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

Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity.

Blood - 29 Oct 2009

Meems Henriët, Meijer Alexander B, Cullinan David B, Mertens Koen, Gilbert Gary E

Abstract excerpt

Binding of factor VIII to membranes containing phosphatidyl-L-serine (Ptd-L-Ser) is mediated, in part, by a motif localized to the C2 domain. We evaluated a putative membrane-binding role of the C1 domain using an anti-C1 antibody fragment, KM33(scFv), and factor VIII mutants with an altered KM33 epitope. We prepared a dual mutant Lys2092/Phe2093 --> Ala/Ala (fVIII(YFP 2092/93)) and 2 single mutants Lys2092 -->...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Antibodies
Share to Coenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Factor VIII

Share to Lysine

Share to Membranes, Artificial

Share to Phenylalanine

Source

Identifiers

PMID: 19687511
DOI: 10.1182/blood-2009-01-197707

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity.PMID 19687511Read ↗

A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function.Semantic proximity Read ↗

Factor VIII C1 domain spikes 2092-2093 and 2158-2159 comprise regions that modulate cofactor function and cellular uptake.Semantic proximity Read ↗

Mutation of the surface-exposed amino acid Trp to Ala in the FVIII C2 domain results in defective secretion of the otherwise functional protein.Semantic proximity Read ↗

A novel cause of mild/moderate hemophilia A: mutations scattered in the factor VIII C1 domain reduce factor VIII binding to von Willebrand factor.Semantic proximity Read ↗

Mutations associated with hemophilia A in the 558-565 loop of the factor VIIIa A2 subunit alter the catalytic activity of the factor Xase complex.Semantic proximity Read ↗

The factor V C1 domain is involved in membrane binding: identification of functionally important amino acid residues within the C1 domain of factor V using alanine scanning mutagenesis.Semantic proximity Read ↗

Contribution of factor VIII light-chain residues 2007-2016 to an activated protein C-interactive site.Semantic proximity Read ↗

Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets.Semantic proximity Read ↗

Defining the critical roles of factor VIII residues 1900 to 1908 in factor VIIIa-factor IXa complex formation and factor VIIIa activity.Semantic proximity Read ↗

Functional mapping of factor VIII C2 domain.Semantic proximity Read ↗

Biophysical characterization of blood coagulation factor VIII binding to lipid nanodiscs that mimic activated platelet surfaces.Semantic proximity Read ↗

Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.Semantic proximity Read ↗

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