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

Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aalpha R16C and gamma G165R.

Blood - 15 Jul 2001

Bolliger-Stucki B, Lord S T, Furlan M

Abstract excerpt

Fibrinogen Milano XII was detected in an asymptomatic Italian woman, whose routine coagulation test results revealed a prolonged thrombin time. Fibrinogen levels in functional assays were considerably lower than levels in immunologic assays. Polymerization of purified fibrinogen was strongly impaired in the presence of calcium or ethylenediaminetetraacetic acid (EDTA). Two heterozygous structural defects were...

Read the complete abstract on PubMed

Topics

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

Share to Blood Coagulation Disorders
Share to Chymotrypsin
Share to Edetic Acid

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

Share to Fibrinogen

Share to Fibrinogens, Abnormal

Share to Fibrinolysin

Share to Serum Albumin

Share to Thrombin

Source

Identifiers

PMID: 11435303
DOI: 10.1182/blood.v98.2.351

Genes

SDS

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

Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aalpha R16C and gamma G165R.PMID 11435303Read ↗

Fibrinogen Milano XIII (Aalpha 19 Arg-->Gly): a dysfunctional variant with an amino acid substitution in the N-terminal polymerization site.Semantic proximity Read ↗

Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.Semantic proximity Read ↗

A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.Semantic proximity Read ↗

Fibrinogen anomalies and disease. A clinical update.Semantic proximity Read ↗

A frameshift mutation in Exon V of the A alpha-chain gene leading to truncated A alpha-chains in the homozygous dysfibrinogen Milano IIISemantic proximity Read ↗

Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly----Val (GGC----GTC) mutation.Semantic proximity Read ↗

Inherited abnormalities of fibrinogen: 10-year clinical experience of an Italian group.Semantic proximity Read ↗

Two different fibrinogen gene mutations associated with bleeding in the same family (A αGly13Glu and γGly16Ser) and their impact on fibrin clot properties: fibrinogen Krakow II and Krakow III.Semantic proximity Read ↗

Fibrinogen Hillsborough: a novel gammaGly309Asp dysfibrinogen with impaired clotting.Semantic proximity Read ↗

Fibrinogen Mannheim II: a novel gamma307 His-->Tyr substitution in the gammaD domain causes hypofibrinogenemia.Semantic proximity Read ↗

Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308----Ile mutation.Semantic proximity Read ↗

An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links.Semantic proximity Read ↗

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