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

Effects of mutations of a phosphorylation site in an exposed loop in acidic fibroblast growth factor.

The Journal of biological chemistry - 18 Jun 1999

Klingenberg O, Wiedlocha A, Olsnes S

Abstract excerpt

Acidic fibroblast growth factor (aFGF) contains a phosphorylation site recognized by protein kinase C. A non-mitogenic mutant growth factor is devoid of this phosphorylation site. We have changed amino acids in and close to the phosphorylation site and studied the consequences of this for binding of the growth factor to high affinity receptors as well as to heparin. We have also studied the ability of the mutants...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to Biological Transport
Share to Calcium-Calmodulin-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Replication

Share to Fibroblast Growth Factor 1

Share to Heparin

Share to Protein Kinase C

Share to Receptors, Fibroblast Growth Factor

Source

Identifiers

PMID: 10364261
DOI: 10.1074/jbc.274.25.18081

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Effects of mutations of a phosphorylation site in an exposed loop in acidic fibroblast growth factor.PMID 10364261Read ↗

Involvement of the conserved acidic amino acid domain of FGF receptor 1 in ligand-receptor interaction.Semantic proximity Read ↗

Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3.Semantic proximity Read ↗

Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor.Semantic proximity Read ↗

Effect of mutation of cytoplasmic receptor domain and of genistein on transport of acidic fibroblast growth factor into cells.Semantic proximity Read ↗

Highly stable mutants of human fibroblast growth factor-1 exhibit prolonged biological action.Semantic proximity Read ↗

Mutants of basic fibroblast growth factor identify different cellular response programs.Semantic proximity Read ↗

A natural kinase-deficient variant of fibroblast growth factor receptor 1.Semantic proximity Read ↗

Asparagine-344 is a key residue for ligand binding in keratinocyte growth factor receptor.Semantic proximity Read ↗

Externally added aFGF mutants do not require extensive unfolding for transport to the cytosol and the nucleus in NIH/3T3 cells.Semantic proximity Read ↗

ATP-binding on fibroblast growth factor 2 partially overlaps with the heparin-binding domain.Semantic proximity Read ↗

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