Sequence co-evolution gives 3D contacts and structures of protein complexes (Q21128770)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25255213 AND SRC:MED&resulttype=core&format=json

19 February 2020

title

Sequence co-evolution gives 3D contacts and structures of protein complexes (English)

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19 February 2020

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1

Thomas A Hopf

Thomas A

Hopf

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19 February 2020

Charlotta P I Schärfe

series ordinal

2

object named as

Charlotta P I Schärfe

author given names

Charlotta P I

author last names

Schärfe

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19 February 2020

3

João P G L M Rodrigues

author given names

João P G L M

author last names

Rodrigues

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19 February 2020

4

Anna G Green

Anna G

Green

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19 February 2020

7

Alexandre M J J Bonvin

author given names

Alexandre M J J

author last names

Bonvin

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19 February 2020

8

Debora S Marks

Debora S

Marks

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19 February 2020

6

Chris Sander

Chris

Sander

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19 February 2020

5

Oliver Kohlbacher

Oliver

Kohlbacher

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19 February 2020

language of work or name

English

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publication date

25 September 2014

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19 February 2020

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19 February 2020

volume

3

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Sequence co-evolution gives 3D contacts and structures of protein complexes

19 February 2020

cites work

0 references

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Direct-coupling analysis of residue coevolution captures native contacts across many protein families

19 March 2017

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Structure of the gamma-epsilon complex of ATP synthase

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19 March 2017

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19 March 2017

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19 March 2017

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Identification of direct residue contacts in protein-protein interaction by message passing

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22 April 2017

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Half channels mediating H( ) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase

12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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12 September 2017

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27 September 2017

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30 May 2018

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30 May 2018

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30 May 2018

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30 May 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25255213

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25255213

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.7554/ELIFE.03430

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

681382

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25255213 AND SRC:MED&resulttype=core&format=json

19 February 2020

1 reference

OpenCitations bibliographic resource ID

681382

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25255213 AND SRC:MED&resulttype=core&format=json

19 February 2020

PubMed publication ID

25255213

1 reference