Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS). (Q44205402)

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scientific article published in November 2002

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English	Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS).	scientific article published in November 2002

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scholarly article

1 reference

Europe PubMed Central

30 November 2017

Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS). (English)

1 reference

Europe PubMed Central

30 November 2017

phosphorylation

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author name string

Yoshitomo Hamuro

1

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Europe PubMed Central

30 November 2017

Lilly Wong

2

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Europe PubMed Central

30 November 2017

Jennifer Shaffer

3

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Europe PubMed Central

30 November 2017

Jack S Kim

4

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Europe PubMed Central

30 November 2017

David D Stranz

5

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Europe PubMed Central

30 November 2017

Patricia A Jennings

6

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Europe PubMed Central

30 November 2017

Virgil L Woods

7

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Europe PubMed Central

30 November 2017

Joseph A Adams

8

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Europe PubMed Central

30 November 2017

language of work or name

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publication date

1 November 2002

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Europe PubMed Central

30 November 2017

number of pages

11

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Journal of Molecular Biology

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30 November 2017

323

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30 November 2017

871-881

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30 November 2017

5

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30 November 2017

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Hydrogen exchange: the modern legacy of Linderstrøm-Lang

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Investigating protein structure and dynamics by hydrogen exchange MS.

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Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection

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Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

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Hydrogen exchange and structural dynamics of proteins and nucleic acids

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Determination of amide hydrogen exchange rates in peptides by mass spectrometry

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7 January 2021

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

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High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: utility in pharmaceutical design.

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Protein phosphorylation analysis by electrospray ionization-mass spectrometry

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Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1

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Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure.

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Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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Active and inactive protein kinases: structural basis for regulation

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Domain interactions in protein tyrosine kinase Csk.

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Mutations in the N-terminal regulatory region reduce the catalytic activity of Csk, but do not affect its recognition of Src.

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7 January 2021

Identifiers

10.1016/S0022-2836(02)01003-3

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Europe PubMed Central

30 November 2017

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Europe PubMed Central

30 November 2017

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