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

Point mutations alter the mechanical stability of immunoglobulin modules.

Nature structural biology - 1 Dec 2000

Li H, Carrion-Vazquez M, Oberhauser A F, Marszalek P E, Fernandez J M

Abstract excerpt

Immunoglobulin-like modules are common components of proteins that play mechanical roles in cells such as muscle elasticity and cell adhesion. Mutations in these proteins may affect their mechanical stability and thus may compromise their function. Using single molecule atomic force microscopy (A...

Read the complete abstract on PubMed

Topics

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

Share to Connectin
Share to Immunoglobulins
Share to Microscopy, Atomic Force

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Monte Carlo Method

Share to Muscle Proteins

Share to Proline

Share to Protein Denaturation

Share to Protein Renaturation

Source

Identifiers

PMID: 11101892
DOI: 10.1038/81964

Genes

AFM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-11101892-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Point mutations alter the mechanical stability of immunoglobulin modules.PMID 11101892Read ↗

Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.Semantic proximity Read ↗

Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains.Semantic proximity Read ↗

Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.Semantic proximity Read ↗

Biophysical characterization of naturally occurring titin M10 mutations.Semantic proximity Read ↗

The influence of disulfide bonds on the mechanical stability of proteins is context dependent.Semantic proximity Read ↗

Structure determination and analysis of titin A-band fibronectin type III domains provides insights for disease-linked variants and protein oligomerisationSemantic proximity Read ↗

Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain- or loss-of-function.Semantic proximity Read ↗

A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues.Semantic proximity Read ↗

The Y9P Variant of the Titin I27 Module: Structural Determinants of Its Revisited Nanomechanics.Semantic proximity Read ↗

Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complexSemantic proximity Read ↗

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.Semantic proximity Read ↗

Mutations targeting intermodular interfaces or calcium binding destabilize the thrombospondin-2 signature domain.Semantic proximity Read ↗

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