(PDF) SH2 Domains Exhibit High-Affinity Binding to

SH2 Domains Exhibit High-Affinity Binding to Tyrosine-Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange.

Molecular and Cellular Biology - United States

doi 10.1128/mcb.13.3.1449

Full Text

Open PDF

Abstract

Available in full text

Date

March 1, 1993

Authors

Publisher

American Society for Microbiology

Related search

Binding Affinities of Tyrosine-Phosphorylated Peptides to the COOH-terminal SH2 and NH-terminal Phosphotyrosine Binding Domains of SHC

Journal of Biological Chemistry

English

Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated fromPseudomonas aeruginosaandKlebsiella Pneumoniae

International Journal of Medicinal Chemistry

English

Redundant Group a Streptococcus Signaling Peptides Exhibit Unique Activation Potentials

Journal of Bacteriology

Microbiology

Molecular Biology

2013

English

The C-Terminal SH2 Domain of P85 Accounts for the High Affinity and Specificity of the Binding of Phosphatidylinositol 3-Kinase to Phosphorylated Platelet-Derived Growth Factor Beta Receptor.

Molecular and Cellular Biology

Cell Biology

Molecular Biology

1992

English

Dissociation of Apolipoprotein E Oligomers to Monomer Is Required for High-Affinity Binding to Phospholipid Vesicles

Biochemistry

2011

English

Delineation of a T-Cell Activation Motif Required for Binding of Protein Tyrosine Kinases Containing Tandem SH2 Domains.

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

Multidisciplinary

1994

English

Interactions Between SH2 Domains and Tyrosine-Phosphorylated Platelet-Derived Growth Factor Beta-Receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor-Based Approach.

Molecular and Cellular Biology

Cell Biology

Molecular Biology

1993

English

The Human Exhibit

CMAJ

Medicine

2018

English

Hydrocarbon Constrained Peptides – Understanding Preorganisation and Binding Affinity

Chemical Science

Chemistry

2016

English

Amanote Research

SH2 Domains Exhibit High-Affinity Binding to Tyrosine-Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange.

Molecular and Cellular Biology - United States

doi 10.1128/mcb.13.3.1449

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Binding Affinities of Tyrosine-Phosphorylated Peptides to the COOH-terminal SH2 and NH-terminal Phosphotyrosine Binding Domains of SHC

Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated fromPseudomonas aeruginosaandKlebsiella Pneumoniae

Redundant Group a Streptococcus Signaling Peptides Exhibit Unique Activation Potentials

The C-Terminal SH2 Domain of P85 Accounts for the High Affinity and Specificity of the Binding of Phosphatidylinositol 3-Kinase to Phosphorylated Platelet-Derived Growth Factor Beta Receptor.

Dissociation of Apolipoprotein E Oligomers to Monomer Is Required for High-Affinity Binding to Phospholipid Vesicles

Delineation of a T-Cell Activation Motif Required for Binding of Protein Tyrosine Kinases Containing Tandem SH2 Domains.

Interactions Between SH2 Domains and Tyrosine-Phosphorylated Platelet-Derived Growth Factor Beta-Receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor-Based Approach.

The Human Exhibit

Hydrocarbon Constrained Peptides – Understanding Preorganisation and Binding Affinity