:30:04Z
has_accepted_license: '1'
language:
- iso: eng
month: '09'
oa: 1
oa_version: None
page: '242'
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
publication_identifier:
isbn:
- 978-3-99078-008-4
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '6848'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
title: Molecular mechanisms of mitochondrial redox-coupled proton pumping enzymes
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2020'
...
---
_id: '6352'
abstract:
- lang: eng
text: Chronic overuse of common pharmaceuticals, e.g. acetaminophen (paracetamol),
often leads to the development of acute liver failure (ALF). This study aimed
to elucidate the effect of cultured mesenchymal stem cells (MSCs) proteome on
the onset of liver damage and regeneration dynamics in animals with ALF induced
by acetaminophen, to test the liver protective efficacy of MSCs proteome depending
on the oxygen tension in cell culture, and to blueprint protein components responsible
for the effect. Protein compositions prepared from MSCs cultured in mild hypoxic
(5% and 10% O2) and normal (21% O2) conditions were used to treat ALF induced
in mice by injection of acetaminophen. To test the effect of reduced oxygen tension
in cell culture on resulting MSCs proteome content we applied a combination of
high performance liquid chromatography and mass-spectrometry (LC–MS/MS) for the
identification of proteins in lysates of MSCs cultured at different O2 levels.
The treatment of acetaminophen-administered animals with proteins released from
cultured MSCs resulted in the inhibition of inflammatory reactions in damaged
liver; the area of hepatocyte necrosis being reduced in the first 24 h. Compositions
obtained from MSCs cultured at lower O2 level were shown to be more potent than
a composition prepared from normoxic cells. A comparative characterization of
protein pattern and identification of individual components done by a cytokine
assay and proteomics analysis of protein compositions revealed that even moderate
hypoxia produces discrete changes in the expression of various subsets of proteins
responsible for intracellular respiration and cell signaling. The application
of proteins prepared from MSCs grown in vitro at reduced oxygen tension significantly
accelerates healing process in damaged liver tissue. The proteomics data obtained
for different preparations offer new information about the potential candidates
in the MSCs protein repertoire sensitive to oxygen tension in culture medium,
which can be involved in the generalized mechanisms the cells use to respond to
acute liver failure.
acknowledgement: The studies were supported by the Austrian Federal Ministry of Economy,
Family and Youth through the initiative “Laura Bassi Centres of Expertise” funding
the Center of Optimized Structural Stud-ies, grant No. 253275
article_processing_charge: Yes (via OA deal)
author:
- first_name: Andrey Alexandrovich
full_name: Temnov, Andrey Alexandrovich
last_name: Temnov
- first_name: Konstantin Arkadevich
full_name: Rogov, Konstantin Arkadevich
last_name: Rogov
- first_name: Alla Nikolaevna
full_name: Sklifas, Alla Nikolaevna
last_name: Sklifas
- first_name: Elena Valerievna
full_name: Klychnikova, Elena Valerievna
last_name: Klychnikova
- first_name: Markus
full_name: Hartl, Markus
last_name: Hartl
- first_name: Kristina
full_name: Djinovic-Carugo, Kristina
last_name: Djinovic-Carugo
- first_name: Alexej
full_name: Charnagalov, Alexej
id: 49F06DBA-F248-11E8-B48F-1D18A9856A87
last_name: Charnagalov
citation:
ama: Temnov AA, Rogov KA, Sklifas AN, et al. Protective properties of the cultured
stem cell proteome studied in an animal model of acetaminophen-induced acute liver
failure. Molecular Biology Reports. 2019. doi:10.1007/s11033-019-04765-z
apa: Temnov, A. A., Rogov, K. A., Sklifas, A. N., Klychnikova, E. V., Hartl, M.,
Djinovic-Carugo, K., & Charnagalov, A. (2019). Protective properties of the
cultured stem cell proteome studied in an animal model of acetaminophen-induced
acute liver failure. Molecular Biology Reports. Springer. https://doi.org/10.1007/s11033-019-04765-z
chicago: Temnov, Andrey Alexandrovich, Konstantin Arkadevich Rogov, Alla Nikolaevna
Sklifas, Elena Valerievna Klychnikova, Markus Hartl, Kristina Djinovic-Carugo,
and Alexej Charnagalov. “Protective Properties of the Cultured Stem Cell Proteome
Studied in an Animal Model of Acetaminophen-Induced Acute Liver Failure.” Molecular
Biology Reports. Springer, 2019. https://doi.org/10.1007/s11033-019-04765-z.
ieee: A. A. Temnov et al., “Protective properties of the cultured stem cell
proteome studied in an animal model of acetaminophen-induced acute liver failure,”
Molecular Biology Reports. Springer, 2019.
ista: Temnov AA, Rogov KA, Sklifas AN, Klychnikova EV, Hartl M, Djinovic-Carugo
K, Charnagalov A. 2019. Protective properties of the cultured stem cell proteome
studied in an animal model of acetaminophen-induced acute liver failure. Molecular
Biology Reports.
mla: Temnov, Andrey Alexandrovich, et al. “Protective Properties of the Cultured
Stem Cell Proteome Studied in an Animal Model of Acetaminophen-Induced Acute Liver
Failure.” Molecular Biology Reports, Springer, 2019, doi:10.1007/s11033-019-04765-z.
short: A.A. Temnov, K.A. Rogov, A.N. Sklifas, E.V. Klychnikova, M. Hartl, K. Djinovic-Carugo,
A. Charnagalov, Molecular Biology Reports (2019).
date_created: 2019-04-28T21:59:14Z
date_published: 2019-04-12T00:00:00Z
date_updated: 2023-08-25T10:14:26Z
day: '12'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1007/s11033-019-04765-z
external_id:
isi:
- '000470332600049'
file:
- access_level: open_access
checksum: 45bf040bbce1cea274f6013fa18ba21b
content_type: application/pdf
creator: dernst
date_created: 2019-04-30T09:52:36Z
date_updated: 2020-07-14T12:47:28Z
file_id: '6362'
file_name: 2019_MolecularBioReport_Temnov.pdf
file_size: 1948014
relation: main_file
file_date_updated: 2020-07-14T12:47:28Z
has_accepted_license: '1'
isi: 1
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
publication: Molecular Biology Reports
publication_identifier:
eissn:
- '15734978'
issn:
- '03014851'
publication_status: published
publisher: Springer
quality_controlled: '1'
scopus_import: '1'
status: public
title: Protective properties of the cultured stem cell proteome studied in an animal
model of acetaminophen-induced acute liver failure
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
year: '2019'
...