Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal (Q24306895)

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M A Lemmon

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M Zhou

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J Green

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M C Botfield

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

11 April 1995

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published in

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volume

92

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page(s)

3199-203

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issue

8

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cites work

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27 September 2017

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27 September 2017

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Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods.

30 May 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=42133

Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins.

30 May 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=42133

Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis

30 May 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=42133

Heat capacity changes for protein-peptide interactions in the ribonuclease S system

30 May 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/7536927

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/7536927

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/7536927