Journal articles on the topic 'Β-crystallin'
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Belisle, E. H., S. W. Su, B. W. Lubit, and S. C. J. Fu. "Homology among β-crystallins: Monoclonal antibodies to β-heavy crystallin." Current Eye Research 6, no. 8 (January 1987): 951–57. http://dx.doi.org/10.3109/02713688709034866.
Full textHejtmancik, J. F., P. T. Wingfield, and Y. V. Sergeev. "β-Crystallin association." Experimental Eye Research 79, no. 3 (September 2004): 377–83. http://dx.doi.org/10.1016/j.exer.2004.06.011.
Full textSong, In-Kang, Seungjin Na, Eunok Paek, and Kong-Joo Lee. "Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes." International Journal of Molecular Sciences 21, no. 18 (September 5, 2020): 6504. http://dx.doi.org/10.3390/ijms21186504.
Full textFeng, Jinhua, David L. Smith, and Jean B. Smith. "Human Lens β-Crystallin Solubility." Journal of Biological Chemistry 275, no. 16 (April 14, 2000): 11585–90. http://dx.doi.org/10.1074/jbc.275.16.11585.
Full textJames, M., and C. Crabbe. "Partial sequence homologies between cytoskeletal proteins, c-myc, Rous sarcoma virus and adenovirus proteins, transducin, and β- and γ-crystallins." Bioscience Reports 5, no. 2 (February 1, 1985): 167–74. http://dx.doi.org/10.1007/bf01117063.
Full textPan, F. M., W. C. Chang, S. F. Lu, A. L. Hsu, and S. H. Chiou. "Sequence Analysis of One Major Basic β-Crystallin (β-Bp) of Amphibian Lenses - Evolutionary Comparison and Phylogenetic Relatedness Between β-Crystallin and γ-Crystallin." Biochemical and Biophysical Research Communications 217, no. 3 (December 1995): 940–49. http://dx.doi.org/10.1006/bbrc.1995.2861.
Full textLeng, Xiao-Yao, Sha Wang, Ni-Qian Cao, Liang-Bo Qi, and Yong-Bin Yan. "The N-Terminal Extension of βB1-Crystallin Chaperones β-Crystallin Folding and Cooperates with αA-Crystallin." Biochemistry 53, no. 15 (April 8, 2014): 2464–73. http://dx.doi.org/10.1021/bi500146d.
Full textLeng, Xiao-Yao, Hai-Yun Li, Jing Wang, Liang-Bo Qi, Yi-Bo Xi, and Yong-Bin Yan. "Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation." Biochemical Journal 473, no. 14 (July 12, 2016): 2087–96. http://dx.doi.org/10.1042/bcj20160247.
Full textWang, Sha, Xiao-Yao Leng, and Yong-Bin Yan. "The Benefits of Being β-Crystallin Heteromers: βB1-Crystallin Protects βA3-Crystallin against Aggregation during Co-refolding." Biochemistry 50, no. 48 (December 6, 2011): 10451–61. http://dx.doi.org/10.1021/bi201375p.
Full textRaman, Bakthisaran, Tadato Ban, Miyo Sakai, Saloni Y. Pasta, Tangirala Ramakrishna, Hironobu Naiki, Yuji Goto, and Ch Mohan Rao. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin." Biochemical Journal 392, no. 3 (December 6, 2005): 573–81. http://dx.doi.org/10.1042/bj20050339.
Full textJiang, Y. J., S. H. Chiou, and W. C. Chang. "Lens crystallin changes associated with amphibian metamorphosis: Involvement of a β-crystallin polypeptide." Biochemical and Biophysical Research Communications 164, no. 3 (November 1989): 1423–30. http://dx.doi.org/10.1016/0006-291x(89)91829-9.
Full textLu, Shao-Fan, Fu-Ming Pan, and Shyh-Horng Chiou. "Sequence Analysis of Four Acidic β-Crystallin Subunits of Amphibian Lenses: Phylogenetic Comparison between β- and γ-Crystallins." Biochemical and Biophysical Research Communications 221, no. 2 (April 1996): 219–28. http://dx.doi.org/10.1006/bbrc.1996.0577.
Full textLiang, Jack J. N. "Interaction between β-amyloid and lens αB-crystallin." FEBS Letters 484, no. 2 (October 31, 2000): 98–101. http://dx.doi.org/10.1016/s0014-5793(00)02136-0.
Full textStege, G. J. J., K. Renkawek, P. S. G. Overkamp, P. Verschuure, A. F. van Rijk, A. Reijnen-Aalbers, W. C. Boelens, G. J. C. G. M. Bosman, and W. W. de Jong. "The Molecular Chaperone αB-crystallin Enhances Amyloid β Neurotoxicity." Biochemical and Biophysical Research Communications 262, no. 1 (August 1999): 152–56. http://dx.doi.org/10.1006/bbrc.1999.1167.
Full textShinkai, Yasuhiro, Yunjie Ding, Takashi Miura, and Yoshito Kumagai. "Aggregation of β-crystallin through covalent binding to 1,2-naphthoquinone is rescued by α-crystallin chaperone." Journal of Toxicological Sciences 45, no. 1 (2020): 37–43. http://dx.doi.org/10.2131/jts.45.37.
Full textKase, Satoru, Shikun He, Shozo Sonoda, Mizuki Kitamura, Christine Spee, Eric Wawrousek, Stephen J. Ryan, Ram Kannan, and David R. Hinton. "αB-crystallin regulation of angiogenesis by modulation of VEGF." Blood 115, no. 16 (April 22, 2010): 3398–406. http://dx.doi.org/10.1182/blood-2009-01-197095.
Full textChen, Jyh-Yih, Bei-En Chang, Yi-Hsuan Chen, Cliff Ji-Fan Lin, Jen-Leih Wu, and Ching-Ming Kuo. "Molecular Cloning, Developmental Expression, and Hormonal Regulation of Zebrafish (Danio rerio) β Crystallin B1, a Member of the Superfamily of β Crystallin Proteins." Biochemical and Biophysical Research Communications 285, no. 1 (July 2001): 105–10. http://dx.doi.org/10.1006/bbrc.2001.5099.
Full textYAN, Hong, Antony C. WILLIS, and John J. HARDING. "γIII-Crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions." Biochemical Journal 374, no. 3 (September 15, 2003): 677–85. http://dx.doi.org/10.1042/bj20030542.
Full textHejtmancik, J. F., P. T. Wingfield, and Y. V. Sergeev. "β-Crystallin association [Experimental Eye Research 79 (2004) 377–383]." Experimental Eye Research 79, no. 6 (December 2004): 785. http://dx.doi.org/10.1016/s0014-4835(04)00303-3.
Full textSiezen, Roland J., Robert D. Anello, and John A. Thomson. "Interactions of lens proteins. Concentration dependence of β-crystallin aggregation." Experimental Eye Research 43, no. 3 (September 1986): 293–303. http://dx.doi.org/10.1016/s0014-4835(86)80067-7.
Full textKroone, R. C., G. S. Elliott, A. Ferszt, C. Slingsby, N. H. Lubsen, and J. G. G. Schoenmakers. "The role of the sequence extensions in β-crystallin assembly." "Protein Engineering, Design and Selection" 7, no. 11 (1994): 1395–99. http://dx.doi.org/10.1093/protein/7.11.1395.
Full textLapatto, R., V. Nalini, B. Bax, H. Driessen, P. F. Lindley, T. L. Blundell, and C. Slingsby. "High resolution structure of an oligomeric eye lens β-crystallin." Journal of Molecular Biology 222, no. 4 (December 1991): 1067–83. http://dx.doi.org/10.1016/0022-2836(91)90594-v.
Full textFeil, Ingeborg K., Marc Malfois, Jörg Hendle, Hans van der Zandt, and Dmitri I. Svergun. "A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity." Journal of Biological Chemistry 276, no. 15 (January 12, 2001): 12024–29. http://dx.doi.org/10.1074/jbc.m010856200.
Full textWu, Fang, Liangkai Cheng, Qi Yu, Lin Zhang, Hong Li, and Caiyan Wang. "Purification and Functional Characterization of the C-Terminal Domain of the β-Actin-Binding Protein AIM1 In Vitro." Molecules 23, no. 12 (December 11, 2018): 3281. http://dx.doi.org/10.3390/molecules23123281.
Full textDuncan, Melinda K., John I. Haynes, Ales Cvekl, and Joram Piatigorsky. "Dual Roles for Pax-6: a Transcriptional Repressor of Lens Fiber Cell-Specific β-Crystallin Genes." Molecular and Cellular Biology 18, no. 9 (September 1, 1998): 5579–86. http://dx.doi.org/10.1128/mcb.18.9.5579.
Full textCRAGHILL, Jane, Andrew D. CRONSHAW, and John J. HARDING. "The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens." Biochemical Journal 379, no. 3 (May 1, 2004): 595–600. http://dx.doi.org/10.1042/bj20031367.
Full textKretschmar, M., E. M. Mayr, and R. Jaenicke. "Homo-Dimeric Spherulin 3a: A Single-Domain Member of the bg-Crystallin Superfamily." Biological Chemistry 380, no. 1 (January 4, 1999): 89–94. http://dx.doi.org/10.1515/bc.1999.012.
Full textReddy, G. Bhanuprakash, P. Yadagiri Reddy, and Avadhesha Surolia. "Alzheimer’s and Danish dementia peptides induce cataract and perturb retinal architecture in rats." Biomolecular Concepts 8, no. 1 (March 1, 2017): 45–84. http://dx.doi.org/10.1515/bmc-2016-0025.
Full textChiou, Shyh-Horng, Fu-Ming Pan, Hsuan-Wan Peng, Yen-Kai Chao, and Wen-Chang Chang. "Characterization of γS-Crystallin Isoforms from a Catfish: Evolutionary Comparison of Various γ-, γS-, and β-Crystallins." Biochemical and Biophysical Research Communications 252, no. 2 (November 1998): 412–19. http://dx.doi.org/10.1006/bbrc.1998.9657.
Full textMacdonald, James T., Andrew G. Purkiss, Myron A. Smith, Paul Evans, Julia M. Goodfellow, and Christine Slingsby. "Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment." Protein Science 14, no. 5 (May 2005): 1282–92. http://dx.doi.org/10.1110/ps.041227805.
Full textMaiti, Motilal, Masahiro Kono, and Bireswar Chakrabarti. "Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin." FEBS Letters 236, no. 1 (August 15, 1988): 109–14. http://dx.doi.org/10.1016/0014-5793(88)80295-3.
Full textCoop, Audrey, Kirsten E. H. Wiesmann, and M. James C. Crabbe. "Translocation of β crystallin in neural cells in response to stress." FEBS Letters 431, no. 3 (July 24, 1998): 319–21. http://dx.doi.org/10.1016/s0014-5793(98)00783-2.
Full textBateman, O. A., R. Sarra, S. T. van Genesen, G. Kappé, N. H. Lubsen, and C. Slingsby. "The stability of human acidic β-crystallin oligomers and hetero-oligomers." Experimental Eye Research 77, no. 4 (October 2003): 409–22. http://dx.doi.org/10.1016/s0014-4835(03)00173-8.
Full textLiedtke, Thomas, Jens Christian Schwamborn, Uwe Schröer, and Solon Thanos. "Elongation of Axons during Regeneration Involves Retinal Crystallin β b2 (crybb2)." Molecular & Cellular Proteomics 6, no. 5 (January 29, 2007): 895–907. http://dx.doi.org/10.1074/mcp.m600245-mcp200.
Full textWang, Kai Jie. "Novel β-Crystallin Gene Mutations in Chinese Families With Nuclear Cataracts." Archives of Ophthalmology 129, no. 3 (March 1, 2011): 337. http://dx.doi.org/10.1001/archophthalmol.2011.11.
Full textSrinivas, P. N. B. S., P. Yadagiri Reddy, and G. Bhanuprakash Reddy. "Significance of α-crystallin heteropolymer with a 3:1 αA/αB ratio: chaperone-like activity, structure and hydrophobicity." Biochemical Journal 414, no. 3 (August 27, 2008): 453–60. http://dx.doi.org/10.1042/bj20080544.
Full textPan, Fu-Ming, Ming-Hong Chuang, and Shyh-Horng Chiou. "Characterization of γS-Crystallin Isoforms from Lip Shark (Chiloscyllium colax): Evolutionary Comparison between γS and β/γ Crystallins." Biochemical and Biophysical Research Communications 240, no. 1 (November 1997): 51–56. http://dx.doi.org/10.1006/bbrc.1997.7600.
Full textKenworthy, Anne K., Alan D. Magid, Timothy N. Oliver, and Thomas J. McIntosh. "Colloid Osmotic Pressure of Steer and β-Crystallins: Possible Functional Roles for Lens Crystallin Distribution and Structural Diversity." Experimental Eye Research 59, no. 1 (July 1994): 11–30. http://dx.doi.org/10.1006/exer.1994.1077.
Full textDavid, Larry L., Jay W. Wright, and Thomas R. Shearer. "Calpain II induced insolubilization of lens β-crystallin polypeptides may induce cataract." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1139, no. 3 (July 1992): 210–16. http://dx.doi.org/10.1016/0925-4439(92)90136-b.
Full textGhosh, Joy G., Denise Fabian, Ashley Mallat, Steve Ramirez, Mark Burton, Juliet Moncaster, Noel Casey, et al. "P2-145: The molecular chaperone human Aβ crystallin modulates amyloid-β neurotoxicity." Alzheimer's & Dementia 5, no. 4S_Part_10 (July 2009): P304. http://dx.doi.org/10.1016/j.jalz.2009.04.456.
Full textCheeseman, Kevin H., Milfred Seccia, Olga Brossa, Trevor Slater, and Enrico Gravela. "Modification of β-crystallin by free radicals predisposes it to transglutaminase activity." Free Radical Biology and Medicine 9 (January 1990): 83. http://dx.doi.org/10.1016/0891-5849(90)90464-t.
Full textHerzog, Rebecca, Juan Manuel Sacnun, Guadalupe González-Mateo, Maria Bartosova, Katarzyna Bialas, Anja Wagner, Markus Unterwurzacher, et al. "Lithium preserves peritoneal membrane integrity by suppressing mesothelial cell αB-crystallin." Science Translational Medicine 13, no. 608 (August 25, 2021): eaaz9705. http://dx.doi.org/10.1126/scitranslmed.aaz9705.
Full textAarts, Henk J. M., Johan T. Den Dunnen, Nicolette H. Lubsen, and John G. G. Schoenmakers. "Linkage between the βB2 and βB3 crystallin genes in man and rat: a remnant of an ancient β-crystallin gene cluster." Gene 59, no. 1 (January 1987): 127–35. http://dx.doi.org/10.1016/0378-1119(87)90273-3.
Full textBruggink, Kim, H. Bea Kuiperij, Marcel M. Verbeek, and Wilbert Boelens. "P1-067: Complexes of amyloid β and Amyloid-β-crystallin as potential biomarkers for early stage Alzheimer's disease." Alzheimer's & Dementia 7 (July 2011): S131. http://dx.doi.org/10.1016/j.jalz.2011.05.346.
Full textLubsen, N. H., H. J. M. Aarts, and J. G. G. Schoenmakers. "The evolution of lenticular proteins: The β- and γ-crystallin super gene family." Progress in Biophysics and Molecular Biology 51, no. 1 (January 1988): 47–76. http://dx.doi.org/10.1016/0079-6107(88)90010-7.
Full textTrivedi, Vishwa D., Bakthisaran Raman, Tangirala Ramakrishna, and Ch Mohan Rao. "Detection and assay of proteases using calf lens β-crystallin aggregate as substrate." Journal of Biochemical and Biophysical Methods 40, no. 1-2 (July 1999): 49–55. http://dx.doi.org/10.1016/s0165-022x(99)00021-4.
Full textBERBERS, Guy A. M., Otto C. BOERMAN, Hans BLOEMENDAL, and Wilfried W. JONG. "Primary Gene Products of Bovine β-Crystallin and Reassociation Behavior of Its Aggregates." European Journal of Biochemistry 128, no. 2-3 (March 3, 2005): 495–502. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06992.x.
Full textTrifonova, N. "Anti-α, anti-β, and anti-γ-crystallin autoantibodies from patients with cataract." Vision Research 35, no. 1 (October 1995): S193. http://dx.doi.org/10.1016/0042-6989(95)98743-s.
Full textLowe, James, Michael Landon, Ian Pike, Ian Spendlove, Helen Mcdermott, and R. John Mayer. "Dementia with β-amyloid deposition: involvement of αB-crystallin supports two main diseases." Lancet 336, no. 8713 (August 1990): 515–16. http://dx.doi.org/10.1016/0140-6736(90)92075-s.
Full textSlingsby, C., and O. A. Bateman. "Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4." Experimental Eye Research 51, no. 1 (July 1990): 21–26. http://dx.doi.org/10.1016/0014-4835(90)90165-q.
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