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

Mutations in the fourth EGF-like domain affect thrombomodulin-induced changes in the active site of thrombin.

Biochemistry - 14 Oct 2008

Koeppe Julia R, Beach Muneera A, Baerga-Ortiz Abel, Kerns S Jordan, Komives Elizabeth A

Abstract excerpt

A number of alanine and more conservative mutants of residues in the fourth domain of thrombomodulin (TM) were prepared and assayed for protein C activation and for thrombin binding. Several of the alanine mutations appeared to cause misfolding or structural defects as assessed by poor expression and/or NMR HSQC experiments, while more conservative mutations at the same site appeared to allow correct folding and...

Read the complete abstract on PubMed

Topics

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

Share to Epidermal Growth Factor
Share to Mutagenesis, Site-Directed

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

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Sequence Homology, Amino Acid

Share to Spectrometry, Fluorescence

Share to Surface Plasmon Resonance

Share to Thrombin

Share to Thrombomodulin

Source

Open in PubMed Open full text

Identifiers

PMID: 18803401
DOI: 10.1021/bi8008278
PMCID: PMC2630536

Genes

EGF

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

Mutations in the fourth EGF-like domain affect thrombomodulin-induced changes in the active site of thrombin.PMID 18803401Read ↗

Sequences required for thrombomodulin cofactor activity within the fourth epidermal growth factor-like domain of human thrombomodulin.Semantic proximity Read ↗

The short loop between epidermal growth factor-like domains 4 and 5 is critical for human thrombomodulin function.Semantic proximity Read ↗

A Frequent Thrombomodulin Amino Acid Dimorphism Is not Associated with ThrombophiliaSemantic proximity Read ↗

Characterization of a thrombomodulin binding site on protein C and its comparison to an activated protein C binding site for factor Va.Semantic proximity Read ↗

Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.Semantic proximity Read ↗

The functional significance of the autolysis loop in protein C and activated protein C.Semantic proximity Read ↗

Naturally occurring mutations in the thrombomodulin gene leading to impaired expression and function.Semantic proximity Read ↗

Engineering thrombin for selective specificity toward protein C and PAR1.Semantic proximity Read ↗

Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme.Semantic proximity Read ↗

Role of the activation peptide in the mechanism of protein C activation.Semantic proximity Read ↗

Tissue plasminogen activator: the biochemistry and pharmacology of variants produced by mutagenesis.Semantic proximity Read ↗

Mutagenesis studies toward understanding allostery in thrombin.Semantic proximity Read ↗

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