CAPN1

CAPN1

Calpain 1, (mu/I) large subunit, also known as CAPN1, is a human gene.cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = ]

PBB_Summary
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summary_text = The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Suzuki K, Sorimachi H, Yoshizawa T, "et al." |title=Calpain: novel family members, activation, and physiologic function. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 9 |pages= 523–9 |year= 1996 |pmid= 8561910 |doi=
*cite journal | author=Huang Y, Wang KK |title=The calpain family and human disease. |journal=Trends in molecular medicine |volume=7 |issue= 8 |pages= 355–62 |year= 2001 |pmid= 11516996 |doi=
*cite journal | author=Goll DE, Thompson VF, Li H, "et al." |title=The calpain system. |journal=Physiol. Rev. |volume=83 |issue= 3 |pages= 731–801 |year= 2003 |pmid= 12843408 |doi= 10.1152/physrev.00029.2002
*cite journal | author=Banik NL, DeVries GH, Neuberger T, "et al." |title=Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. |journal=J. Neurosci. Res. |volume=29 |issue= 3 |pages= 346–54 |year= 1991 |pmid= 1656060 |doi= 10.1002/jnr.490290310
*cite journal | author=Ohno S, Minoshima S, Kudoh J, "et al." |title=Four genes for the calpain family locate on four distinct human chromosomes. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 225–9 |year= 1990 |pmid= 2209092 |doi=
*cite journal | author=Sorimachi H, Ohmi S, Emori Y, "et al." |title=A novel member of the calcium-dependent cysteine protease family. |journal=Biol. Chem. Hoppe-Seyler |volume=371 Suppl |issue= |pages= 171–6 |year= 1990 |pmid= 2400579 |doi=
*cite journal | author=Harris AS, Croall DE, Morrow JS |title=The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15754–61 |year= 1988 |pmid= 2844821 |doi=
*cite journal | author=Aoki K, Imajoh S, Ohno S, "et al." |title=Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence. |journal=FEBS Lett. |volume=205 |issue= 2 |pages= 313–7 |year= 1986 |pmid= 3017764 |doi=
*cite journal | author=Ishiguro H, Higashiyama S, Namikawa C, "et al." |title=Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. |journal=Biochemistry |volume=26 |issue= 10 |pages= 2863–70 |year= 1987 |pmid= 3038169 |doi=
*cite journal | author=Morishita R, Nakayama H, Isobe T, "et al." |title=Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C. |journal=J. Biol. Chem. |volume=270 |issue= 49 |pages= 29469–75 |year= 1996 |pmid= 7493986 |doi=
*cite journal | author=Kavita U, Mizel SB |title=Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27758–65 |year= 1996 |pmid= 7499244 |doi=
*cite journal | author=Du X, Saido TC, Tsubuki S, "et al." |title=Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26146–51 |year= 1995 |pmid= 7592818 |doi=
*cite journal | author=Bradford HN, Jameson BA, Adam AA, "et al." |title=Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26546–51 |year= 1994 |pmid= 8253784 |doi=
*cite journal | author=Oda A, Ozaki K, Druker BJ, "et al." |title=p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin. |journal=Blood |volume=88 |issue= 4 |pages= 1330–8 |year= 1996 |pmid= 8695851 |doi=
*cite journal | author=Zhang W, Lane RD, Mellgren RL |title=The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells. |journal=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18825–30 |year= 1996 |pmid= 8702541 |doi=
*cite journal | author=Courseaux A, Grosgeorge J, Gaudray P, "et al." |title=Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1). |journal=Genomics |volume=37 |issue= 3 |pages= 354–65 |year= 1997 |pmid= 8938448 |doi=
*cite journal | author=Corasaniti MT, Navarra M, Catani MV, "et al." |title=NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 299–304 |year= 1997 |pmid= 8954122 |doi= 10.1006/bbrc.1996.1796
*cite journal | author=Stabach PR, Cianci CD, Glantz SB, "et al." |title=Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. |journal=Biochemistry |volume=36 |issue= 1 |pages= 57–65 |year= 1997 |pmid= 8993318 |doi= 10.1021/bi962034i
*cite journal | author=Norris FA, Atkins RC, Majerus PW |title=Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 10987–9 |year= 1997 |pmid= 9110986 |doi=

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