The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
The place of human γ-trace (cystatin C) amongst the cysteine proteinase inhibitors
Abstract
Native gamma-trace, a small basic protein present in high concentration in cerebrospinal fluid, semen and neuroendocrine cells, but of unknown biological function, is shown to be a potent inhibitor of the cysteine proteinases papain, ficin, and human cathepsins B, H and L. It proves to be the tightest -binding protein inhibitor of cathepsin B so far discovered. The name cystatin C is proposed for gamma-trace to reflect the many similarities in activity and structure to chicken egg-white cystatin and mammalian cystatins A and B. The inhibition constants of cystatin C, taken together with its widespread distribution in human tissues and extracellular fluids, suggest that a physiological function could well be the regulation of cysteine proteinase activity.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“CyC is biologically active as a potent cysteine protease inhibitor,74”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
In the citing paper
“CyC levels are highest in cerebrospinal and seminal fluid,74”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
In the citing paper
“CyC is a known potent inhibitor of cysteine proteases,74 such as those involved in antigen presentation,75”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
Citations
Cites
Anastasi, A., Brown, M. A., Kembhavi, A. A., Nicklin, M. J. H., Sayers, C. A., Sunter, D. C., & Barrett, A. J. (1983) · Biochemical Journal · doi:10.1042/bj2110129 · Cited by 314
Self-citationLöfberg, H., & GRUBB, A. O. (1979) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365517909108866 · Cited by 208
Self-citationHuman cystatin, a new protein inhibitor of cysteine proteinases
Brzin, J., Popovič, T., Türk, V., Borchart, U., & Machleidt, W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91073-8 · Cited by 182
Cystatin-like cysteine proteinase inhibitors from human liver
Green, G. D. J., Kembhavi, A. A., Davies, M., & Barrett, A. J. (1984) · Biochemical Journal · doi:10.1042/bj2180939 · Cited by 153
Self-citationLimited autolysis reduces the Ca2+ requirement of a smooth muscle Ca2+-activated protease.
Hathaway, D. R., Werth, D. K., & Haeberle, J. R. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34244-3 · Cited by 138
Türk, V., Brzin, J., LONGER, M., Ritonja, A., EROPKIN, M., Borchart, U., & Machleidt, W. (1983) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1983.364.2.1487 · Cited by 126
[57] Cystatin, the egg white inhibitor of cysteine proteinases
Barrett, A. J. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)80059-6 · Cited by 122
Self-citationThe occurrence of post-gamma protein in urine: a new protein abnormality
Butler, E. A., & Flynn, F. V. (1961) · Journal of Clinical Pathology · doi:10.1136/jcp.14.2.172 · Cited by 117
Brzin, J., Kopitar, M., Türk, V., & Machleidt, W. (1983) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1983.364.2.1475 · Cited by 109
Järvinen, M., & Rinne, A. (1982) · PubMed · Cited by 105
MACHLEIDT, W., Borchart, U., Fritz, H., Brzin, J., Ritonja, A., & Türk, V. (1983) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1983.364.2.1481 · Cited by 102
The Slow, Tight‐Binding Inhibition of Cathepsin B by Leupeptin
Baici, A., & GYGER‐MARAZZI, M. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb07017.x · Cited by 96
Human spleen cysteineproteinase inhibitor
Järvinen, M., & Rinne, A. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90222-9 · Cited by 91
Cystatin. Amino acid sequence and possible secondary structure
Schwabe, C., Anastasi, A., Crow, H., McDonald, J. K., & Barrett, A. J. (1984) · Biochemical Journal · doi:10.1042/bj2170813 · Cited by 82
Self-citationAmino acid sequence of rat liver thiol proteinase inhibitor
Takio, K., Kominami, E., Wakamatsu, N., Katunuma, N., & Titani, K. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(83)80020-5 · Cited by 71
IMMUNOCHEMICAL EVIDENCE FOR A GAMMA GLOBULIN PECULIAR TO CEREBROSPINAL FLUID
Macpherson, C. F., & Cosgrove, J. B. R. (1961) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o61-170 · Cited by 66
Löfberg, H., GRUBB, A. O., & Brun, A. E. (1981) · Biomedical Research · doi:10.2220/biomedres.2.298 · Cited by 51
Self-citationLow molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF
Lenney, J. F., Liao, J. R., Sugg, S. L., Gopalakrishnan, V., Wong, H. C. H., Ouye, K. H., & Chan, P. W. H. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(82)80088-0 · Cited by 35
Chicken α2-proteinase inhibitor: A serum protein homologous with ovoinhibitor of egg white
Barrett, A. J. (1974) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(74)90154-8 · Cited by 30
Self-citationGrubb, A. O., Weiber, H., & Lofberg, H. (1983) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.1080/00365518309168281 · Cited by 26
Self-citationA heat stable low molecular weight inhibitor of lysosomal cysteine proteinases in human serum
Gauthier, F., Pagano, M., Esnard, F., Mouray, H., & Engler, R. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)91170-1 · Cited by 26
Partial amino acid sequence of two forms of human Post-γ-globulin
Tonnelle, C., Collé, A., Fougereau, M., & Manuel, Y. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91757-1 · Cited by 25
Localization of three inhibitors of cysteineproteinases in the human oral mucosa
Järvinen, M., Pernu, H., Rinne, A., Hopsu‐Havu, V. K., & Altonen, M. (1983) · Acta Histochemica · doi:10.1016/s0065-1281(83)80039-7 · Cited by 19
Existence of two kinds of thiol protease inhibitors in rat serum
Iwata, D., Hirado, M., Niinobe, M., & Fujii, S. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91424-3 · Cited by 19
Löfberg, H., Strömblad, L.-G., GRUBB, A. O., & Olsson, S.-O. R. (1981) · Biomedical Research · doi:10.2220/biomedres.2.527 · Cited by 18
Self-citationLöfberg, H., GRUBB, A. O., Davidsson, L., KJELLANDER, B., Strömblad, L. ‐., Tibblin, S., & Olsson, S. (1983) · European Journal of Endocrinology · doi:10.1530/acta.0.1040069 · Cited by 17
Self-citationDemonstration of γ-trace in normal endocrine cells of the adrenal medulla and in phaeochromocytoma
Löfberg, H., Nilsson, K., Strömblad, L. ‐., Lasson, Å., & Olsson, S.-O. R. (1982) · European Journal of Endocrinology · doi:10.1530/acta.0.1000595 · Cited by 12
Hirado, M., Niinobe, M., & Fujii, S. (1983) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(83)90109-5 · Cited by 10
Research works printed but not linked: 5
- Clausen, 1961, 107, 170
- Grubb, 1982, 79, 3024
- Grubb, 1983, Scand. J. Clin. Lab. Invest, 43, 421, 10.3109/00365518309168281 · DOI
- Davies, 1984, Histochemistry
- Bieth, 1980, Bull. Eur. Physiopath. Resp, 16, 183
Cited by
Sorted by citations
Cysteine cathepsins: From structure, function and regulation to new frontiers
Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., & Turk, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.002 · Cited by 1,377
The cystatins: Protein inhibitors of cysteine proteinases
Türk, V., & Bode, W. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80804-c · Cited by 822
Cystatin C as a marker of GFR—history, indications, and future research
Filler, G., Bökenkamp, A., Hofmann, W. J., Bricon, T. L., Martínez-Brú, C., & GRUBB, A. O. (2004) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2004.09.025 · Cited by 730
Self-citationNewman, D. J., Thakkar, H., Edwards, R. G., Wilkie, M. E., White, T., GRUBB, A. O., & Price, C. P. (1995) · Kidney International · doi:10.1038/ki.1995.40 · Cited by 646
Self-citationPathogenesis and Treatment of Chronic Kidney Disease: A Review of Our Recent Basic and Clinical Data
Tomino, Y. (2014) · Kidney & Blood Pressure Research · doi:10.1159/000368458 · Cited by 572
Metadata
- Authors
- Barrett, A. J., Davies, M. E., & Grubb, A.
- Affiliations
- University of Cambridge (GB)
- Lund University (SE)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1984-04
- Volume
- 120
- Issue
- 2
- Pages
- 631-636
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1984079474
- Cited by
- 294
- References
- 28
- Citations by year
- 2025: 3 · 2024: 7 · 2023: 4 · 2022: 1 · 2021: 5 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 8 · 2014: 9 · 2013: 12 · 2012: 2
- FWCI
- 8.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- cystatin C, cysteine protease inhibitors, papain, ficin, cathepsin B, cathepsin H, cathepsin L, tight-binding inhibition, cerebrospinal fluid, cystatin A, cystatin B
- MeSH terms
- Epitopes, Cathepsins, Drug Stability, Ficain, Humans, Kinetics, Papain, Protease Inhibitors, Proteins, Cystatins, Cystatin C
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
