Revisiting the structural flexibility of the complex p21(ras)-GTP: the catalytic conformation of the molecular switch II. (Q43825549)

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5 December 2019

title

Revisiting the structural flexibility of the complex p21(ras)-GTP: the catalytic conformation of the molecular switch II (English)

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5 December 2019

1

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5 December 2019

author name string

J H Miller

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11746677%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

T P Straatsma

series ordinal

3

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5 December 2019

language of work or name

English

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publication date

1 December 2001

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5 December 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11746677%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

volume

45

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5 December 2019

issue

4

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5 December 2019

page(s)

297-312

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The structure of Ras protein: a model for a universal molecular switch

5 December 2019

cites work

1 reference

X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis

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Role of glutamine-61 in the hydrolysis of GTP by p21H-ras: an experimental and theoretical study.

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

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

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Calculation of the electric potential in the active site cleft due to alpha-helix dipoles

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Identification of functional and unfolding motions of cutinase as obtained from molecular dynamics computer simulations

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Hinge-bending motions in annexins: molecular dynamics and essential dynamics of apo-annexin V and of calcium bound annexin V and I

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Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR

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