Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide (Q27677473)

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English	Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide	scientific article

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instance of

scholarly article

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title

Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide (English)

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main subject

G protein-coupled receptor

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protein structure

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author

Arun K Shukla

object named as

Arun K Shukla

series ordinal

1

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Shohei Koide

object named as

Shohei Koide

series ordinal

14

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William I Weis

object named as

William I Weis

series ordinal

15

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Brian Kobilka

series ordinal

17

object named as

Brian K Kobilka

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Aashish Manglik

series ordinal

2

object named as

Aashish Manglik

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Robert Lefkowitz

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18

object named as

Robert J Lefkowitz

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Kunhong Xiao

series ordinal

4

object named as

Kunhong Xiao

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Dean P Staus

series ordinal

7

object named as

Dean P Staus

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Prachi Tripathi-Shukla

series ordinal

12

object named as

Prachi Tripathi-Shukla

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author name string

Andrew C Kruse

series ordinal

3

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Rosana I Reis

series ordinal

5

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Wei-Chou Tseng

series ordinal

6

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Daniel Hilger

series ordinal

8

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Serdar Uysal

series ordinal

9

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Li-Yin Huang

series ordinal

10

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Marcin Paduch

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11

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Akiko Koide

series ordinal

13

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Anthony A Kossiakoff

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16

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language of work or name

English

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publication date

2 May 2013

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published in

Nature

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volume

497

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issue

7447

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page(s)

137-41

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cites work

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Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

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Seven-transmembrane receptors

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G proteins

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Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge

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27 November 2018

An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation

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based on heuristic

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Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin

1 reference

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reference URL

https://pubmed.ncbi.nlm.nih.gov/23604254

retrieved

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based on heuristic

inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/23604254

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme

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Identifiers

DOI

10.1038/NATURE12120

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

434997

Dimensions Publication ID

1045536210

0 references

OpenCitations bibliographic resource ID

434997

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

434997

PMC publication ID

3654799

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

434997

PubMed publication ID

23604254

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

434997

ResearchGate publication ID

236252876

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