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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Calpain 7

calpain-like protease, Calpain 7, PalBH, Capn7
Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The function of the protein encoded by this gene is not known. An orthologue has been found in mouse but it seems to diverge from other family members. The mouse orthologue is thought to be calcium independent with protease activity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Calpain, ACID, V1a, CAN, Ipaf
Papers on calpain-like protease
Calpain-like: A Ca(2+) dependent cystein protease in Entamoeba histolytica cell death.
Pérez Ishiwara et al., Mexico. In Exp Parasitol, Dec 2015
In this study, we evaluate the expression and activity of a specific dependent Ca(2+) protease, the calpain-like protease, by real-time quantitative PCR (RTq-PCR), Western blot assays and a enzymatic method during the induction of PCD by G418.
Interleukin-1α activation and localization in lipopolysaccharide-stimulated human monocytes and macrophages.
Birkelund et al., Aalborg, Denmark. In J Immunol Methods, Jul 2015
It is synthesized as a 33kDa precursor peptide that is cleaved by a calpain-like protease to a 16 kDa propiece and a 17 kDa mature IL-1α peptide.
Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway.
Maki et al., Nagoya, Japan. In Febs J, 2014
UNLABELLED: Calpain-7 (CAPN7) is a unique intracellular cysteine protease that has a tandem repeat of microtubule interacting and trafficking (MIT) domains and lacks a penta-EF-hand domain.
Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells.
Maki et al., Nagoya, Japan. In Febs J, 2013
Calpain-7 is a mammalian ortholog of a fungal non-classical calpain named PalB, which is an intracellular cysteine protease and functions in fungal alkaline adaptation in association with the endosomal sorting complex required for transport (ESCRT) system.
Identification of active Plasmodium falciparum calpain to establish screening system for Pf-calpain-based drug development.
Park et al., Namwŏn, South Korea. In Malar J, 2012
Pf-calpain, a cysteine protease of Plasmodium falciparum, belongs to calpain-7 family, which is an atypical calpain not harboring Ca2+-binding regulatory motifs.
Regulation of voltage-gated calcium channels by proteolysis.
Yang et al., New York City, United States. In Sheng Li Xue Bao, 2012
Proteolysis of the distal C-terminus of L-type channels also occurs in the brain and is probably catalyzed by a calpain-like protease.
Evolutionary and physical linkage between calpains and penta-EF-hand Ca2+-binding proteins.
Shibata et al., Nagoya, Japan. In Febs J, 2012
Fungi and budding yeasts have calpain-like sequences that lack the PEF domain, and each protein (designated PalB and Rim13, respectively) is orthologous to human calpain-7, indicating that the calpain-7 orthologs are evolutionarily more conserved than classical calpains possessing PEF domains.
Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes.
Hankeln et al., Zürich, Switzerland. In Mol Biol Evol, 2012
The calpain-like region is homologous to the catalytic domain II of the large subunit of human calpain-7.
Calpains: an elaborate proteolytic system.
Sorimachi et al., Tokyo, Japan. In Biochim Biophys Acta, 2012
Fifteen genes within the human genome encode a calpain-like protease domain.
In silico characterization of alkaline proteases from different species of Aspergillus.
Yadav et al., Inch'ŏn, South Korea. In Appl Biochem Biotechnol, 2012
The sequence level homology was obtained among different groups of alkaline protease enzymes, viz alkaline serine protease, oryzin, calpain-like protease, serine protease, subtilisin-like alkaline proteases.
Calpain-7 binds to CHMP1B at its second α-helical region and forms a ternary complex with IST1.
Maki et al., Nagoya, Japan. In J Biochem, 2011
The detected enhancement of autolysis of mGFP-fused calpain-7 by coexpression with CHMP1B and observed further activation by additional coexpression of IST1 in HEK293T cells.
Impact of genetic insights into calpain biology.
Ono et al., Tokyo, Japan. In J Biochem, 2011
Within the human genome, 15 genes (CAPN1-3, CAPN5-16) encode a calpain-like protease (CysPc) domain along with several different functional domains.
Calpain chronicle--an enzyme family under multidisciplinary characterization.
Ono et al., Tokyo, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2010
In the human genome, 15 genes--CAPN1, CAPN2, etc.--encode a calpain-like protease domain.
Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction.
Maki et al., Nagoya, Japan. In Febs J, 2010
Results demonstrate that human calpain 7 is proteolytically active, and imply that calpain 7 is activated by ESCRT-III-related protein IST1.
Expanding members and roles of the calpain superfamily and their genetically modified animals.
Ono et al., Tokyo, Japan. In Exp Anim, 2009
The human genome has 15 genes that encode a calpain-like protease domain, generating diverse calpain homologues that possess combinations of several functional domains such as Ca²(+)-binding domains and Zn-finger domains.
Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus.
Ellerby et al., Novato, United States. In J Biol Chem, 2004
calpain-derived Htt fragmentation has a role in Huntington's disease and aberrant activation of calpains may play a role in HD pathogenesis
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