Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of three amino acid residues in the B-chain of platelet-derived growth factor with different importance for binding to PDGF alpha- and beta-receptors.

FEBS letters - 6 May 1996

Kreysing J, Ostman A, van de Poll M, Bäckström G, Heldin C H

Abstract excerpt

The B-chain homodimer isoform of platelet-derived growth factor (PDGF) binds with high affinity both to alpha- and to beta-receptors. In order to localize amino acid residues in PDGF-BB of differential importance for the binding to the two receptors, PDGF-BB mutants were analyzed in which single amino acid residues were changed to alanine residues. We found that Phe-118 in loop 1 of the PDGF B-chain is crucial...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Source

Identifiers

PMID: 8647246
DOI: 10.1016/0014-5793(96)00349-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of three amino acid residues in the B-chain of platelet-derived growth factor with different importance for binding to PDGF alpha- and beta-receptors.PMID 8647246Read ↗

Structural coincidence of alpha PDGFR epitopes binding to platelet-derived growth factor-AA and a potent neutralizing monoclonal antibody.Semantic proximity Read ↗

Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization.Semantic proximity Read ↗

Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration.Semantic proximity Read ↗

Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF.Semantic proximity Read ↗

Increased mitogenicity of an alphabeta heterodimeric PDGF receptor complex correlates with lack of RasGAP binding.Semantic proximity Read ↗

Platelet-derived growth factor AB heterodimer interchain interactions influence secretion as well as receptor binding and activation.Semantic proximity Read ↗

Assignment of intrachain disulfide bonds in platelet-derived growth factor B-chain.Semantic proximity Read ↗

Alternative splicing determines the binding of platelet-derived growth factor (PDGF-AA) to glycosaminoglycans.Semantic proximity Read ↗

Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.Semantic proximity Read ↗

The conformational stability of a non-covalent dimer of a platelet-derived growth factor-B mutant lacking the two cysteines involved in interchain disulfide bonds.Semantic proximity Read ↗

Evidence for distinct signaling properties and biological responses induced by the PDGF receptor alpha and beta subtypes.Semantic proximity Read ↗

A two-amino acid insertion in the Cys146- Cys167 loop of the alphaIIb subunit is associated with a variant of Glanzmann thrombasthenia. Critical role of Asp163 in ligand binding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.