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

The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin.

Protein science : a publication of the Protein Society - 1 Dec 2001

Bottomley S P, Lawrenson I D, Tew D, Dai W, Whisstock J C, Pike R N

Abstract excerpt

Serpins inhibit cognate serine proteases involved in a number of important processes including blood coagulation and inflammation. Consequently, loss of serpin function or stability results in a number of disease states. Many of the naturally occurring mutations leading to disease are located within strand 1 of the C beta-sheet of the serpin. To ascertain the structural and functional importance of each residue...

Read the complete abstract on PubMed

Topics

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

Share to alpha 1-Antitrypsin
Share to Antithrombins

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

Share to Circular Dichroism

Share to Electrophoresis, Polyacrylamide Gel

Share to Protein Structure, Secondary

Share to Serpins

Share to Temperature

Share to Thrombin

Source

Open in PubMed Open full text

Identifiers

PMID: 11714919
DOI: 10.1110/ps.ps.24101
PMCID: PMC2374035

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

The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin.PMID 11714919Read ↗

Alpha 1-antitrypsin deficiency. A conformational disease.Semantic proximity Read ↗

Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition.Semantic proximity Read ↗

An overview of the serpin superfamily.Semantic proximity Read ↗

Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization.Semantic proximity Read ↗

Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease.Semantic proximity Read ↗

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.Semantic proximity Read ↗

A novel SERPINA1 mutation causing serum alpha(1)-antitrypsin deficiency.Semantic proximity Read ↗

Local and global effects of a cavity filling mutation in a metastable serpin.Semantic proximity Read ↗

A protein family under 'stress' - serpin stability, folding and misfolding.Semantic proximity Read ↗

Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide.Semantic proximity Read ↗

The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality controlSemantic proximity Read ↗

Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution--implications for serpin mechanistic model and prediction of nsSNP activities.Semantic proximity Read ↗

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