Structural and functional studies on a variant of cystatin purified from brain of Capra hircus

References

• Abrahamson, M. (1988). Human cysteine proteinase inhibitors. Isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhage. Scandinavian Journal of Clinical and Laboratory Investigation. Supplementum, 191, 21–31. doi:10.1080/00365518809168291
   PubMedGoogle Scholar
• Abrahamson, M., Alvarez-Fernandez, M., & Nathanson, C.-M. (2003). Cystatins. Biochemical Society Symposium, 70, 179–199. doi:10.1042/bss0700179
   PubMed Web of Science ®Google Scholar
• Abrahamson, M., Barrett, A. J., Salvesen, G., & Grubb, A. (1986). Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. The Journal of Biological Chemistry, 261, 11282–11289.
   PubMed Web of Science ®Google Scholar
• Amin, F., Khan, A. A., Rizvi, S. J., & Bano, B. (2011). Purification and characterizaion of buffalo brain cystatin. Protein and Peptide Letters, 18, 210–218. doi:10.2174/092986611794475011
   PubMed Web of Science ®Google Scholar
• Andrews, P. (1964). Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochemical Journal, 91, 222–233. doi:10.1042/bj0910222
   PubMed Web of Science ®Google Scholar
• Aramesh-Boroujeni, Z., Khorasani-Motlagh, M., & Noroozifar, M. (2015). Multispectroscopic DNA-binding studies of a terbium(III) complex containing 2,2′-bipyridine ligand. Journal of Biomolecular Structure and Dynamics, 34, 414–426. doi:10.1080/07391102.2015.1038585
   PubMed Web of Science ®Google Scholar
• Assfalg-Machleidt, I., Jochum, M., Klaubert, W., Inthorn, D., & Machleidt, W. (1988). Enzymatically active cathepsin B dissociating from its inhibitor complexes is elevated in blood plasma of patients with septic shock and some malignant tumors. Biological Chemistry Hoppe-Seyler, 369(Suppl), 263–269.
   PubMed Web of Science ®Google Scholar
• Baba, S. P., Zehra, S., & Bano, B. (2005). Purification and characterization of kininogens from sheep plasma. The Protein Journal, 24, 95–102. doi:10.1007/s10930-004-1516-6
   PubMed Web of Science ®Google Scholar
• Balbín, M., Hall, A., Grubb, A., Mason, R. W., López-Otín, C., & Abrahamson, M. (1994). Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. The Journal of Biological Chemistry, 269, 23156–23162.
   PubMed Web of Science ®Google Scholar
• Bernstein, H. G., Kirschke, H., Wiederanders, B., Pollak, K. H., Zipress, A., & Rinne, A. (1996). The possible place of cathepsins and cystatins in the puzzle of Alzheimer disease: A review. Molecular and Chemical Neuropathology/Sponsored by the International Society for Neurochemistry and the World Federation of Neurology and Research Groups on Neurochemistry and Cerebrospinal Fluid, 27, 225–247. doi:10.1007/BF02815106
   Google Scholar
• Bhat, W. F., Bhat, S. A., Khaki, P. S. S., & Bano, B. (2015). Employing in vitro analysis to test the potency of methylglyoxal in inducing the formation of amyloid-like aggregates of caprine brain cystatin. Amino Acids, 47, 135–146. doi:10.1007/s00726-014-1848-2
   PubMed Web of Science ®Google Scholar
• Björk, I., Alriksson, E., & Ylinenjärvi, K. (1989). Kinetics of binding of chicken cystatin to papain. Biochemistry, 28, 1568–1573. doi:10.1021/bi00430a022
   PubMed Web of Science ®Google Scholar
• Björk, I., Pol, E., Raub-Segall, E., Abrahamson, M., Rowan, A. D., & Mort, J. S. (1994). Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes. Biochemical Journal, 299, 219–225. doi:10.1042/bj2990219
   PubMed Web of Science ®Google Scholar
• Björk, I., & Ylinenjärvi, K. (1990). Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain A, and ficin. Biochemistry, 29, 1770–1776. doi:10.1021/bi00459a016
   PubMed Web of Science ®Google Scholar
• Blaydon, D. C., Nitoiu, D., Eckl, K.-M., Cabral, R. M., Bland, P., Hausser, I., … Kelsell, D. P. (2011). Mutations in CSTA, encoding cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesion. The American Journal of Human Genetics, 89, 564–571. doi:10.1016/j.ajhg.2011.09.001
   PubMed Web of Science ®Google Scholar
• Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., … Turk, V. (1988). The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. The EMBO Journal, 7, 2593–2599. doi:10.2210/pdb1cew/pdb
   PubMed Web of Science ®Google Scholar
• Bramanti, E., & Benedetti, E. (1996). Determination of the secondary structure of isomeric forms of human serum albumin by a particular frequency deconvolution procedure applied to Fourier transform IR analysis. Biopolymers, 38, 639–653. doi:10.1002/(SICI)1097-0282(199605)38:5<639:AID-BIP8>3.0.CO;2-T
   PubMed Web of Science ®Google Scholar
• Bui, A. L., Katz, R., Kestenbaum, B., de Boer, I. H., Fried, L. F., Polak, J. F., … Shlipak, M. G. (2009). Cystatin C and carotid intima-media thickness in asymptomatic adults: The multi-ethnic study of atherosclerosis (MESA). American Journal of Kidney Diseases, 53, 389–398. doi:10.1053/j.ajkd.2008.06.025
   PubMed Web of Science ®Google Scholar
• Butinar, M., Prebanda, M. T., Rajković, J., Jerič, B., Stoka, V., Peters, C., … Vasiljeva, O. (2014). Stefin B deficiency reduces tumor growth via sensitization of tumor cells to oxidative stress in a breast cancer model. Oncogene, 33, 3392–3400. doi:10.1038/onc.2013.314
   PubMed Web of Science ®Google Scholar
• Chen, Y.-H., Yang, J. T., & Martinez, H. M. (1972). Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 11, 4120–4131. doi:10.1021/bi00772a015
   PubMed Web of Science ®Google Scholar
• Chi, Z., & Liu, R. (2011). Phenotypic characterization of the binding of tetracycline to human serum albumin. Biomacromolecules, 12, 203–209. doi:10.1021/bm1011568
   PubMed Web of Science ®Google Scholar
• Chong, X., Lu, X., Wang, Y., Chang, A. K., Xu, L., Wang, N., … He, J. (2016). Distinct structural changes in wild-type and amyloidogenic chicken cystatin caused by disruption of C95-C115 disulfide bond. Journal of Biomolecular Structure & Dynamics, 1–9. doi:10.1080/07391102.2015.1126796
   PubMed Web of Science ®Google Scholar
• Cooper, A. (1999). Thermodynamic analysis of biomolecular interactions. Current Opinion in Chemical Biology, 3, 557–563. doi:10.1016/S1367-5931(99)00008-3
   PubMed Web of Science ®Google Scholar
• Delaissé, J. M., Ledent, P., & Vaes, G. (1991). Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase. Biochemical Journal, 279, 167–174. doi:10.1042/bj2790167
   PubMed Web of Science ®Google Scholar
• Djoussé, L., Kurth, T., & Gaziano, J. M. (2008). Cystatin C and risk of heart failure in the Physicians’ Health Study (PHS). American Heart Journal, 155, 82–86. doi:10.1016/j.ahj.2007.08.023
   PubMed Web of Science ®Google Scholar
• DuBois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., & Smith, F. (1956). Colorimetric method for determination of sugars and related substances. Analytical Chemistry, 28, 350–356. doi:10.1021/ac60111a017
   Web of Science ®Google Scholar
• Elliott, A., & Ambrose, E. J. (1950). Structure of synthetic polypeptides. Nature, 165, 921–922. doi:10.1038/165921a0
   PubMed Web of Science ®Google Scholar
• Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics, 82, 70–77. doi:10.1016/0003-9861(59)90090-6
   PubMed Web of Science ®Google Scholar
• Gauthier, S., Kaur, G., Mi, W., Tizon, B., & Levy, E. (2011). Protective mechanisms by cystatin C in neurodegenerative diseases. Frontiers in Bioscience (Scholar Edition), 3, 541–554.
   PubMedGoogle Scholar
• Grzonka, Z., Jankowska, E., Kasprzykowski, F., Kasprzykowska, R., Lankiewicz, L., Wiczk, W., … Grubb, A. (2001). Structural studies of cysteine proteases and their inhibitors. Acta Biochimica Polonica, 48(1), 1–20.
   PubMed Web of Science ®Google Scholar
• Hansson, S. F., Andréasson, U., Wall, M., Skoog, I., Andreasen, N., Wallin, A., … Blennow, K. (2009). Reduced levels of amyloid-beta-binding proteins in cerebrospinal fluid from Alzheimer’s disease patients. Journal of Alzheimer’s Disease: JAD, 16, 389–397. doi:10.3233/JAD-2009-0966
   PubMed Web of Science ®Google Scholar
• He, W., Li, Y., Xue, C., Hu, Z., Chen, X., & Sheng, F. (2005). Effect of Chinese medicine alpinetin on the structure of human serum albumin. Bioorganic & Medicinal Chemistry, 13, 1837–1845. doi:10.1016/j.bmc.2004.11.038
   PubMed Web of Science ®Google Scholar
• Herskovits, T. T., & Mescanti, L. (1965). Conformation of proteins and polypeptides. II. Optical rotatory dispersion and conformation of the milk proteins and other proteins in organic solvents. The Journal of Biological Chemistry, 240, 639–644.
   PubMed Web of Science ®Google Scholar
• Honey, K., & Rudensky, A. Y. (2003). Lysosomal cysteine proteases regulate antigen presentation. Nature Reviews. Immunology, 3, 472–482. doi:10.1038/nri1110
   PubMed Web of Science ®Google Scholar
• Jahani, S., Khorasani-Motlagh, M., & Noroozifar, M. (2016). DNA interaction of europium (III) complex containing 2,2′-bipyridine and its antimicrobial activity. Journal of Biomolecular Structure & Dynamics, 34, 612–624. doi:10.1080/07391102.2015.1048481
   PubMed Web of Science ®Google Scholar
• Jensson, O., Pálsdóttir, A., Thorsteinsson, L., Arnason, A., Abrahamson, M., Olafsson, I., & Grubb, A. (1990). Cystatin C mutation causing amyloid angiopathy and brain hemorrhage. Biological Chemistry Hoppe-Seyler, 371(Suppl), 229–232.
   PubMed Web of Science ®Google Scholar
• Kabanda, A., Goffin, E., Bernard, A., Lauwerys, R., & van Ypersele de Strihou, C. (1995). Factors influencing serum levels and peritoneal clearances of low molecular weight proteins in continuous ambulatory peritoneal dialysis. Kidney International, 48, 1946–1952. doi:10.1038/ki.1995.495
   PubMed Web of Science ®Google Scholar
• Kato, H., Nagasawa, S., & Iwanaga, S. (1981). HMW and LMW kininogens. Methods in Enzymology, 80, 172–198. doi:10.1016/S0076-6879(81)80017-1
   PubMed Web of Science ®Google Scholar
• Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39, 549–559. doi:10.1111/j.1745-7270.2007.00320.x
   PubMed Web of Science ®Google Scholar
• Kunitz, M. (1947). Crystalline soybean trypsin inhibitor: II. General properties. The Journal of General Physiology, 30, 291–310. doi:10.1085/jgp.30.4.291
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685. doi:10.1038/227680a0
   PubMed Web of Science ®Google Scholar
• Laurent, T. C., & Killander, J. (1964). A theory of gel filtration and its exeperimental verification. Journal of Chromatography A, 14, 317–330. doi:10.1016/S0021-9673(00)86637-6
   Web of Science ®Google Scholar
• Levy, E., Jaskolski, M., & Grubb, A. (2006). The role of cystatin C in cerebral amyloid angiopathy and stroke: Cell biology and animal models. Brain Pathology, 16, 60–70. doi:10.1111/j.1750-3639.2006.tb00562.x
   PubMed Web of Science ®Google Scholar
• Li, F., An, H., Seymour, T. A., & Barnes, D. W. (2000). Rainbow trout (Oncorhynchus mykiss) cystatin C: Expression in Escherichia coli and properties of the recombinant protease inhibitor. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 125, 493–502. doi:10.1016/S0305-0491(00)00156-5
   PubMed Web of Science ®Google Scholar
• Lieuallen, K., Pennacchio, L. A., Park, M., Myers, R. M., & Lennon, G. G. (2001). Cystatin B-deficient mice have increased expression of apoptosis and glial activation genes. Human Molecular Genetics, 10, 1867–1871. doi:10.1093/hmg/10.18.1867
   PubMed Web of Science ®Google Scholar
• Lombardi, G., Burzyn, D., Mundiñano, J., Berguer, P., Bekinschtein, P., Costa, H., … Nepomnaschy, I. (2005). Cathepsin-L influences the expression of extracellular matrix in lymphoid organs and plays a role in the regulation of thymic output and of peripheral T cell number. Journal of Immunology (Baltimore, Md. : 1950), 174, 7022–7032. doi:10.4049/jimmunol.174.11.7022
   PubMed Web of Science ®Google Scholar
• Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. The Journal of Biological Chemistry, 193, 265–275.
   PubMed Web of Science ®Google Scholar
• Lukasiuk, K., Pirttilä, T. J., & Pitkänen, A. (2002). Upregulation of cystatin C expression in the rat hippocampus during epileptogenesis in the amygdala stimulation model of temporal lobe epilepsy. Epilepsia, 43(Suppl. 5), 137–145. doi:10.1046/j.1528-1157.43.s.5.20.x
   PubMed Web of Science ®Google Scholar
• Martin, J. R., Craven, C. J., Jerala, R., Kroon-Zitko, L., Zerovnik, E., Turk, V., & Waltho, J. P. (1995). The three-dimensional solution structure of human stefin A. Journal of Molecular Biology, 246, 331–343. doi:10.1006/jmbi.1994.0088
   PubMed Web of Science ®Google Scholar
• McGeer, P. L., & McGeer, E. G. (1995). The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Research Reviews, 21, 195–218. doi:10.1016/0165-0173(95)00011-9
   PubMed Web of Science ®Google Scholar
• Miyazawa, T., & Blout, E. R. (1961). The infrared spectra of polypeptides in various conformations: Amide I and II Bands 1. Journal of the American Chemical Society, 83, 712–719. doi:10.1021/ja01464a042
   Web of Science ®Google Scholar
• Moran, A., Katz, R., Smith, N. L., Fried, L. F., Sarnak, M. J., Seliger, S. L., … Shlipak, M. G. (2008). Cystatin C concentration as a predictor of systolic and diastolic heart failure. Journal of Cardiac Failure, 14, 19–26. doi:10.1016/j.cardfail.2007.09.002
   PubMed Web of Science ®Google Scholar
• Narvaez-Sanchez, R., Gonzalez, L., Salamanca, A., Silva, M., Rios, D., Arevalo, S., … Sanchez, J. (2008). Cystatin C could be a replacement to serum creatinine for diagnosing and monitoring kidney function in children. Clinical Biochemistry, 41, 498–503. doi:10.1016/j.clinbiochem.2008.01.022
   PubMed Web of Science ®Google Scholar
• Ni, J., Abrahamson, M., Zhang, M., Fernandez, M. A., Grubb, A., Su, J., … Gentz, R. (1997). Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. The Journal of Biological Chemistry, 272, 10853–10858. doi:10.1074/jbc.272.16.10853
   PubMed Web of Science ®Google Scholar
• Ni, J., Fernandez, M. A., Danielsson, L., Chillakuru, R. A., Zhang, J., Grubb, A., & Abrahamson, M. (1998). Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor. Journal of Biological Chemistry, 273, 24797–24804. doi:10.1074/jbc.273.38.24797
   PubMed Web of Science ®Google Scholar
• Nicklin, M. J., & Barrett, A. J. (1984). Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochemical Journal, 223, 245–253. doi:10.1042/bj2230245
   PubMed Web of Science ®Google Scholar
• Nishiyama, K., Konishi, A., Nishio, C., Araki-Yoshida, K., Hatanaka, H., Kojima, M., & Koshimizu, H. (2005). Expression of cystatin C prevents oxidative stress-induced death in PC12 cells. Brain Research Bulletin, 67, 94–99. doi:10.1016/j.brainresbull.2005.05.020
   PubMed Web of Science ®Google Scholar
• North, M. J., Mottram, J. C., & Coombs, G. H. (1990). Cysteine proteinases of parasitic protozoa. Parasitology Today, 6, 270–275. doi:10.1016/0169-4758(90)90189-B
   PubMedGoogle Scholar
• Ohkubo, I., Kurachi, K., Takasawa, T., Shiokawa, H., & Sasaki, M. (1984). Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry, 23, 5691–5697. doi:10.1021/bi00319a005
   PubMed Web of Science ®Google Scholar
• Olsson, S. L., Ek, B., & Björk, I. (1999). The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 1432, 73–81. doi:10.1016/S0167-4838(99)00090-4
   PubMed Web of Science ®Google Scholar
• Priyadarshini, M., & Bano, B. (2010). Cystatin like thiol proteinase inhibitor from pancreas of Capra hircus: Purification and detailed biochemical characterization. Amino Acids, 38, 1001–1010. doi:10.1007/s00726-009-0308-x
   PubMed Web of Science ®Google Scholar
• Ramasarma, P. R., Rao, A. G., & Rao, D. R. (1995). Role of disulfide linkages in structure and activity of proteinase inhibitor from horsegram (Dolichos biflorus). Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 1248, 35–42. doi:10.1016/0167-4838(95)00004-E
   PubMed Web of Science ®Google Scholar
• Rashid, F., Sharma, S., & Bano, B. (2006). Detailed biochemical characterization of human placental cystatin (HPC). Placenta, 27, 822–831. doi:10.1016/j.placenta.2005.09.005
   PubMed Web of Science ®Google Scholar
• Rehman, M. T., Dey, P., Hassan, M. I., Ahmad, F., & Batra, J. K. (2011). Functional role of glutamine 28 and arginine 39 in double stranded RNA cleavage by human pancreatic ribonuclease. PLoS One, 6, e17159. doi:10.1371/journal.pone.0017159
   PubMedGoogle Scholar
• Rehman, M. T., Faheem, M., & Khan, A. U. (2015). An insight into the biophysical characterization of different states of cefotaxime hydrolyzing β-lactamase 15 (CTX-M-15). Journal of Biomolecular Structure & Dynamics, 33, 625–638. doi:10.1080/07391102.2014.899925
   PubMed Web of Science ®Google Scholar
• Rüegg, M., Metzger, V., & Susi, H. (1975). Computer analyses of characteristic infrared bands of globular proteins. Biopolymers, 14, 1465–1471. doi:10.1002/bip.1975.360140712
   PubMed Web of Science ®Google Scholar
• Sadaf, Z., Shahid, P. B., & Bilqees, B. (2005). Isolation, characterization and kinetics of goat cystatins. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 142, 361–368. doi:10.1016/j.cbpb.2005.08.007
   PubMed Web of Science ®Google Scholar
• Schurmann, G., Haspel, J., Grumet, M., & Erickson, H. P. (2001). Cell adhesion molecule L1 in folded (Horseshoe) and extended conformations. Molecular Biology of the Cell, 12, 1765–1773. doi:10.1091/mbc.12.6.1765
   PubMed Web of Science ®Google Scholar
• Schwabe, C., Anastasi, A., Crow, H., McDonald, J. K., & Barrett, A. J. (1984). Cystatin. Amino acid sequence and possible secondary structure. Biochemical Journal, 217, 813–817. doi:10.1042/bj2170813
   PubMed Web of Science ®Google Scholar
• Shamsi, A., Ahmed, A., & Bano, B. (2016). Structural transition of kidney cystatin in dimethylnitrosamine-induced renal cancer in rats: Identification as a novel biomarker for kidney cancer and prognosis. Journal of Biomolecular Structure & Dynamics, 1–10. doi:10.1080/07391102.2016.1166988
   PubMed Web of Science ®Google Scholar
• Sloane, B. F. (1990). Cathepsin B and cystatins: Evidence for a role in cancer progression. Seminars in Cancer Biology, 1, 137–152.
   PubMedGoogle Scholar
• Sotiropoulou, G., Anisowicz, A., & Sager, R. (1997). Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. Journal of Biological Chemistry, 272, 903–910. doi:10.1074/jbc.272.2.903
   PubMed Web of Science ®Google Scholar
• Stites, W. E. (1997). Protein−protein interactions: Interface structure, binding thermodynamics, and mutational analysis. Chemical Reviews, 97, 1233–1250. doi:10.1021/cr960387h
   PubMed Web of Science ®Google Scholar
• Stubbs, M. T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenarcic, B., & Turk, V. (1990). The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction. The EMBO Journal, 9, 1939–1947. PMID: 2347312
   PubMed Web of Science ®Google Scholar
• Sumbul, S., & Bano, B. (2006). Purification and characterization of high molecular mass and low molecular mass cystatin from goat brain. Neurochemical Research, 31, 1327–1336. doi:10.1007/s11064-006-9175-y
   PubMed Web of Science ®Google Scholar
• Timasheff, S. N., Susi, H., & Stevens, L. (1967). Infrared spectra and protein conformations in aqueous solutions. II. Survey of globular proteins. Journal of Biological Chemistry, 242, 5467–5473.
   PubMed Web of Science ®Google Scholar
• Trabandt, A., Gay, R. E., Fassbender, H. G., & Gay, S. (1991). Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis. Arthritis and Rheumatism, 34, 1444–1451. doi:10.1002/art.1780341116
   PubMed Web of Science ®Google Scholar
• Turk, V., & Bode, W. (1991). The cystatins: Protein inhibitors of cysteine proteinases. FEBS Letters, 285, 213–219. doi:10.1016/0014-5793(91)80804-C
   PubMed Web of Science ®Google Scholar
• Turk, B., Turk, V., & Turk, D. (1997). Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biological Chemistry, 378, 141–150.
   PubMed Web of Science ®Google Scholar
• Weber, K., & Osborn, M. (1969). The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. The Journal of Biological Chemistry, 244, 4406–4412.
   PubMed Web of Science ®Google Scholar
• Wille, A., Gerber, A., Heimburg, A., Reisenauer, A., Peters, C., Saftig, P., … Bühling, F. (2004). Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells. Biological Chemistry, 385, 665–670. doi:10.1515/BC.2004.082
   PubMed Web of Science ®Google Scholar