Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits. (Q52974843)

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scientific article published in January 2000

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English	Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits.	scientific article published in January 2000

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits. (English)

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

Thomas P Sakmar

6

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

author name string

O P Ernst

1

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

C K Meyer

2

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

E P Marin

3

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

P Henklein

4

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

W Y Fu

5

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

K P Hofmann

7

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

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publication date

1 January 2000

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

275

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

3

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Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

1937-1943

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

How receptors talk to trimeric G proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Structure and function of proteins in G-protein-coupled signal transfer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Rhodopsin mutants that bind but fail to activate transducin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

The 2.0 A crystal structure of a heterotrimeric G protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Signal transfer from rhodopsin to the G-protein: evidence for a two-site sequential fit mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Binding of transducin and transducin-derived peptides to rhodopsin studies by attenuated total reflection-Fourier transform infrared difference spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Receptor-G protein coupling is established by a potential conformational switch in the beta gamma complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Role of the C9 methyl group in rhodopsin activation: characterization of mutant opsins with the artificial chromophore 11-cis-9-demethylretinal

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Palmitoylation of bovine opsin and its cysteine mutants in COS cells.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Three cytoplasmic loops of rhodopsin interact with transducin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Molecular determinants of the reversible membrane anchorage of the G-protein transducin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

The molecular mechanism of visual excitation and its relation to the structure and composition of the rod outer segment

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Kinetic study on the equilibrium between membrane-bound and free photoreceptor G-protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.3.1937

21 January 2018

Identifiers

10.1074/JBC.275.3.1937

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

10 May 2018

http://europepmc.org/abstract/MED/10636895

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