(Q38337486)

2 September 2017

title

The importance of two conserved arginine residues for catalysis by the ras GTPase-activating protein, neurofibromin (English)

1 reference

2 September 2017

Sermon BA

1

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2 September 2017

Lowe PN

series ordinal

2

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2 September 2017

Strom M

series ordinal

3

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2 September 2017

Eccleston JF

series ordinal

4

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2 September 2017

language of work or name

English

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publication date

1 April 1998

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

273

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2 September 2017

issue

16

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2 September 2017

page(s)

9480-9485

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The biochemistry of ras p21.

2 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Proteins regulating Ras and its relatives

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Identification of neurofibromin mutants that exhibit allele specificity or increased Ras affinity resulting in suppression of activated ras alleles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

p120 Ras GTPase-activating protein interacts with Ras-GTP through specific conserved residues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Mechanism of inhibition by arachidonic acid of the catalytic activity of Ras GTPase-activating proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

A general method for rapid site-directed mutagenesis using the polymerase chain reaction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.16.9480

21 January 2018

Identifiers

DOI

10.1074/JBC.273.16.9480

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2 September 2017

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