[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-26.
PubMed=3463996 [NCBI, ExPASy, EBI, Israel, Japan]
Chan S.J.,
San Segundo B.,
McCormick M.B.,
Steiner D.F.;
"Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.";
Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gastric carcinoma;
DOI=10.1016/0378-1119(94)90750-1; PubMed=8112600 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L.,
Taggart R.T.,
Berquin I.M.,
Moin K.,
Fong D.,
Sloane B.F.;
"Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene.";
Gene 139:163-169(1994).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-26.
TISSUE=Brain, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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PROTEIN SEQUENCE OF 80-126 AND 129-333.
TISSUE=Liver;
DOI=10.1016/0014-5793(85)81136-4; PubMed=3972105 [NCBI, ExPASy, EBI, Israel, Japan]
Ritonja A.,
Popovic T.,
Turk V.,
Wiedenmann K.,
Machleidt W.;
"Amino acid sequence of human liver cathepsin B.";
FEBS Lett. 181:169-172(1985).
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[5]
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PROTEIN SEQUENCE OF 80-91 AND 129-139.
TISSUE=Liver;
PubMed=1637335 [NCBI, ExPASy, EBI, Israel, Japan]
Moin K.,
Day N.A.,
Sameni M.,
Hasnain S.,
Hirama T.,
Sloane B.F.;
"Human tumour cathepsin B. Comparison with normal liver cathepsin B.";
Biochem. J. 285:427-434(1992).
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[6]
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NUCLEOTIDE SEQUENCE [MRNA] OF 131-339.
PubMed=3010323 [NCBI, ExPASy, EBI, Israel, Japan]
Fong D.,
Calhoun D.H.,
Hsieh W.-T.,
Lee B.,
Wells R.D.;
"Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B.";
Proc. Natl. Acad. Sci. U.S.A. 83:2909-2913(1986).
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[7]
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SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr025562r; PubMed=12643545 [NCBI, ExPASy, EBI, Israel, Japan]
Basrur V.,
Yang F.,
Kushimoto T.,
Higashimoto Y.,
Yasumoto K.,
Valencia J.,
Muller J.,
Vieira W.D.,
Watabe H.,
Shabanowitz J.,
Hearing V.J.,
Hunt D.F.,
Appella E.;
"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
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[8]
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SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A.,
Valencia J.C.,
Hu Z.-Z.,
Watabe H.,
Yamaguchi H.,
Mangini N.J.,
Huang H.,
Canfield V.A.,
Cheng K.C.,
Yang F.,
Abe R.,
Yamagishi S.,
Shabanowitz J.,
Hearing V.J.,
Wu C.,
Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
PubMed=1868826 [NCBI, ExPASy, EBI, Israel, Japan]
Musil D.,
Zucic D.,
Turk D.,
Engh R.A.,
Mayr I.,
Huber R.,
Popovic T.,
Turk V.,
Towatari T.,
Katunuma N.,
Bode W.;
"The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.";
EMBO J. 10:2321-2330(1991).
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[10]
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X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
DOI=10.1016/0014-5793(96)00309-2; PubMed=8617355 [NCBI, ExPASy, EBI, Israel, Japan]
Turk D.,
Podobnik M.,
Kuhelj R.,
Dolinar M.,
Turk V.;
"Crystal structures of human procathepsin B at 3.2- and 3.3-A resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide.";
FEBS Lett. 384:211-214(1996).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1006/jmbi.1997.1218; PubMed=9299326 [NCBI, ExPASy, EBI, Israel, Japan]
Podobnik M.,
Kuhelj R.,
Turk V.,
Turk D.;
"Crystal structure of the wild-type human procathepsin B at 2.5-A resolution reveals the native active site of a papain-like cysteine protease zymogen.";
J. Mol. Biol. 271:774-788(1997).
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