[41] Cathepsin B, cathepsin H, and cathepsin L
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CTSB was more active in DS lysosomes.
“Notably, CTSB, a lysosomal exopeptidase with a pH optimum in the mildly acidic range (Barrett and Kirschke, 1981), was more active in DS lysosomes.”
From Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99) (2019) · cites this paper as Barrett and Kirschke, 1981
CTSB is a lysosomal exopeptidase with a pH optimum in the mildly acidic range.
“Notably, CTSB, a lysosomal exopeptidase with a pH optimum in the mildly acidic range (Barrett and Kirschke, 1981), was more active in DS lysosomes.”
From Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99) (2019) · cites this paper as Barrett and Kirschke, 1981
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Androgens regulate bone resorption activity of isolated osteoclasts <i>in vitro</i>
Pederson, L., Kremer, M., Judd, J., Pascoe, D., Spelsberg, T. C., Riggs, B. L., & Oursler, M. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.505 · Cited by 123 · see citing works
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ANNAND, R. R., DAHLEN, J. R., SPRECHER, C. A., DREU, P. D., FOSTER, D. C., MANKOVICH, J. A., TALANIAN, R. V., KISIEL, W., & GIEGEL, D. A. (1999) · Biochemical Journal · doi:10.1042/bj3420655 · Cited by 106 · see citing works
Cathepsin D in Podocytes Is Important in the Pathogenesis of Proteinuria and CKD
Yamamoto-Nonaka, K., Koike, M., Asanuma, K., Takagi, M., Oliva Trejo, J. A., Seki, T., Hidaka, T., Ichimura, K., Sakai, T., Tada, N., et al. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015040366 · Cited by 59 · see citing works
Involvement of cystatin C in pathophysiology of CNS diseases
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Bruno, M. A., Trejo, S. A., Avilés, X. F., Caffini, N. O., & López, L. M. I. (2006) · The Protein Journal · doi:10.1007/s10930-006-9005-8 · Cited by 29 · see citing works
- Authors
- Barrett, A. J., & Kirschke, H.
- ORCID
- Barrett, Alan J.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1981
- Volume
- 80 Pt C
- Pages
- 535-561
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W1484675846
- Cited by
- 1,698
- References
- 0
- Citations by year
- 2026: 5 · 2025: 19 · 2024: 8 · 2023: 10 · 2022: 19 · 2021: 16 · 2020: 18 · 2019: 18 · 2018: 18 · 2017: 9 · 2016: 18 · 2015: 27 · 2014: 26 · 2013: 22 · 2012: 40
- FWCI
- 16.50
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pineapple and bromelain studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Keywords
- cathepsin B, cathepsin H, cathepsin L, lysosomal aspartic protease, enzyme purification, human liver, rat liver, DEAE-cellulose chromatography, concanavalin A-Sepharose, enzyme inhibitors
- MeSH terms
- Animals, Binding Sites, Cathepsin B, Cathepsins, Cysteine Endopeptidases, Humans, Indicators and Reagents, Endopeptidases, Rats, Cathepsin H, Cathepsin L
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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