(Q32014468)

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Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides

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Europe PubMed Central

PubMed publication ID

5 July 2017

Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides (English)

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Europe PubMed Central

PubMed publication ID

5 July 2017

Marketa J Zvelebil

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ORCID Public Data File 2021

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Chung E

1

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Europe PubMed Central

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5 July 2017

Henriques D

2

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5 July 2017

Renzoni D

3

1 reference

Europe PubMed Central

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5 July 2017

Zvelebil M

4

1 reference

Europe PubMed Central

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5 July 2017

Bradshaw JM

5

1 reference

Europe PubMed Central

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5 July 2017

Waksman G

6

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5 July 2017

Robinson CV

7

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5 July 2017

Ladbury JE

8

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5 July 2017

publication date

1 September 1998

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5 July 2017

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Europe PubMed Central

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5 July 2017

6

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5 July 2017

9

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Europe PubMed Central

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5 July 2017

1141-1151

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5 July 2017

Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors

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Design of inhibitors of glycogen phosphorylase: a study of alpha- and beta-C-glucosides and 1-thio-beta-D-glucose compounds

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Enthalpy of hydrogen bond formation in a protein-ligand binding reaction

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The effect of water activity on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1.

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The role of water in sequence-independent ligand binding by an oligopeptide transporter protein

1 reference

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The Role of Water Molecules in the Structure-Based Design of (5-Hydroxynorvaline)-2-cyclosporin: Synthesis, Biological Activity, and Crystallographic Analysis with Cyclophilin A

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Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design

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Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

1 reference

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

1 reference

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Three-dimensional structure of the tyrosine kinase c-Src

1 reference

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based on heuristic

inferred from DOI database lookup

SH2 domains recognize specific phosphopeptide sequences

1 reference

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Studying noncovalent protein complexes by electrospray ionization mass spectrometry

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The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: Promise, pitfalls and prognosis

1 reference

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Hydration in drug design. 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions

1 reference

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A computational procedure for determining energetically favorable binding sites on biologically important macromolecules

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Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal

1 reference

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Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study

1 reference

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Alternative Modes of Tyrosyl Phosphopeptide Binding to a Src Family SH2 Domain: Implications for Regulation of Tyrosine Kinase Activity†

1 reference

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Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck

1 reference

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Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2

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Novel phosphotyrosine mimetics in the design of peptide ligands for pp60src SH2 domain

1 reference

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Design of peptidomimetic ligands for the pp60src SH2 domain

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

The crystal structures of the SH2 domain of p56lck complexed with two phosphonopeptides suggest a gated peptide binding site

1 reference

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Rapid measurement of binding constants and heats of binding using a new titration calorimeter

1 reference

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Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions

1 reference

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Identifiers

10.1016/S0969-2126(98)00115-4

1 reference

Europe PubMed Central

PubMed publication ID

5 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 July 2017

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