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

Thermodynamic characterization of mutants of human fibroblast growth factor 1 with an increased physiological half-life.

Biochemistry - 20 Jun 2000

Culajay J F, Blaber S I, Khurana A, Blaber M

Abstract excerpt

Human acidic fibroblast growth factor (FGF-1) is a potent mitogen and angiogenic factor, with reportedly poor thermal stability and a relatively short in vivo half-life. However, certain mutants of FGF-1 have been described that exhibit a significant increase in half-life in tissue culture-based assays. FGF-1 contains three cysteine residues, two of which are highly conserved and buried within the protein core....

Read the complete abstract on PubMed

Topics

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

Share to Calorimetry, Differential Scanning
Share to Circular Dichroism

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

Share to Cysteine

Share to Fibroblast Growth Factor 1

Share to Guanidine

Share to Half-Life

Share to Protein Denaturation

Share to Serine

Source

Identifiers

PMID: 10852713
DOI: 10.1021/bi9927742

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

Thermodynamic characterization of mutants of human fibroblast growth factor 1 with an increased physiological half-life.PMID 10852713Read ↗

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

Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor.Semantic proximity Read ↗

Structure of a highly stable mutant of human fibroblast growth factor 1.Semantic proximity Read ↗

Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor.Semantic proximity Read ↗

An empirical phase diagram approach to investigate conformational stability of "second-generation" functional mutants of acidic fibroblast growth factor-1.Semantic proximity Read ↗

Pharmacokinetic properties of 2nd-generation fibroblast growth factor-1 mutants for therapeutic application.Semantic proximity Read ↗

Structural and biochemical investigation into stable FGF2 mutants with novel mutation sites and hydrophobic replacements for surface-exposed cysteines.Semantic proximity Read ↗

Increased thermal stability of FGF10 leads to ectopic signaling during developmentSemantic proximity Read ↗

Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.Semantic proximity Read ↗

Mutation choice to eliminate buried free cysteines in protein therapeutics.Semantic proximity Read ↗

Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: thermodynamic and functional consequences of structural symmetry.Semantic proximity Read ↗

Structure, stability and biological properties of a N-terminally truncated form of recombinant human interleukin-6 containing a single disulfide bond.Semantic proximity Read ↗

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