The frozen solution structure of p21 ras determined by ESEEM spectroscopy reveals weak coordination of Thr35 to the active site metal ion (Q73728631)

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6 November 2019

title

The frozen solution structure of p21 ras determined by ESEEM spectroscopy reveals weak coordination of Thr35 to the active site metal ion (English)

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6 November 2019

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1

C. T. Farrar

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17 November 2024

author name string

C. J. Halkides

series ordinal

2

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17 November 2024

D. J. Singel

series ordinal

3

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17 November 2024

language of work or name

English

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National Center for Biotechnology Information

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17 November 2024

publication date

1 August 1997

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6 November 2019

15 August 1997

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National Center for Biotechnology Information

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full work available at URL

17 November 2024

http://www.cell.com/article/S0969212697002578/pdf

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https://api.elsevier.com/content/article/PII:S0969212697002578?httpAccept=text/xml

17 November 2024

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10.1016/S0969-2126(97)00257-8

DOI

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https://api.elsevier.com/content/article/PII:S0969212697002578?httpAccept=text/plain

17 November 2024

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10.1016/S0969-2126(97)00257-8

DOI

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17 November 2024

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6 November 2019

volume

5

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6 November 2019

issue

8

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6 November 2019

page(s)

1055-1066

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Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms

6 November 2019

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Altered growth of human colon cancer cell lines disrupted at activated Ki-ras

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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

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The effector interactions of p21ras

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Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP

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Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins

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High frequency (139.5 GHz) electron paramagnetic resonance spectroscopy of the GTP form of p21 ras with selective 17O labeling of threonine

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Simulation of the solution structure of the H-ras p21-GTP complex

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Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain

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Crystal structure of interleukin 8: symbiosis of NMR and crystallography

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Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations

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Structural studies of .alpha.-bungarotoxin. 1. Sequence-specific proton NMR resonance assignments

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Molecular conformation of alpha-bungarotoxin as studied by nuclear magnetic resonance and circular dichroism

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X-ray absorption fine structure investigation of the zinc transition metal binding site of Zn concanavalin A in solution and in the crystal.

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Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme

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Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: flexibility, possible hinges, and levers of the conformational transition.

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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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7 January 2021

An NMR comparison of the changes produced by different guanosine 5'-triphosphate analogs in wild-type and oncogenic mutant p21ras

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7 January 2021

Molecular dynamics simulations in biology

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Dominant inhibitory mutations in the Mg(2+)-binding site of RasH prevent its activation by GTP

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7 January 2021

Probing the role of loop 2 in Ras function with unnatural amino acids

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Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli

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NMR studies of the conformational change in human N-p21ras produced by replacement of bound GDP with the GTP analog GTP gamma S

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7 January 2021

10.1016/S0969-2126(97)00257-8

Identifiers

DOI

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6 November 2019

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