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.
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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
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
Items 201–294 of 294
Tomino, Y. (2001) · KARGER eBooks · doi:10.1159/000060137 · Cited by 11
Collé, A., Tavera, C., Laurent, P., Leung-Tack, J., & Girolami, J. P. (1990) · Journal of Immunoassay · doi:10.1080/01971529008053269 · Cited by 11
Yamashita, M., & Eguchi, M. (1987) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(87)90198-2 · Cited by 11
Chaudhuri, A., Biswas, S., & Chakraborty, S. S. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1429311 · Cited by 10
Gupta‐Malhotra, M., Levine, D. M., Cooper, R., & Zabriskie, J. B. (2003) · Cardiology · doi:10.1159/000070668 · Cited by 10
Gompou, A., Perrea, D. N., Karatzas, T., Bellos, J. K., Kastania, A., Boletis, I. N., & Kostakis, A. I. (2015) · Transplantation Proceedings · doi:10.1016/j.transproceed.2015.04.084 · Cited by 9
Action of Carica papaya latex on cell wall glycosidases from Lactuca sativa pith
Giordani, R., & Lafon, L. (1993) · Phytochemistry · doi:10.1016/s0031-9422(00)90830-6 · Cited by 9
Simulation of the inhibitory cystatin surface by a synthetic peptide
Moreau, T., Hoebeke, J., Lalmanach, G., Hattab, M., & Gauthier, F. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91738-e · Cited by 9
Characteristics, Structure, and Biological Role of Stefins (Type-1 Cystatins) of Human,
Türk, V., Turk, D., Dolenc, I., & Stoka, V. (2019) · Acta chimica slovenica · doi:10.17344/acsi.2018.4639 · Cited by 8
Ahn, S. J., Bak, H. J., Park, J. H., Lee, J., Kim, N. Y., Han, J. W., Jo, H. I., Chung, J. K., & Lee, H. H. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0248-5 · Cited by 8
Papain-like Cysteine Proteases and Their Implications in Neurodegenerative Diseases
Brömme, D., & Petanceska, S. S. (2002) · Springer eBooks · doi:10.1007/0-306-46847-6_4 · Cited by 8
Larsson, L., Alumets, J., Eriksson, B. K., Håkanson, R., Lundquist, G., Öberg, K., & Sundler, F. (1992) · Endocrine Pathology · doi:10.1007/bf02921339 · Cited by 8
[Cystatin C in the evaluation of renal function].
Delanaye, P., Chapelle, J.-P., GIELEN, J. E., Krzesinski, J.-M., & Rorive, G. L. (2003) · PubMed · Cited by 8
Acidic Cysteine Proteinase Inhibitor in Seminal Plasma
Minakata, K., & Asano, M. (1985) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1985.366.1.15 · Cited by 8
Chaparro, O., Yu, W.-H. A., & Shaw, P. A. (1997) · Archives of Oral Biology · doi:10.1016/s0003-9969(97)00042-3 · Cited by 8
Biomarkers in acute kidney injury and cirrhosis
Lima, C., & Macedo, E. M. (2024) · Journal of Translational Critical Care Medicine · doi:10.1097/jtccm-d-23-00014 · Cited by 7
Cystatin C and Kidney Function Recovery in Patients Requiring Continuous KRT for Acute Kidney Injury
Haeger, S. M., Okamura, K., Li, A. S., He, Z., Park, B. D., Budnick, I. M., Foulon, N., Kennis, M., Blaine, R. E., Miyazaki, M., et al. (2024) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.0000000000000531 · Cited by 7
Shah, A., Priyadarshini, M., Khan, M. S., Aatif, M., Amin, F., & Bano, B. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0383-z · Cited by 7
Human cystatin C in fibrotic diseases
Lalmanach, G., Rigoux, B., David, A., Tahri-Joutey, M., Lecaille, F., Marchand-Adam, S., & Saidi, A. (2024) · Clinica Chimica Acta · doi:10.1016/j.cca.2024.120016 · Cited by 8
Cystatin C is associated with poor survival in amyotrophic lateral sclerosis patients
Jiang, Q., Guo, Y., Yang, T., Li, S., Hou, Y., Lin, J., Xiao, Y., Ou, R., Wei, Q., & Shang, H. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1309568 · Cited by 7
Serum Cystatin C for Assessment of Glomerular Filtration Rate in Hypertensive Disorders of Pregnancy
Moodley, J., Gangaram, R., Khanyile, R., & Ojwang, P. (2004) · Hypertension in Pregnancy · doi:10.1081/prg-200030345 · Cited by 7
Evangelopoulos, A. A., Vallianou, N. G., Bountziouka, V. P., Giotopoulou, A. N., Bonou, M. S., Barbetseas, J. D., Avgerinos, P. C., & Panagiotakos, D. B. (2010) · Cardiology Research and Practice · doi:10.4061/2011/163281 · Cited by 7
Nation, A., Cui, S., & Selwood, L. (2008) · Reproduction · doi:10.1530/rep-08-0159 · Cited by 7
Testatin transgenic and knockout mice exhibit normal sex-differentiation
Hasegawa, K., Chuma, S., Tada, T., Sakurai, T., Tamura, M., Suemori, H., & Nakatsuji, N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.183 · Cited by 7
MNDO study of the mechanism of the inhibition of cysteine proteinases by diazomethyl ketones
Tarnowska, M., Ołdziej, S., Liwo, A., Kania, P., Kasprzykowski, F., & Grzonka, Z. (1992) · European Biophysics Journal · doi:10.1007/bf00196766 · Cited by 7
Demonstration of sequence variations in the promoter region of the human cystatin C gene
Balbı́n, M., GRUBB, A. O., & Abrahamson, M. (1992) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1992.373.2.471 · Cited by 7
Self-citationAllsop, D. (1986) · Springer eBooks · doi:10.1007/978-94-009-4309-4_25 · Cited by 7
Cysteine proteinase inhibitors in human placenta
Warwas, M., & Sawicki, G. (1985) · Placenta · doi:10.1016/s0143-4004(85)80023-0 · Cited by 6
Cystatin C is a glucocorticoid response gene predictive of cancer immunotherapy failurePreprint
Kleeman, S. O., Ferrer, M., Demestichas, B., Bankier, S., Lee, H., Heywood, T., Ruusalepp, A., Bjorkegren, J. L. M., Walker, B., Meyer, H. V., et al. (2021) · medRxiv · doi:10.1101/2021.08.17.21261668 · Cited by 4
Yang, W., Zhang, S., Zhang, S., & Zhu, Y. (2018) · Clinical and Experimental Hypertension · doi:10.1080/10641963.2016.1248769 · Cited by 5
Differential Expression of Neutrophilic Granule Proteins between Th1 and Th2 Cells
Xie, D., Liu, Z., Li, Z., Ji, Y., Chen, J., & Sun, B. (2007) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2007.00242.x · Cited by 5
Reaction mechanism of HSH and CH3SH with NH2CH2COCH2X (X = F and Cl) molecules
Vijayakumar, S., & Kolandaivel, P. G. (2007) · International Journal of Quantum Chemistry · doi:10.1002/qua.21555 · Cited by 5
Zolezzi, C., Ferrari, S. M., Fasano, M., Telentinis, L., Bacci, G., & Pizzoferrato, A. (2001) · Journal of Chemotherapy · doi:10.1179/joc.2001.13.3.316 · Cited by 5
A Rapid Two-Step Purification of Rat Cystatin C, One Major Inhibitor of Cysteine Proteinases
Tavera, C., Guillemot, J.-C., Capdevielle, J., Ferrara, P., Leung-Tack, J., & Collé, A. (1989) · Preparative Biochemistry · doi:10.1080/10826068908544918 · Cited by 5
Chen, D., Jiang, L., Tan, Y. L., Zhao, J., Huang, W., Pan, B., & Wan, X. H. (2023) · Renal Failure · doi:10.1080/0886022x.2023.2194444 · Cited by 5
Xiong, H., Wang, L., Jin, F., Zhang, B., Wang, X., Chang, X., & Zhao, L. (2021) · Medicine · doi:10.1097/md.0000000000026761 · Cited by 4
Cysteine proteinase inhibitor levels in semen
Minakata, K., Asano, M., & Yonekawa, O. (1986) · Clinical Biochemistry · doi:10.1016/s0009-9120(86)80018-2 · Cited by 4
Lysosomes and prohormone activation
Hales, C. N. (1985) · Nature · doi:10.1038/314020a0 · Cited by 4
Enhancement of Testicular Cysteine Proteinase Inhibitor Level in Vitamin E–Deficient Rats
Minakata, K., Asano, M., Takahashi, Y., & Harada, N. (1987) · Journal of Nutrition · doi:10.1093/jn/117.8.1416 · Cited by 4
Liang, Y., Liang, S., Huang, J., Hu, L., Wu, Q., Li, Z., Pan, C., He, Y., Zhou, X., & Chen, C. (2024) · BMC Cardiovascular Disorders · doi:10.1186/s12872-024-04408-7 · Cited by 3
Bricon, T. L., Thervet, É., Legendre, C., & Erlich, D. (2000) · Immuno-analyse & Biologie Spécialisée · doi:10.1016/s0923-2532(00)89072-9 · Cited by 3
Ausencia de implicación de la cistatina C en el remodelado ventricular y la insuficiencia cardiaca
Pérez‐Calvo, J. I., Castiella, T., Barjud, M. B., Josa‐Laorden, C., Marteles, M. S., Lacambra, I., Lopez, M., & Pascual-Figal, D. A. (2015) · Revista Clínica Española · doi:10.1016/j.rce.2015.11.003 · Cited by 3
Absence of cystatin C involvement in ventricular remodelling and heart failure
Pérez‐Calvo, J. I., Muruzábal, T. C., Barjud, M. B., Laorden, C. J., Marteles, M. S., Lacambra, I., Lopez, M., & Pascual-Figal, D. A. (2016) · Revista Clínica Española (English Edition) · doi:10.1016/j.rceng.2015.12.002 · Cited by 3
Serum cystatin C as a potential biomarker for the evaluation COPD.
Zhang, Y., Zhu, Y., Wu, Y., Wang, G., Xie, X., Ke, R., Li, S., Liu, L., Fen, W., Li, F., et al. (2014) · PubMed Central · Cited by 3
Ludueña, R. F. (1997) · Springer eBooks · doi:10.1007/978-3-642-95866-3_18 · Cited by 3
Rinno, H., Iijima, T., Takeda, Y., Shimizu, A., Kobata, M., Gohda, T., Saito, K., & Tomino, Y. (2002) · Acta Nephrologica · Cited by 2
Clinical Biochemistry of the Central Nervous System
Firth, G., Cowdrey, G., & Frost, S. J. (1994) · Elsevier eBooks · doi:10.1016/b978-0-7506-0167-2.50037-6 · Cited by 2
Blood pressure, renal functional and structural changes, in normal and preeclamptic pregnancy
Strevens, H. (2002) · Lund University Publications (Lund University) · Cited by 2
Larsson, L., Alumets, J., Håkanson, R., Simonsson, M., & Sundler, F. (1990) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01600296 · Cited by 2
The high alkaline fraction on isoelectric focusing of cerebrospinal fluid is cystatin C
Roelandse, F. W. C., Amons, R., ter Braak, E. P., Nieuwland, R., van Loon, J., & Souverijn, J. H. M. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00055-0 · Cited by 2
Toku, S., Fukuyama, K., & Epstein, W. L. (1987) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(87)90146-2 · Cited by 2
Hereditary Central Nervous System γ-Trace Amyloid Angiopathy and Stroke in Icelandic Families
Jensson, Ó., Guðmundsson, G., Árnason, A., Blöndal, H., Grugg, A., & Löfberg, H. (1986) · Springer eBooks · doi:10.1007/978-1-4613-2199-6_99 · Cited by 2
Inhibitors of Papain-Like Cysteine Peptidases in Cancer
Shridhar, R., Sloane, B. F., & KEPPLER, D. O. R. (2000) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-57092-6_16 · Cited by 2
Lu, S., Wang, Y., Zhou, Z., Zhang, Y., Yang, L., & Yang, X. (2025) · Updates in Surgery · doi:10.1007/s13304-025-02208-y · Cited by 1
Pytelková, J., Orsághová, K., Beňová, M., Horn, M., Schabussova, I., & Mareš, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148383 · Cited by 2
Mathew, G. G. (2025) · Irish Journal of Medical Science (1971 -) · doi:10.1007/s11845-025-04221-x · Cited by 1
Nakamura, K., Maeda, Y., Morimoto, K., Katayama, S., Kondo, K., & Nakamura, S. (2013) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1079 · Cited by 1
Nakamura, S. (2005) · Nutraceutical science and technology · doi:10.1201/9781420028836.ch12 · Cited by 1
Conventional and emerging renal biomarkers
Ford, S. M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404630-6.00014-2 · Cited by 1
Domain swapping as a molecular mechanism in amyloidosis
Wahlbom, M. (2007) · Lund University Publications (Lund University) · Cited by 1
Quantification and Clinical Relevance of Cystatin C
Ristiniemi, N. (2014) · UTUPub (University of Turku) · Cited by 1
Cystatin: a novel bioactive protein.
Nakamura, S., Mine, Y., & Shahidi, F. (2006) · Cited by 1
(1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.10.1167 · Cited by 1
Post-translational Proteolytic Processing on Intracellular Proteins by Cathepsins and Cystatins
Katunuma, N., Takahashi, M., & Tezuka, T. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_18
Pillay, W. R. (2003) · ResearchSpace (University of KwaZulu-Natal)
Glycan-based biomarkers for the quality assurance in stem cell therapy
Montacir, H. (2014) · Refubium (Universitätsbibliothek der Freien Universität Berlin) · doi:10.17169/refubium-8658
Chapter 7 Cerebrovascular Disease
Penix, L. P., & Lanska, D. J. (1999) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60027-9
Cabrera‐Lafuente, M. (2014) · Biblos-e Archivo (Universidad Autónoma de Madrid)
Wallin, H. (2013) · Lund University Publications (Lund University)
Molecular biology of progressive myoclonus epilepsy of Unverricht-Lundborg type (EPM1)
Alakurtti, K. (2006) · Työväentutkimus Vuosikirja
Cystatin S: Molecular biology and sympathetic innervation
Shaw, P. A., & Chaparro, O. (1998) · Biomedical Reviews · doi:10.14748/bmr.v9.134
Predictive factors in esophageal carcinoma.
Dreilich, M. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Acute kidney injury in cardiac surgery
Ristikankare, A. (2015) · Työväentutkimus Vuosikirja
Recent Research on Genetic Regulation and Function of Some Serum Proteins
Grubb, R. (1986) · Advances in forensic haemogenetics · doi:10.1007/978-3-642-71150-3_9
Cystatine C : point d'étape et perspectives Cystatin C: current step and future prospects
Delanaye, P., Piéroni, L., Mariat, C., & Froissart, M. (2008)
Cohen, D. H., Feiner, H. D., Jensson, Ó., & Frangione, B. (1986) · Springer eBooks · doi:10.1007/978-1-4613-2199-6_96
Production of Monoclonal Antibodies to Dog Post-Gamma Globulin
Poulik, M. D., Piston, S., Prepolec, M., & CHEN, J. C. (1985) · Protides of the biological fluids · doi:10.1016/b978-0-08-033215-4.50151-5
Chromogranin A to Cytochrome C Oxidase
Haeberli, A. (1998) · doi:10.1002/9783527619764.ch4
Cowdrey, G. (1991) · OpenGrey (Institut de l'Information Scientifique et Technique)
Jaskólski, M., & GRUBB, A. O. (2005) · doi:10.1002/9783527619344.ch27
Self-citationАндреевич, Х. А., Abdulkarim, D., Vlasenko, S., Александрович, А. С., Scherbak, S., Popov, V., Vorobyovskii, D., Васильевич, А. М., Михайлович, С. А., & Karmazanashvili, E. (2019) · World Journal of Cardiovascular Diseases · doi:10.4236/wjcd.2019.912083
Novos Marcadores de Lesão Renal Aguda
Nascimento, H. F. M. (2012) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · doi:10.34626/qms1-a492
Biomarkers of renal and hepatic failure
Plebani, M., Mion, M. M., & Zaninotto, M. (2021) · Oxford University Press eBooks · doi:10.1093/med/9780198849346.003.0036
(2005) · Elsevier eBooks · doi:10.1016/b978-012369369-3/50020-5
Conventional and Emerging Renal Biomarkers
Ford, S. M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814655-2.00015-3
Cystatin C and lipocalin — endogenous markers of glomerular filtration in children born prematurely
Tsintsadze, B. D. (2022) · Russian Pediatric Journal · doi:10.46563/1560-9561-2022-25-3-206-211
Increased serum cystatin C levels in patients with idiopathic epiretinal membrane
Hu, W., Huang, Y., Kou, P., & Huang, X. (2023) · Clinical and Experimental Optometry · doi:10.1080/08164622.2023.2215381
Liang, Y., Liang, S., Wu, Q., Huang, J., Hu, L., Li, Z., Pan, C., He, Y., Zhou, X., & Chen, C. (2023) · Research Square · doi:10.21203/rs.3.rs-3412912/v1
Monomer‐Dimer Equilibrium of Human Cystatin C During Internalization Into Cancer Cells
Jurczak, P., Fayad, N., Bénard, M., Czaplewska, P., & Hildebrandt, N. (2024) · ChemBioChem · doi:10.1002/cbic.202400226
Solichová, P., Vašutová, I., Buček, P., Kubíček, Z., & Stejskal, D. (2006) · Klinická biochemie a metabolismus · doi:10.61568/kbm.2006.014
Xie, L. (2007) · UA Campus Repository (The University of Arizona)
Pathobiological Aspects of Nonreheumatic Aortic Valve Stenosis
Helske, S. (2007) · Työväentutkimus Vuosikirja
Acute renal failure in critically ill patients : With special reference to prediction of outcome
Åhlström, A. (2006) · Työväentutkimus Vuosikirja
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
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