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

Molecular modeling studies of peptide inhibitors highlight the importance of conformational prearrangement for inhibition of calpain.

Biochemistry - 6 Jul 2010

Jiao Wanting, McDonald D Quentin, Coxon James M, Parker Emily J

Abstract excerpt

The overexpression of the cysteine protease calpain is associated with many diseases, including brain trauma, spinal cord injury, Alzheimer's disease, Parkinson's disease, muscular dystrophy, arthritis, and cataract. Calpastatin is the naturally occurring specific regulator of calpain activity. It has previously been reported that a 20-mer peptide truncated from region B of calpastatin inhibitory domain 1 (named...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Binding Proteins
Share to Calpain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Cysteine Proteinase Inhibitors

Share to Models, Molecular

Share to Peptide Fragments

Share to Peptides

Share to Protein Conformation

Source

Identifiers

PMID: 20499928
DOI: 10.1021/bi100048y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular modeling studies of peptide inhibitors highlight the importance of conformational prearrangement for inhibition of calpain.PMID 20499928Read ↗

Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase.Semantic proximity Read ↗

Calpains for dummies: What you need to know about the calpain family.Semantic proximity Read ↗

Residue-specific annotation of disorder-to-order transition and cathepsin inhibition of a propeptide-like crammer from D. melanogaster.Semantic proximity Read ↗

Structural Insights into the Unique Activation Mechanisms of a Non-classical Calpain and Its Disease-Causing Variants.Semantic proximity Read ↗

Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.Semantic proximity Read ↗

Affinity purification of human m-calpain through an intrinsically disordered inhibitor, calpastatin.Semantic proximity Read ↗

Structures of C1q-like proteins reveal unique features among the C1q/TNF superfamily.Semantic proximity Read ↗

<i>In Silico</i> Targeting of Calpain-5 in Autosomal Dominant Neovascular Inflammatory Vitreoretinopathy (ADNIV) with Peptides and Natural ProductsSemantic proximity Read ↗

Identification and neuroprotective properties of NA-184, a selective calpain-2 inhibitorSemantic proximity Read ↗

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-MetalloproteasesSemantic proximity Read ↗

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches.Semantic proximity Read ↗

Purification and characterization of the active-site-mutated recombinant human mu-calpain expressed in baculovirus-infected insect cells.Semantic proximity Read ↗

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