Cystatin (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Cystatin" in English language version.

refsWebsite

Global rank English rank

9nih.gov

4^th place

7doi.org

2^nd place

3semanticscholar.org

11^th place

8^th place

2harvard.edu

18^th place

17^th place

doi.org

Salát J, Paesen GC, Rezácová P, Kotsyfakis M, Kovárová Z, Sanda M, et al. (July 2010). "Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata". The Biochemical Journal. 429 (1): 103–112. doi:10.1042/BJ20100280. PMC 3523712. PMID 20545626.; rendered with PyMOL
Rawlings ND, Barrett AJ (January 1990). "Evolution of proteins of the cystatin superfamily". Journal of Molecular Evolution. 30 (1): 60–71. Bibcode:1990JMolE..30...60R. doi:10.1007/BF02102453. PMID 2107324. S2CID 33504413.
Abrahamson M, Alvarez-Fernandez M, Nathanson CM (2003). "Cystatins". Biochemical Society Symposium. 70 (70): 179–199. doi:10.1042/bss0700179. PMID 14587292.
Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213–219. Bibcode:1991FEBSL.285..213T. doi:10.1016/0014-5793(91)80804-C. PMID 1855589. S2CID 40444629.
Machleidt W, Borchart U, Fritz H, Brzin J, Ritonja A, Turk V (November 1983). "Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes". Hoppe-Seyler's Zeitschrift für physiologische Chemie. 364 (11): 1481–1486. doi:10.1515/bchm2.1983.364.2.1481. PMID 6689312.
van Wyk SG, Du Plessis M, Cullis CA, Kunert KJ, Vorster BJ (November 2014). "Cysteine protease and cystatin expression and activity during soybean nodule development and senescence". BMC Plant Biology. 14: 294. doi:10.1186/s12870-014-0294-3. PMC 4243279. PMID 25404209.
Kocevar N, Obermajer N, Kreft S (September 2008). "Membrane permeability of acylated cystatin depends on the fatty acyl chain length". Chemical Biology & Drug Design. 72 (3): 217–224. doi:10.1111/j.1747-0285.2008.00693.x. PMID 18702630. S2CID 24573152.

harvard.edu

ui.adsabs.harvard.edu

Rawlings ND, Barrett AJ (January 1990). "Evolution of proteins of the cystatin superfamily". Journal of Molecular Evolution. 30 (1): 60–71. Bibcode:1990JMolE..30...60R. doi:10.1007/BF02102453. PMID 2107324. S2CID 33504413.
Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213–219. Bibcode:1991FEBSL.285..213T. doi:10.1016/0014-5793(91)80804-C. PMID 1855589. S2CID 40444629.

nih.gov

pubmed.ncbi.nlm.nih.gov

Salát J, Paesen GC, Rezácová P, Kotsyfakis M, Kovárová Z, Sanda M, et al. (July 2010). "Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata". The Biochemical Journal. 429 (1): 103–112. doi:10.1042/BJ20100280. PMC 3523712. PMID 20545626.; rendered with PyMOL
Rawlings ND, Barrett AJ (January 1990). "Evolution of proteins of the cystatin superfamily". Journal of Molecular Evolution. 30 (1): 60–71. Bibcode:1990JMolE..30...60R. doi:10.1007/BF02102453. PMID 2107324. S2CID 33504413.
Abrahamson M, Alvarez-Fernandez M, Nathanson CM (2003). "Cystatins". Biochemical Society Symposium. 70 (70): 179–199. doi:10.1042/bss0700179. PMID 14587292.
Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213–219. Bibcode:1991FEBSL.285..213T. doi:10.1016/0014-5793(91)80804-C. PMID 1855589. S2CID 40444629.
Machleidt W, Borchart U, Fritz H, Brzin J, Ritonja A, Turk V (November 1983). "Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes". Hoppe-Seyler's Zeitschrift für physiologische Chemie. 364 (11): 1481–1486. doi:10.1515/bchm2.1983.364.2.1481. PMID 6689312.
van Wyk SG, Du Plessis M, Cullis CA, Kunert KJ, Vorster BJ (November 2014). "Cysteine protease and cystatin expression and activity during soybean nodule development and senescence". BMC Plant Biology. 14: 294. doi:10.1186/s12870-014-0294-3. PMC 4243279. PMID 25404209.
Kocevar N, Obermajer N, Kreft S (September 2008). "Membrane permeability of acylated cystatin depends on the fatty acyl chain length". Chemical Biology & Drug Design. 72 (3): 217–224. doi:10.1111/j.1747-0285.2008.00693.x. PMID 18702630. S2CID 24573152.

ncbi.nlm.nih.gov

Salát J, Paesen GC, Rezácová P, Kotsyfakis M, Kovárová Z, Sanda M, et al. (July 2010). "Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata". The Biochemical Journal. 429 (1): 103–112. doi:10.1042/BJ20100280. PMC 3523712. PMID 20545626.; rendered with PyMOL
van Wyk SG, Du Plessis M, Cullis CA, Kunert KJ, Vorster BJ (November 2014). "Cysteine protease and cystatin expression and activity during soybean nodule development and senescence". BMC Plant Biology. 14: 294. doi:10.1186/s12870-014-0294-3. PMC 4243279. PMID 25404209.

semanticscholar.org

api.semanticscholar.org

Rawlings ND, Barrett AJ (January 1990). "Evolution of proteins of the cystatin superfamily". Journal of Molecular Evolution. 30 (1): 60–71. Bibcode:1990JMolE..30...60R. doi:10.1007/BF02102453. PMID 2107324. S2CID 33504413.
Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213–219. Bibcode:1991FEBSL.285..213T. doi:10.1016/0014-5793(91)80804-C. PMID 1855589. S2CID 40444629.
Kocevar N, Obermajer N, Kreft S (September 2008). "Membrane permeability of acylated cystatin depends on the fatty acyl chain length". Chemical Biology & Drug Design. 72 (3): 217–224. doi:10.1111/j.1747-0285.2008.00693.x. PMID 18702630. S2CID 24573152.