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

Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity.

Protein engineering - 1 Dec 2002

van der Walle Christopher F, Altroff Harri, Mardon Helen J

Abstract excerpt

The ninth and tenth type III domains (FIII9-10) in the central cell binding domain of human fibronectin contain integrin receptor binding sites, including RGD in FIII10 and a synergy site, PHSRN, in FIII9. The specific amino acids that contribute to cell binding have been identified by the use of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Cell Adhesion
Share to Fibronectins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Leucine

Share to Proline

Share to Recombinant Proteins

Share to Serine

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 12601142
DOI: 10.1093/protein/15.12.1021
PMCID: PMC1630685

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12601142-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity.PMID 12601142Read ↗

Synergistic activity of the ninth and tenth FIII domains of human fibronectin depends upon structural stability.Semantic proximity Read ↗

The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain.Semantic proximity Read ↗

Exploring the potential of the monobody scaffold: effects of loop elongation on the stability of a fibronectin type III domain.Semantic proximity Read ↗

Integrin α3β1 Binding to Fibronectin Is Dependent on the Ninth Type III Repeat.Semantic proximity Read ↗

Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.Semantic proximity Read ↗

Antibody mimics based on human fibronectin type three domain engineered for thermostability and high-affinity binding to vascular endothelial growth factor receptor twoSemantic proximity Read ↗

High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement.Semantic proximity Read ↗

2.0 Å Crystal Structure of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy RegionSemantic proximity Read ↗

Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin.Semantic proximity Read ↗

Structural and functional characterization of the product of disease-related factor H gene conversion.Semantic proximity Read ↗

Motogenic sites in human fibronectin are masked by long range interactions.Semantic proximity Read ↗

The role of the fibronectin IGD motif in stimulating fibroblast migration.Semantic proximity Read ↗

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