组织蛋白酶D (Chinese Wikipedia)

Analysis of information sources in references of the Wikipedia article "组织蛋白酶D" in Chinese language version.

Last modified: 06:06:42, 18 June 2026 (UTC)

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Faust PL, Kornfeld S, Chirgwin JM. Cloning and sequence analysis of cDNA for human cathepsin D. Proceedings of the National Academy of Sciences of the United States of America. August 1985, 82 (15): 4910–4. Bibcode:1985PNAS...82.4910F. PMC 390467 . PMID 3927292. doi:10.1073/pnas.82.15.4910 .

archive.org (Global: 6^th place; Chinese: 2^nd place)

Barrett AJ. Cathepsin D. Purification of isoenzymes from human and chicken liver. The Biochemical Journal. April 1970, 117 (3): 601–7. PMC 1178965 . PMID 5419752. doi:10.1042/bj1170601.
Diment S, Martin KJ, Stahl PD. Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins. The Journal of Biological Chemistry. August 1989, 264 (23): 13403–6. PMID 2760027. doi:10.1016/S0021-9258(18)80010-2 .
Saftig P, Hetman M, Schmahl W, Weber K, Heine L, Mossmann H, Köster A, Hess B, Evers M, von Figura K. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. The EMBO Journal. August 1995, 14 (15): 3599–608. PMC 394433 . PMID 7641679. doi:10.1002/j.1460-2075.1995.tb00029.x.
Ramirez-Montealegre D, Rothberg PG, Pearce DA. Another disorder finds its gene. Brain. June 2006, 129 (Pt 6): 1353–6. PMID 16738059. doi:10.1093/brain/awl132 .
Metcalf P, Fusek M. Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. The EMBO Journal. April 1993, 12 (4): 1293–302. PMC 413340 . PMID 8467789. doi:10.1002/j.1460-2075.1993.tb05774.x.
Briozzo P, Morisset M, Capony F, Rougeot C, Rochefort H. In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells. Cancer Research. July 1988, 48 (13): 3688–92. PMID 3378211.
Authier F, Metioui M, Fabrega S, Kouach M, Briand G. Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D. The Journal of Biological Chemistry. March 2002, 277 (11): 9437–46. PMID 11779865. doi:10.1074/jbc.M110188200 .
Baechle D, Flad T, Cansier A, Steffen H, Schittek B, Tolson J, et al. Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. The Journal of Biological Chemistry. March 2006, 281 (9): 5406–15. PMID 16354654. doi:10.1074/jbc.M504670200 .
Hakala JK, Oksjoki R, Laine P, Du H, Grabowski GA, Kovanen PT, Pentikäinen MO. Lysosomal enzymes are released from cultured human macrophages, hydrolyze LDL in vitro, and are present extracellularly in human atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology. August 2003, 23 (8): 1430–6. PMID 12750117. doi:10.1161/01.ATV.0000077207.49221.06 .
Haidar B, Kiss RS, Sarov-Blat L, Brunet R, Harder C, McPherson R, Marcel YL. Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux. The Journal of Biological Chemistry. December 2006, 281 (52): 39971–81. PMID 17032648. doi:10.1074/jbc.M605095200 .
Heinrich M, Wickel M, Schneider-Brachert W, Sandberg C, Gahr J, Schwandner R, Weber T, Saftig P, Peters C, Brunner J, Krönke M, Schütze S. Cathepsin D targeted by acid sphingomyelinase-derived ceramide. The EMBO Journal. October 1999, 18 (19): 5252–63. PMC 1171596 . PMID 10508159. doi:10.1093/emboj/18.19.5252.

books.google.com (Global: 3^rd place; Chinese: 6^th place)

Petsko G, Ringe D. Protein Structure and Function. Oxford [England]; Sunderland, MA; New York: Oxford University Press. 2004. ISBN 978-1-4051-1922-1.

doi.org (Global: 2^nd place; Chinese: 5^th place)

Faust PL, Kornfeld S, Chirgwin JM. Cloning and sequence analysis of cDNA for human cathepsin D. Proceedings of the National Academy of Sciences of the United States of America. August 1985, 82 (15): 4910–4. Bibcode:1985PNAS...82.4910F. PMC 390467 . PMID 3927292. doi:10.1073/pnas.82.15.4910 .
Barrett AJ. Cathepsin D. Purification of isoenzymes from human and chicken liver. The Biochemical Journal. April 1970, 117 (3): 601–7. PMC 1178965 . PMID 5419752. doi:10.1042/bj1170601.
Diment S, Martin KJ, Stahl PD. Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins. The Journal of Biological Chemistry. August 1989, 264 (23): 13403–6. PMID 2760027. doi:10.1016/S0021-9258(18)80010-2 .
Saftig P, Hetman M, Schmahl W, Weber K, Heine L, Mossmann H, Köster A, Hess B, Evers M, von Figura K. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. The EMBO Journal. August 1995, 14 (15): 3599–608. PMC 394433 . PMID 7641679. doi:10.1002/j.1460-2075.1995.tb00029.x.
Ramirez-Montealegre D, Rothberg PG, Pearce DA. Another disorder finds its gene. Brain. June 2006, 129 (Pt 6): 1353–6. PMID 16738059. doi:10.1093/brain/awl132 .
Metcalf P, Fusek M. Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. The EMBO Journal. April 1993, 12 (4): 1293–302. PMC 413340 . PMID 8467789. doi:10.1002/j.1460-2075.1993.tb05774.x.
Minarowska A, Gacko M, Karwowska A, Minarowski Ł. Human cathepsin D. Folia Histochemica et Cytobiologica / Polish Academy of Sciences, Polish Histochemical and Cytochemical Society. 2008, 46 (1): 23–38. PMID 18296260. doi:10.2478/v10042-008-0003-x .
Authier F, Metioui M, Fabrega S, Kouach M, Briand G. Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D. The Journal of Biological Chemistry. March 2002, 277 (11): 9437–46. PMID 11779865. doi:10.1074/jbc.M110188200 .
Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nature Structural Biology. October 1998, 5 (10): 866–71 [2022-09-18]. PMID 9783744. S2CID 5685201. doi:10.1038/2306. （原始内容存档于2022-09-22）.
Baechle D, Flad T, Cansier A, Steffen H, Schittek B, Tolson J, et al. Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. The Journal of Biological Chemistry. March 2006, 281 (9): 5406–15. PMID 16354654. doi:10.1074/jbc.M504670200 .
Hakala JK, Oksjoki R, Laine P, Du H, Grabowski GA, Kovanen PT, Pentikäinen MO. Lysosomal enzymes are released from cultured human macrophages, hydrolyze LDL in vitro, and are present extracellularly in human atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology. August 2003, 23 (8): 1430–6. PMID 12750117. doi:10.1161/01.ATV.0000077207.49221.06 .
Benes P, Vetvicka V, Fusek M. Cathepsin D—many functions of one aspartic protease. Critical Reviews in Oncology/Hematology. October 2008, 68 (1): 12–28. PMC 2635020 . PMID 18396408. doi:10.1016/j.critrevonc.2008.02.008.
Lkhider M, Castino R, Bouguyon E, Isidoro C, Ollivier-Bousquet M. Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions. Journal of Cell Science. October 2004, 117 (Pt 21): 5155–64. PMID 15456852. doi:10.1242/jcs.01396 .
Jha, Sawan Kumar; Rauniyar, Khushbu; Chronowska, Ewa; Mattonet, Kenny; Maina, Eunice Wairimu; Koistinen, Hannu; Stenman, Ulf-Håkan; Alitalo, Kari; Jeltsch, Michael. KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D. eLife. 2019-05-17, 8: –44478. ISSN 2050-084X. PMC 6588350 . PMID 31099754. doi:10.7554/eLife.44478.
Traynor JP, Oun HA, McKenzie P, Shilliday IR, McKay IG, Dunlop A, Geddes CC, Mactier RA. Assessing the utility of the stop dialysate flow method in patients receiving haemodiafiltration. Nephrology, Dialysis, Transplantation. November 2005, 20 (11): 2479–84. PMID 16046508. doi:10.1093/ndt/gfi021 .
Wolf M, Clark-Lewis I, Buri C, Langen H, Lis M, Mazzucchelli L. Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer. The American Journal of Pathology. April 2003, 162 (4): 1183–90. PMC 1851240 . PMID 12651610. doi:10.1016/S0002-9440(10)63914-4.
Menzer G, Müller-Thomsen T, Meins W, Alberici A, Binetti G, Hock C, Nitsch RM, Stoppe G, Reiss J, Finckh U. Non-replication of association between cathepsin D genotype and late onset Alzheimer disease. American Journal of Medical Genetics. March 2001, 105 (2): 179–82. PMID 11304834. doi:10.1002/ajmg.1204.
Haidar B, Kiss RS, Sarov-Blat L, Brunet R, Harder C, McPherson R, Marcel YL. Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux. The Journal of Biological Chemistry. December 2006, 281 (52): 39971–81. PMID 17032648. doi:10.1074/jbc.M605095200 .
Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M. Pepstatin, a new pepsin inhibitor produced by Actinomycetes. The Journal of Antibiotics. May 1970, 23 (5): 259–62. PMID 4912600. doi:10.7164/antibiotics.23.259 .
Kim SJ, Kim KH, Ahn ER, Yoo BC, Kim SY. Depletion of cathepsin D by transglutaminase 2 through protein cross-linking promotes cell survival. Amino Acids. January 2013, 44 (1): 73–80. PMID 21960143. S2CID 17149825. doi:10.1007/s00726-011-1089-6.
Devosse T, Dutoit R, Migeotte I, De Nadai P, Imbault V, Communi D, Salmon I, Parmentier M. Processing of HEBP1 by cathepsin D gives rise to F2L, the agonist of formyl peptide receptor 3. Journal of Immunology. August 2011, 187 (3): 1475–85. PMID 21709160. doi:10.4049/jimmunol.1003545 .
Mariani E, Seripa D, Ingegni T, Nocentini G, Mangialasche F, Ercolani S, Cherubini A, Metastasio A, Pilotto A, Senin U, Mecocci P. Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer's disease. Journal of the Neurological Sciences. September 2006, 247 (2): 187–91. PMID 16784755. S2CID 34224448. doi:10.1016/j.jns.2006.05.043.
Heinrich M, Wickel M, Schneider-Brachert W, Sandberg C, Gahr J, Schwandner R, Weber T, Saftig P, Peters C, Brunner J, Krönke M, Schütze S. Cathepsin D targeted by acid sphingomyelinase-derived ceramide. The EMBO Journal. October 1999, 18 (19): 5252–63. PMC 1171596 . PMID 10508159. doi:10.1093/emboj/18.19.5252.

ensembl.org (Global: 630^th place; Chinese: 669^th place)

may2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000117984 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000007891 – Ensembl, 2017年5月

nih.gov (Global: 5^th place; Chinese: 3^rd place)

ncbi.nlm.nih.gov

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.
Faust PL, Kornfeld S, Chirgwin JM. Cloning and sequence analysis of cDNA for human cathepsin D. Proceedings of the National Academy of Sciences of the United States of America. August 1985, 82 (15): 4910–4. Bibcode:1985PNAS...82.4910F. PMC 390467 . PMID 3927292. doi:10.1073/pnas.82.15.4910 .
Entrez Gene: CTSD cathepsin D. [2022-09-18]. （原始内容存档于2010-04-12）.
Barrett AJ. Cathepsin D. Purification of isoenzymes from human and chicken liver. The Biochemical Journal. April 1970, 117 (3): 601–7. PMC 1178965 . PMID 5419752. doi:10.1042/bj1170601.
Diment S, Martin KJ, Stahl PD. Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins. The Journal of Biological Chemistry. August 1989, 264 (23): 13403–6. PMID 2760027. doi:10.1016/S0021-9258(18)80010-2 .
Saftig P, Hetman M, Schmahl W, Weber K, Heine L, Mossmann H, Köster A, Hess B, Evers M, von Figura K. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. The EMBO Journal. August 1995, 14 (15): 3599–608. PMC 394433 . PMID 7641679. doi:10.1002/j.1460-2075.1995.tb00029.x.
Ramirez-Montealegre D, Rothberg PG, Pearce DA. Another disorder finds its gene. Brain. June 2006, 129 (Pt 6): 1353–6. PMID 16738059. doi:10.1093/brain/awl132 .
Metcalf P, Fusek M. Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. The EMBO Journal. April 1993, 12 (4): 1293–302. PMC 413340 . PMID 8467789. doi:10.1002/j.1460-2075.1993.tb05774.x.
Minarowska A, Gacko M, Karwowska A, Minarowski Ł. Human cathepsin D. Folia Histochemica et Cytobiologica / Polish Academy of Sciences, Polish Histochemical and Cytochemical Society. 2008, 46 (1): 23–38. PMID 18296260. doi:10.2478/v10042-008-0003-x .
Briozzo P, Morisset M, Capony F, Rougeot C, Rochefort H. In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells. Cancer Research. July 1988, 48 (13): 3688–92. PMID 3378211.
Authier F, Metioui M, Fabrega S, Kouach M, Briand G. Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D. The Journal of Biological Chemistry. March 2002, 277 (11): 9437–46. PMID 11779865. doi:10.1074/jbc.M110188200 .
Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nature Structural Biology. October 1998, 5 (10): 866–71 [2022-09-18]. PMID 9783744. S2CID 5685201. doi:10.1038/2306. （原始内容存档于2022-09-22）.
Baechle D, Flad T, Cansier A, Steffen H, Schittek B, Tolson J, et al. Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. The Journal of Biological Chemistry. March 2006, 281 (9): 5406–15. PMID 16354654. doi:10.1074/jbc.M504670200 .
Hakala JK, Oksjoki R, Laine P, Du H, Grabowski GA, Kovanen PT, Pentikäinen MO. Lysosomal enzymes are released from cultured human macrophages, hydrolyze LDL in vitro, and are present extracellularly in human atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology. August 2003, 23 (8): 1430–6. PMID 12750117. doi:10.1161/01.ATV.0000077207.49221.06 .
Bańkowska A, Gacko M, Chyczewska E, Worowska A. Biological and diagnostic role of cathepsin D. Roczniki Akademii Medycznej W Białymstoku. 1997,. 42 Suppl 1: 79–85. PMID 9337526.
Benes P, Vetvicka V, Fusek M. Cathepsin D—many functions of one aspartic protease. Critical Reviews in Oncology/Hematology. October 2008, 68 (1): 12–28. PMC 2635020 . PMID 18396408. doi:10.1016/j.critrevonc.2008.02.008.
Lkhider M, Castino R, Bouguyon E, Isidoro C, Ollivier-Bousquet M. Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions. Journal of Cell Science. October 2004, 117 (Pt 21): 5155–64. PMID 15456852. doi:10.1242/jcs.01396 .
Jha, Sawan Kumar; Rauniyar, Khushbu; Chronowska, Ewa; Mattonet, Kenny; Maina, Eunice Wairimu; Koistinen, Hannu; Stenman, Ulf-Håkan; Alitalo, Kari; Jeltsch, Michael. KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D. eLife. 2019-05-17, 8: –44478. ISSN 2050-084X. PMC 6588350 . PMID 31099754. doi:10.7554/eLife.44478.
Traynor JP, Oun HA, McKenzie P, Shilliday IR, McKay IG, Dunlop A, Geddes CC, Mactier RA. Assessing the utility of the stop dialysate flow method in patients receiving haemodiafiltration. Nephrology, Dialysis, Transplantation. November 2005, 20 (11): 2479–84. PMID 16046508. doi:10.1093/ndt/gfi021 .
Wolf M, Clark-Lewis I, Buri C, Langen H, Lis M, Mazzucchelli L. Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer. The American Journal of Pathology. April 2003, 162 (4): 1183–90. PMC 1851240 . PMID 12651610. doi:10.1016/S0002-9440(10)63914-4.
Menzer G, Müller-Thomsen T, Meins W, Alberici A, Binetti G, Hock C, Nitsch RM, Stoppe G, Reiss J, Finckh U. Non-replication of association between cathepsin D genotype and late onset Alzheimer disease. American Journal of Medical Genetics. March 2001, 105 (2): 179–82. PMID 11304834. doi:10.1002/ajmg.1204.
Haidar B, Kiss RS, Sarov-Blat L, Brunet R, Harder C, McPherson R, Marcel YL. Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux. The Journal of Biological Chemistry. December 2006, 281 (52): 39971–81. PMID 17032648. doi:10.1074/jbc.M605095200 .
Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M. Pepstatin, a new pepsin inhibitor produced by Actinomycetes. The Journal of Antibiotics. May 1970, 23 (5): 259–62. PMID 4912600. doi:10.7164/antibiotics.23.259 .
Kim SJ, Kim KH, Ahn ER, Yoo BC, Kim SY. Depletion of cathepsin D by transglutaminase 2 through protein cross-linking promotes cell survival. Amino Acids. January 2013, 44 (1): 73–80. PMID 21960143. S2CID 17149825. doi:10.1007/s00726-011-1089-6.
Devosse T, Dutoit R, Migeotte I, De Nadai P, Imbault V, Communi D, Salmon I, Parmentier M. Processing of HEBP1 by cathepsin D gives rise to F2L, the agonist of formyl peptide receptor 3. Journal of Immunology. August 2011, 187 (3): 1475–85. PMID 21709160. doi:10.4049/jimmunol.1003545 .
Mariani E, Seripa D, Ingegni T, Nocentini G, Mangialasche F, Ercolani S, Cherubini A, Metastasio A, Pilotto A, Senin U, Mecocci P. Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer's disease. Journal of the Neurological Sciences. September 2006, 247 (2): 187–91. PMID 16784755. S2CID 34224448. doi:10.1016/j.jns.2006.05.043.
Heinrich M, Wickel M, Schneider-Brachert W, Sandberg C, Gahr J, Schwandner R, Weber T, Saftig P, Peters C, Brunner J, Krönke M, Schütze S. Cathepsin D targeted by acid sphingomyelinase-derived ceramide. The EMBO Journal. October 1999, 18 (19): 5252–63. PMC 1171596 . PMID 10508159. doi:10.1093/emboj/18.19.5252.

semanticscholar.org (Global: 15^th place; Chinese: 141^st place)

api.semanticscholar.org

Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nature Structural Biology. October 1998, 5 (10): 866–71 [2022-09-18]. PMID 9783744. S2CID 5685201. doi:10.1038/2306. （原始内容存档于2022-09-22）.
Kim SJ, Kim KH, Ahn ER, Yoo BC, Kim SY. Depletion of cathepsin D by transglutaminase 2 through protein cross-linking promotes cell survival. Amino Acids. January 2013, 44 (1): 73–80. PMID 21960143. S2CID 17149825. doi:10.1007/s00726-011-1089-6.
Mariani E, Seripa D, Ingegni T, Nocentini G, Mangialasche F, Ercolani S, Cherubini A, Metastasio A, Pilotto A, Senin U, Mecocci P. Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer's disease. Journal of the Neurological Sciences. September 2006, 247 (2): 187–91. PMID 16784755. S2CID 34224448. doi:10.1016/j.jns.2006.05.043.

web.archive.org (Global: 1^st place; Chinese: 1^st place)

Entrez Gene: CTSD cathepsin D. [2022-09-18]. （原始内容存档于2010-04-12）.
Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nature Structural Biology. October 1998, 5 (10): 866–71 [2022-09-18]. PMID 9783744. S2CID 5685201. doi:10.1038/2306. （原始内容存档于2022-09-22）.

worldcat.org (Global: 4^th place; Chinese: 4^th place)

Jha, Sawan Kumar; Rauniyar, Khushbu; Chronowska, Ewa; Mattonet, Kenny; Maina, Eunice Wairimu; Koistinen, Hannu; Stenman, Ulf-Håkan; Alitalo, Kari; Jeltsch, Michael. KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D. eLife. 2019-05-17, 8: –44478. ISSN 2050-084X. PMC 6588350 . PMID 31099754. doi:10.7554/eLife.44478.

zenodo.org (Global: 737^th place; Chinese: 1,063^rd place)

Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nature Structural Biology. October 1998, 5 (10): 866–71 [2022-09-18]. PMID 9783744. S2CID 5685201. doi:10.1038/2306. （原始内容存档于2022-09-22）.

组织蛋白酶D (Chinese Wikipedia)

adsabs.harvard.edu (Global: 14th place; Chinese: 27th place)

ui.adsabs.harvard.edu

archive.org (Global: 6th place; Chinese: 2nd place)

books.google.com (Global: 3rd place; Chinese: 6th place)

doi.org (Global: 2nd place; Chinese: 5th place)

ensembl.org (Global: 630th place; Chinese: 669th place)