(Q28909851)

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Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded

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scholarly article

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PubMed publication ID

7 March 2017

Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded (English)

1 reference

PubMed publication ID

7 March 2017

protein folding

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Gamma-aminobutyric acid type B receptor subunit 2

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GOA release 2020-03-11

object named as

Brian O. Smith

4

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9

object named as

Paul N. Barlow

1 reference

PubMed publication ID

7 March 2017

author name string

Stanislas Blein

1

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PubMed publication ID

7 March 2017

Rachel Ginham

2

1 reference

PubMed publication ID

7 March 2017

Dusan Uhrin

3

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PubMed publication ID

7 March 2017

Dinesh C. Soares

5

1 reference

PubMed publication ID

7 March 2017

Stefvan Veltel

6

1 reference

PubMed publication ID

7 March 2017

R. A. Jeffrey McIlhinney

7

1 reference

PubMed publication ID

7 March 2017

Julia H. White

8

1 reference

PubMed publication ID

7 March 2017

language of work or name

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publication date

12 November 2004

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PubMed publication ID

7 March 2017

Journal of Biological Chemistry

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PubMed publication ID

7 March 2017

279

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PubMed publication ID

7 March 2017

46

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PubMed publication ID

7 March 2017

48292–48306

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PubMed publication ID

7 March 2017

The metabotropic GABA receptor: molecular insights and their functional consequences

1 reference

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International Union of Pharmacology. XXXIII. Mammalian gamma-aminobutyric acid(B) receptors: structure and function

1 reference

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21 January 2018

GABAB receptors: a new paradigm in G protein signaling

1 reference

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Heterodimerization is required for the formation of a functional GABA(B) receptor

1 reference

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21 January 2018

GABA(B)-receptor subtypes assemble into functional heteromeric complexes.

1 reference

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21 January 2018

GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2.

1 reference

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21 January 2018

Role of heteromer formation in GABAB receptor function

1 reference

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Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors

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A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor

1 reference

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Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function

1 reference

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Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit.

1 reference

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Human GABA(B)R genomic structure: evidence for splice variants in GABA(B)R1 but not GABA(B)R2.

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Cloning and tissue distribution of novel splice variants of the rat GABAB receptor

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Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1) splice variant encoding a truncated receptor.

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GABA(B) receptors: from monogamy to promiscuity

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Protein-protein interactions at G-protein-coupled receptors

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Cloning and characterization of seizure-related gene, SEZ-6.

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Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding

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The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx

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Scanning microcalorimetry in studying temperature-induced changes in proteins.

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1 reference

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An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins

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Effects of proline cis-trans isomerization on TB domain secondary structure

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Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor

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Protein structure alignment by incremental combinatorial extension (CE) of the optimal path

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Expression of highly disulfide-bonded proteins in Pichia pastoris

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Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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NMR studies of a viral protein that mimics the regulators of complement activation

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Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans

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Intrinsic disorder and protein function

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Intrinsically disordered protein

1 reference

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Sequence complexity of disordered protein

1 reference

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Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces

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