Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis. (Q45999872)

18 December 2017

title

Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis. (English)

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18 December 2017

1

Tobias Vöpel

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18 December 2017

Simone Kunzelmann

2

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18 December 2017

Christian Herrmann

series ordinal

3

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18 December 2017

language of work or name

English

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publication date

20 May 2009

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18 December 2017

published in

FEBS Letters

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18 December 2017

volume

583

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18 December 2017

issue

12

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18 December 2017

page(s)

1923-1927

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18 December 2017

Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus

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Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1).

21 January 2018

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Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

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Transient kinetic investigation of GTP hydrolysis catalyzed by interferon-gamma-induced hGBP1 (human guanylate binding protein 1).

21 January 2018

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Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif

21 January 2018

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Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis

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Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism

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How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP

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Calculation of protein extinction coefficients from amino acid sequence data

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Reassessment of Ellman's reagent

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Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine

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Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature.

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21 January 2018

Identifiers

DOI

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18 December 2017

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18 December 2017