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KNOTTIN specifications

Information


Unique identifier OMICS_06179
Name KNOTTIN
Restrictions to use None
Community driven No
Data access File download, Browse
User data submission Allowed
Version 2.0
Maintained Yes

Maintainer


  • person_outline Jean-Christophe Gelly

Additional information


Previous version: http://knottin.cbs.cnrs.fr/ http://www.dsimb.inserm.fr/KNOTTIN/doc.php

Publications for KNOTTIN

KNOTTIN citations

 (16)
library_books

Molecular Characterization and Biodiversity of a Putative Chlorotoxin from the Iranian Yellow Scorpion Odontobuthus doriae

2017
PMCID: 5548967
PMID: 28415833
DOI: 10.18869/acadpub.ibj.21.5.342

[…] e and 82.35% identity. In the built model of OdClTx1, three strand (8.57%), one helix (28.57%), and one loop (62.86%) were found. OdClTx1 folding was done by the highest confidence of similarity with knottin domains. These domains are small inhibitors, toxins, and lectins belonging to the scorpion toxin-like superfamily and short-chain scorpion toxins family[]. In OdClTx1 mature peptide, the knott […]

library_books

Identification and Characterization of Roseltide, a Knottin type Neutrophil Elastase Inhibitor Derived from Hibiscus sabdariffa

2016
Sci Rep
PMCID: 5171801
PMID: 27991569
DOI: 10.1038/srep39401

[…] oyed a peptidomic approach to identify a panel of CRPs, roseltides (rT1-rT8), from the medicinal plant Hibiscus sabdariffa. Roseltide rT1, the smallest member of roseltide family, was identified as a knottin-type inhibitor against human neutrophil elastase. There has been only one reported knottin-type porcine elastase inhibitor (MCEI-IV) with three N-terminal truncated analogs (MCEI-I to MCEI-III […]

library_books

Clustering of disulfide rich peptides provides scaffolds for hit discovery by phage display: application to interleukin 23

2016
BMC Bioinformatics
PMCID: 5120537
PMID: 27881076
DOI: 10.1186/s12859-016-1350-9

[…] ected manually through visualization of the resulting clusters; alternate cutoffs of 0.6 and 0.8 were also assessed and rejected. Any cluster containing four or more peptides annotated with the SCOP “knottin” fold (SCOP identifier g.3) were considered “knottin clusters”; peptides from these clusters were pooled and reclustered hierarchically, using the disulfide distance metric and imposing a cuto […]

library_books

Complex lasso: new entangled motifs in proteins

2016
Sci Rep
PMCID: 5118788
PMID: 27874096
DOI: 10.1038/srep36895

[…] antimicrobial (disulfide based) lasso proteins – for example this motif might serve as a “molecular plug”, as in case of the action of mini-proteins, blocking the uptake channel.The first engineered knottin was already successfully applied for tumor imaging. The cyclotides, a family of mini-proteins that contain a head-to-tail cyclized backbone, also have a diverse range of biological activities, […]

library_books

A sodium channel inhibitor ISTX I with a novel structure provides a new hint at the evolutionary link between two toxin folds

2016
Sci Rep
PMCID: 4942781
PMID: 27407029
DOI: 10.1038/srep29691

[…] in the primary sequence and the relative orientation of the disulfide bond pairs and the secondary structures between the ISTX-I and ICK fold. Furthermore, we used our structure to search against the KNOTTIN database, which provides standardized data on the knottin structural family. Both the Knoter3D and Knoter1D tools suggested that ISTX-I does not exhibit the inhibitor cysteine knot topology. R […]

library_books

Genome Wide Reprogramming of Transcript Architecture by Temperature Specifies the Developmental States of the Human Pathogen Histoplasma

2015
PLoS Genet
PMCID: 4503680
PMID: 26177267
DOI: 10.1371/journal.pgen.1005395

[…] The curated Fungi1 alignment was downloaded from the KNOTTIN database [] and trimmed to the conserved cysteine residues plus 10 residues of padding on either side (alignment positions 423 through 483, counting from 1). Hmmer 3.0 (http://hmmer.org) was u […]

Citations

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KNOTTIN institution(s)
INSERM, U 1134, DSIMB, Paris, France; Universite Paris Diderot, Sorbonne Paris Cite, UMRS 1134, Paris, France; Institut National de la Transfusion Sanguine, Paris, France; Laboratory of Excellence GR-Ex, Paris, France; CNRS UMR 5048, INSERM U1054, Centre de Biochimie Structurale, Universite Montpellier, Montpellier, France

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