^Pavlova, Alona; Björk Ingemar. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. Biochemistry (United States). Sep 2003, 42 (38): 11326–33. ISSN 0006-2960. PMID 14503883. doi:10.1021/bi030119v.
^Pol, E; Björk I. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases. Protein Sci. (United States). Sep 2001, 10 (9): 1729–38. ISSN 0961-8368. PMC 2253190. PMID 11514663. doi:10.1110/ps.11901.
拓展阅读
Turk V, Bode W. The cystatins: protein inhibitors of cysteine proteinases.. FEBS Lett. 1991, 285 (2): 213–9. PMID 1855589. S2CID 40444629. doi:10.1016/0014-5793(91)80804-C.
Järvinen M, Rinne A, Hopsu-Havu VK. Human cystatins in normal and diseased tissues--a review.. Acta Histochem. 1988, 82 (1): 5–18. PMID 3122506. doi:10.1016/s0065-1281(87)80043-0.
Brown WM, Dziegielewska KM. Friends and relations of the cystatin superfamily--new members and their evolution.. Protein Sci. 1997, 6 (1): 5–12. PMC 2143511. PMID 9007972. doi:10.1002/pro.5560060102.
Kos J, Lah TT. Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review).. Oncol. Rep. 1998, 5 (6): 1349–61. PMID 9769367. doi:10.3892/or.5.6.1349.
Stubbs MT, Laber B, Bode W, et al. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.. EMBO J. 1990, 9 (6): 1939–47. PMC 551902. PMID 2347312. doi:10.1002/j.1460-2075.1990.tb08321.x.
Jerala R, Trstenjak M, Lenarcic B, Turk V. Cloning a synthetic gene for human stefin B and its expression in E. coli.. FEBS Lett. 1988, 239 (1): 41–4. PMID 3053245. S2CID 33859701. doi:10.1016/0014-5793(88)80541-6.
Lenarcic B, Kos J, Dolenc I, et al. Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.. Biochem. Biophys. Res. Commun. 1988, 154 (2): 765–72. PMID 3261170. doi:10.1016/0006-291X(88)90206-9.
Ritonja A, Machleidt W, Barrett AJ. Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver.. Biochem. Biophys. Res. Commun. 1985, 131 (3): 1187–92. PMID 3902020. doi:10.1016/0006-291X(85)90216-5.
Spiess E, Brüning A, Gack S, et al. Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level.. J. Histochem. Cytochem. 1994, 42 (7): 917–29. PMID 8014475. doi:10.1177/42.7.8014475.
Lehesjoki AE, Koskiniemi M, Norio R, et al. Localization of the EPM1 gene for progressive myoclonus epilepsy on chromosome 21: linkage disequilibrium allows high resolution mapping.. Hum. Mol. Genet. 1993, 2 (8): 1229–34. PMID 8104628. doi:10.1093/hmg/2.8.1229.
Pennacchio LA, Myers RM. Isolation and characterization of the mouse cystatin B gene.. Genome Res. 1997, 6 (11): 1103–9. PMID 8938434. doi:10.1101/gr.6.11.1103.
Lalioti MD, Mirotsou M, Buresi C, et al. Identification of mutations in cystatin B, the gene responsible for the Unverricht-Lundborg type of progressive myoclonus epilepsy (EPM1).. Am. J. Hum. Genet. 1997, 60 (2): 342–51. PMC 1712389. PMID 9012407.
Lafrenière RG, Rochefort DL, Chrétien N, et al. Unstable insertion in the 5' flanking region of the cystatin B gene is the most common mutation in progressive myoclonus epilepsy type 1, EPM1.. Nat. Genet. 1997, 15 (3): 298–302. PMID 9054946. S2CID 21180258. doi:10.1038/ng0397-298.
Bespalova IN, Adkins S, Pranzatelli M, Burmeister M. Novel cystatin B mutation and diagnostic PCR assay in an Unverricht-Lundborg progressive myoclonus epilepsy patient. (PDF). Am. J. Med. Genet. 1997, 74 (5): 467–71. PMID 9342192. doi:10.1002/(SICI)1096-8628(19970919)74:5<467::AID-AJMG1>3.0.CO;2-L. hdl:2027.42/38271.
外部链接
GeneReviews/NCBI/NIH/UW entry on Unverricht-Lundborg Disease or EPM1 （页面存档备份，存于互联网档案馆）
The MEROPS online database for peptidases and their inhibitors: I25.003
PDBe-KB （页面存档备份，存于互联网档案馆） provides an overview of all the structure information available in the PDB for Human Cystatin-B
行進 27, 2023
胱抑素b, 英文, cystatin, 是一种在人体中由cstb基因编码的蛋白质, 人类地, 血清已知的結構pdb直系同源搜索, pdbe, rcsbpdbid列表1stf, 2oct, 4n6v識別號别名cstb, cst6, epm1, epm1a, stfb, cystatin, b外部idomim, 601145, 109514, homologene, genecards, cstb基因位置, 人类, 染色体21號染色體, 基因座21q22, 3起始43, 终止43, 基因位置, 小鼠, 染色体小鼠10号. 胱抑素B 英文 Cystatin B 是一种在人体中由CSTB基因编码的蛋白质 5 6 人类地胱抑素B 血清胱抑素B已知的結構PDB直系同源搜索 PDBe RCSBPDBID列表1STF 2OCT 4N6V識別號别名CSTB CST6 EPM1 EPM1A PME STFB ULD Cystatin B CPI B外部IDOMIM 601145 MGI 109514 HomoloGene 79 GeneCards CSTB基因位置 人类 染色体21號染色體 1 基因座21q22 3起始43 772 511 bp 1 终止43 776 330 bp 1 基因位置 小鼠 染色体小鼠10号染色体 2 基因座10 C1 10 39 72 cM起始78 261 503 bp 2 终止78 263 456 bp 2 RNA表达模式查阅更多表达数据基因本體分子功能 peptidase inhibitor activity 蛋白酶結合 endopeptidase inhibitor activity cysteine type endopeptidase inhibitor activity RNA binding細胞組分 細胞質 核仁 外排體 胞內 细胞核 細胞外區域 細胞外空間 细胞质基质 secretory granule lumen tertiary granule lumen ficolin 1 rich granule lumen collagen containing extracellular matrix生物學過程 adult locomotory behavior negative regulation of proteolysis negative regulation of peptidase activity negative regulation of endopeptidase activity neutrophil degranulationSources Amigo QuickGO直系同源物種人類小鼠Entrez147613014EnsemblENSG00000160213ENSMUSG00000005054UniProtP04080Q62426mRNA 序列NM 000100NM 007793蛋白序列NP 000091NP 031819基因位置 UCSC Chr 21 43 77 43 78 MbChr 10 78 26 78 26 MbPubMed 查找 3 4 維基數據檢視 編輯人類檢視 編輯小鼠胱抑素超家族包括含有多个胱抑素样序列的蛋白质 一些成员是活性半胱氨酸蛋白酶抑制剂 而其他成员已经失去或可能从未获得这种抑制活性 超家族中有3个抑制家族 包括1型胱抑素 stefin 2型胱抑素和激肽原 该基因编码一种作为细胞内半胱氨酸蛋白酶抑制剂而起作用的stefin 胱抑素B能够形成由非共价作用力稳定的二聚体 抑制木瓜蛋白酶和组织蛋白酶L1 H和B 胱抑素B被认为在防止蛋白酶从溶酶体泄漏方面发挥作用 有证据表明 该基因突变是导致进行性肌阵挛性癫痫患者出现主要缺陷的原因 6 目录 1 交互作用 2 参考文献 3 拓展阅读 4 外部链接交互作用 编辑胱抑素B已被证明与组织蛋白酶B产生交互作用 7 8 参考文献 编辑 1 0 1 1 1 2 GRCh38 Ensembl release 89 ENSG00000160213 Ensembl May 2017 2 0 2 1 2 2 GRCm38 Ensembl release 89 ENSMUSG00000005054 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Pennacchio LA Lehesjoki AE Stone NE Willour VL Virtaneva K Miao J D Amato E Ramirez L Faham M Koskiniemi M Warrington JA Norio R de la Chapelle A Cox DR Myers RM Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy EPM1 Science Apr 1996 271 5256 1731 4 Bibcode 1996Sci 271 1731P PMID 8596935 S2CID 84361089 doi 10 1126 science 271 5256 1731 6 0 6 1 Entrez Gene CSTB cystatin B stefin B Pavlova Alona Bjork Ingemar Grafting of features of cystatins C or B into the N terminal region or second binding loop of cystatin A stefin A substantially enhances inhibition of cysteine proteinases Biochemistry United States Sep 2003 42 38 11326 33 ISSN 0006 2960 PMID 14503883 doi 10 1021 bi030119v Pol E Bjork I Role of the single cysteine residue Cys 3 of human and bovine cystatin B stefin B in the inhibition of cysteine proteinases Protein Sci United States Sep 2001 10 9 1729 38 ISSN 0961 8368 PMC 2253190 PMID 11514663 doi 10 1110 ps 11901 拓展阅读 编辑Turk V Bode W The cystatins protein inhibitors of cysteine proteinases FEBS Lett 1991 285 2 213 9 PMID 1855589 S2CID 40444629 doi 10 1016 0014 5793 91 80804 C Jarvinen M Rinne A Hopsu Havu VK Human cystatins in normal and diseased tissues a review Acta Histochem 1988 82 1 5 18 PMID 3122506 doi 10 1016 s0065 1281 87 80043 0 Brown WM Dziegielewska KM Friends and relations of the cystatin superfamily new members and their evolution Protein Sci 1997 6 1 5 12 PMC 2143511 PMID 9007972 doi 10 1002 pro 5560060102 Kos J Lah TT Cysteine proteinases and their endogenous inhibitors target proteins for prognosis diagnosis and therapy in cancer review Oncol Rep 1998 5 6 1349 61 PMID 9769367 doi 10 3892 or 5 6 1349 Stubbs MT Laber B Bode W et al The refined 2 4 A X ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain a novel type of proteinase inhibitor interaction EMBO J 1990 9 6 1939 47 PMC 551902 PMID 2347312 doi 10 1002 j 1460 2075 1990 tb08321 x Jerala R Trstenjak M Lenarcic B Turk V Cloning a synthetic gene for human stefin B and its expression in E coli FEBS Lett 1988 239 1 41 4 PMID 3053245 S2CID 33859701 doi 10 1016 0014 5793 88 80541 6 Lenarcic B Kos J Dolenc I et al Cathepsin D inactivates cysteine proteinase inhibitors cystatins Biochem Biophys Res Commun 1988 154 2 765 72 PMID 3261170 doi 10 1016 0006 291X 88 90206 9 Ritonja A Machleidt W Barrett AJ Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver Biochem Biophys Res Commun 1985 131 3 1187 92 PMID 3902020 doi 10 1016 0006 291X 85 90216 5 Spiess E Bruning A Gack S et al Cathepsin B activity in human lung tumor cell lines ultrastructural localization pH sensitivity and inhibitor status at the cellular level J Histochem Cytochem 1994 42 7 917 29 PMID 8014475 doi 10 1177 42 7 8014475 Lehesjoki AE Koskiniemi M Norio R et al Localization of the EPM1 gene for progressive myoclonus epilepsy on chromosome 21 linkage disequilibrium allows high resolution mapping Hum Mol Genet 1993 2 8 1229 34 PMID 8104628 doi 10 1093 hmg 2 8 1229 Pennacchio LA Myers RM Isolation and characterization of the mouse cystatin B gene Genome Res 1997 6 11 1103 9 PMID 8938434 doi 10 1101 gr 6 11 1103 Lalioti MD Mirotsou M Buresi C et al Identification of mutations in cystatin B the gene responsible for the Unverricht Lundborg type of progressive myoclonus epilepsy EPM1 Am J Hum Genet 1997 60 2 342 51 PMC 1712389 PMID 9012407 Lafreniere RG Rochefort DL Chretien N et al Unstable insertion in the 5 flanking region of the cystatin B gene is the most common mutation in progressive myoclonus epilepsy type 1 EPM1 Nat Genet 1997 15 3 298 302 PMID 9054946 S2CID 21180258 doi 10 1038 ng0397 298 Virtaneva K D Amato E Miao J et al Unstable minisatellite expansion causing recessively inherited myoclonus epilepsy EPM1 Nat Genet 1997 15 4 393 6 PMID 9090386 S2CID 24971949 doi 10 1038 ng0497 393 Bespalova IN Adkins S Pranzatelli M Burmeister M Novel cystatin B mutation and diagnostic PCR assay in an Unverricht Lundborg progressive myoclonus epilepsy patient PDF Am J Med Genet 1997 74 5 467 71 PMID 9342192 doi 10 1002 SICI 1096 8628 19970919 74 5 lt 467 AID AJMG1 gt 3 0 CO 2 L hdl 2027 42 38271 外部链接 编辑GeneReviews NCBI NIH UW entry on Unverricht Lundborg Disease or EPM1 页面存档备份 存于互联网档案馆 The MEROPS online database for peptidases and their inhibitors I25 003 PDBe KB 页面存档备份 存于互联网档案馆 provides an overview of all the structure information available in the PDB for Human Cystatin B 取自 https zh wikipedia org w index php title 胱抑素B amp oldid 75103251, 维基百科，wiki，书籍，书籍，图书馆，
