Journal articles on the topic 'Α-crystallin'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the top 50 journal articles for your research on the topic 'Α-crystallin.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.
Selivanova, Olga M., and Oxana V. Galzitskaya. "Structural and Functional Peculiarities of α-Crystallin." Biology 9, no. 4 (April 23, 2020): 85. http://dx.doi.org/10.3390/biology9040085.
Full textEvans, Paul, Christine Slingsby, and B. A. Wallace. "Association of partially folded lens βB2-crystallins with the α-crystallin molecular chaperone." Biochemical Journal 409, no. 3 (January 15, 2008): 691–99. http://dx.doi.org/10.1042/bj20070993.
Full textDERHAM, Barry K., and John J. HARDING. "Effects of modifications of α-crystallin on its chaperone and other properties." Biochemical Journal 364, no. 3 (June 15, 2002): 711–17. http://dx.doi.org/10.1042/bj20011512.
Full textSathish, Hasige A., Hanane A. Koteiche, and Hassane S. Mchaourab. "Binding of Destabilized βB2-Crystallin Mutants to α-Crystallin." Journal of Biological Chemistry 279, no. 16 (February 3, 2004): 16425–32. http://dx.doi.org/10.1074/jbc.m313402200.
Full textSingh, Kamalendra, D. Zewge, B. Groth-Vasselli, and P. N. Farnsworth. "A comparison of structural relationships among α-crystallin, human Hsp27, γ-crystallins and βB2-crystallin." International Journal of Biological Macromolecules 19, no. 4 (December 1996): 227–33. http://dx.doi.org/10.1016/s0141-8130(96)01131-2.
Full textLINDNER, Robyn A., Teresa M. TREWEEK, and John A. CARVER. "The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin." Biochemical Journal 354, no. 1 (February 8, 2001): 79–87. http://dx.doi.org/10.1042/bj3540079.
Full textCrabbe, M. J., and D. Goode. "α-Crystallin: chaperoning and aggregation." Biochemical Journal 297, no. 3 (February 1, 1994): 653–54. http://dx.doi.org/10.1042/bj2970653.
Full textMerck, K. B., W. A. de Haard-Hoekman, H. Bloemendal, and W. W. de Jong. "Protein engineering of α-crystallin." Experimental Eye Research 55 (September 1992): 165. http://dx.doi.org/10.1016/0014-4835(92)90772-k.
Full textNagaraj, Ram H., Rooban B. Nahomi, Niklaus H. Mueller, Cibin T. Raghavan, David A. Ammar, and J. Mark Petrash. "Therapeutic potential of α-crystallin." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 1 (January 2016): 252–57. http://dx.doi.org/10.1016/j.bbagen.2015.03.012.
Full textNarberhaus, Franz. "α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network." Microbiology and Molecular Biology Reviews 66, no. 1 (March 2002): 64–93. http://dx.doi.org/10.1128/mmbr.66.1.64-93.2002.
Full textMalik, Ajamaluddin, Hajar Ahmed Almaharfi, Javed Masood Khan, Malik Hisamuddin, Salman Freeh Alamery, Samina Hyder Haq, and Mohammad Z. Ahmed. "Protection of ζ-crystallin by α-crystallin under thermal stress." International Journal of Biological Macromolecules 167 (January 2021): 289–98. http://dx.doi.org/10.1016/j.ijbiomac.2020.11.183.
Full textGOENKA, Shradha, Bakthisaran RAMAN, Tangirala RAMAKRISHNA, and Ch Mohan RAO. "Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation." Biochemical Journal 359, no. 3 (October 25, 2001): 547–56. http://dx.doi.org/10.1042/bj3590547.
Full textKumar, P. Anil, M. Satish Kumar, and G. Bhanuprakash Reddy. "Effect of glycation on α-crystallin structure and chaperone-like function." Biochemical Journal 408, no. 2 (November 14, 2007): 251–58. http://dx.doi.org/10.1042/bj20070989.
Full textDERHAM, K. Barry, and J. John HARDING. "Effect of aging on the chaperone-like function of human α-crystallin assessed by three methods." Biochemical Journal 328, no. 3 (December 15, 1997): 763–68. http://dx.doi.org/10.1042/bj3280763.
Full textTimsina, Raju, and Laxman Mainali. "Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation." Membranes 11, no. 6 (June 15, 2021): 447. http://dx.doi.org/10.3390/membranes11060447.
Full textKarmakar, Srabani, Shrutidhara Biswas, Kali P. Das, and Umakanta Tripathy. "Surface plasmon resonance study of the interaction of 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) and adenosine triphosphate (ATP) with oligomeric recombinant human lens αA-crystallin." Canadian Journal of Chemistry 97, no. 6 (June 2019): 504–11. http://dx.doi.org/10.1139/cjc-2018-0412.
Full textKUMAR, M. Satish, P. Yadagiri REDDY, P. Anil KUMAR, Ira SUROLIA, and G. Bhanuprakash REDDY. "Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays." Biochemical Journal 379, no. 2 (April 15, 2004): 273–82. http://dx.doi.org/10.1042/bj20031633.
Full textPosner, Mason, Kelly L. Murray, Matthew S. McDonald, Hayden Eighinger, Brandon Andrew, Amy Drossman, Zachary Haley, Justin Nussbaum, Larry L. David, and Kirsten J. Lampi. "The zebrafish as a model system for analyzing mammalian and native α-crystallin promoter function." PeerJ 5 (November 27, 2017): e4093. http://dx.doi.org/10.7717/peerj.4093.
Full textKase, Satoru. "Expression of α-Crystallin in Retinoblastoma." Archives of Ophthalmology 127, no. 2 (February 9, 2009): 187. http://dx.doi.org/10.1001/archophthalmol.2008.580.
Full textWang, Xiaowei, and Frederick A. Bettelheim. "Second virial coefficient of α-crystallin." Proteins: Structure, Function, and Genetics 5, no. 2 (1989): 166–69. http://dx.doi.org/10.1002/prot.340050211.
Full textCherian, M., and E. C. Abraham. "Diabetes Affects α-Crystallin Chaperone Function." Biochemical and Biophysical Research Communications 212, no. 1 (July 1995): 184–89. http://dx.doi.org/10.1006/bbrc.1995.1954.
Full textHorwitz, Joseph, Michael P. Bova, Lin Lin Ding, Dana A. Haley, and Phoebe L. Stewart. "Lens α-crystallin: Function and structure." Eye 13, no. 3 (May 1999): 403–8. http://dx.doi.org/10.1038/eye.1999.114.
Full textFacchiano, Francesco, Teodosio Libondi, Paola Stiuso, Ciro Esposito, Raffaele Ragone, and Giovanni Colonna. "Effect of Galactose on α-Crystallin." Ophthalmic Research 28, no. 1 (1996): 97–100. http://dx.doi.org/10.1159/000267980.
Full textAugusteyn, Robert C., and Jane F. Koretz. "A possible structure for α-crystallin." FEBS Letters 222, no. 1 (September 28, 1987): 1–5. http://dx.doi.org/10.1016/0014-5793(87)80180-1.
Full textTardieu, Annette, Dominique Laporte, Pedro Licinio, Brigitte Krop, and Mireille Delaye. "Calf lens α-crystallin quaternary structure." Journal of Molecular Biology 192, no. 4 (December 1986): 711–24. http://dx.doi.org/10.1016/0022-2836(86)90023-9.
Full textAttanasio, Francesco, Claudia Cascio, Salvatore Fisichella, Vincenzo Giuseppe Nicoletti, Bruno Pignataro, Anna Savarino, and Enrico Rizzarelli. "Trehalose effects on α-crystallin aggregates." Biochemical and Biophysical Research Communications 354, no. 4 (March 2007): 899–905. http://dx.doi.org/10.1016/j.bbrc.2007.01.061.
Full textGANEA, Elena, and John J. HARDING. "α-Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase." Biochemical Journal 345, no. 3 (January 25, 2000): 467–72. http://dx.doi.org/10.1042/bj3450467.
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 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 textBagnéris, C., O. A. Bateman, C. E. Naylor, N. Cronin, W. C. Boelens, N. H. Keep, and C. Slingsby. "Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20." Journal of Molecular Biology 392, no. 5 (October 2009): 1242–52. http://dx.doi.org/10.1016/j.jmb.2009.07.069.
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 textBiswas, Ashis, Benlian Wang, Masaru Miyagi, and Ram H. Nagaraj. "Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human αA-crystallin." Biochemical Journal 409, no. 3 (January 15, 2008): 771–77. http://dx.doi.org/10.1042/bj20071006.
Full textPiatigorsky, Joram. "Molecular biology: Recent studies on enzyme/crystallins and α-crystallin gene expression." Experimental Eye Research 50, no. 6 (June 1990): 725–27. http://dx.doi.org/10.1016/0014-4835(90)90121-a.
Full textPutilina, T., Z. W. Zhang, and R. C. Augusteyn. "The effects of sonication on α-crystallin." Current Eye Research 10, no. 2 (January 1991): 113–20. http://dx.doi.org/10.3109/02713689109001738.
Full textVanhoudt, Jos, Saïd Abgar, Tony Aerts, and Julius Clauwaert. "Native Quaternary Structure of Bovine α-Crystallin†." Biochemistry 39, no. 15 (April 2000): 4483–92. http://dx.doi.org/10.1021/bi990386u.
Full textCobb, Brian A., and J. Mark Petrash. "Characterization of α-crystallin-plasma membrane binding." Journal of Biological Chemistry 277, no. 2 (January 2002): 1628. http://dx.doi.org/10.1016/s0021-9258(20)87969-1.
Full textHo, Yuh, Ming-Ching Hsu, and Fu-Yung Huang. "Chaperone Function of Rat Lens α-Crystallin." Journal of the Chinese Chemical Society 45, no. 2 (April 1998): 285–92. http://dx.doi.org/10.1002/jccs.199800045.
Full textFinley, Eric L., James Dillon, Rosalie K. Crouch, and Kevin L. Schey. "Radiolysis-Induced Oxidation of Bovine α-Crystallin." Photochemistry and Photobiology 68, no. 1 (July 1998): 9–15. http://dx.doi.org/10.1111/j.1751-1097.1998.tb03245.x.
Full textCobb, Brian A., and J. Mark Petrash. "Characterization of α-Crystallin-Plasma Membrane Binding." Journal of Biological Chemistry 275, no. 9 (February 25, 2000): 6664–72. http://dx.doi.org/10.1074/jbc.275.9.6664.
Full textGroenen, Patricia J. T. A., Paul R. L. A. van den Ijssel, Christina E. M. Voorter, Hans Bloemendal, and Wilfried W. de Jong. "Site-specific racemization in aging α-crystallin." FEBS Letters 269, no. 1 (August 20, 1990): 109–12. http://dx.doi.org/10.1016/0014-5793(90)81131-7.
Full textCarver, John A., J. Andrew Aquilina, Philip G. Cooper, Gavin A. Williams, and Roger J. W. Truscott. "α-Crystallin: molecular chaperone and protein surfactant." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1204, no. 2 (February 1994): 195–206. http://dx.doi.org/10.1016/0167-4838(94)90009-4.
Full textTue, Nguyen Trong, Kouhei Shimaji, Naoki Tanaka, and Masamitsu Yamaguchi. "Effect ofαB-Crystallin on Protein Aggregation inDrosophila." Journal of Biomedicine and Biotechnology 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/252049.
Full textBanerjee, Priya R., Ajay Pande, Alexander Shekhtman, and Jayanti Pande. "Molecular Mechanism of the Chaperone Function of Mini-α-Crystallin, a 19-Residue Peptide of Human α-Crystallin." Biochemistry 54, no. 2 (December 26, 2014): 505–15. http://dx.doi.org/10.1021/bi5014479.
Full textLiu, Haiquan, Xin Du, Meng Wang, Qingling Huang, Linlin Ding, Hayes W. McDonald, John R. Yates, Bruce Beutler, Joseph Horwitz, and Xiaohua Gong. "Crystallin γB-I4F Mutant Protein Binds to α-Crystallin and Affects Lens Transparency." Journal of Biological Chemistry 280, no. 26 (May 4, 2005): 25071–78. http://dx.doi.org/10.1074/jbc.m502490200.
Full textMichiel, Magalie, Elodie Duprat, Fériel Skouri-Panet, Jason A. Lampi, Annette Tardieu, Kirsten J. Lampi, and Stéphanie Finet. "Aggregation of deamidated human βB2-crystallin and incomplete rescue by α-crystallin chaperone." Experimental Eye Research 90, no. 6 (June 2010): 688–98. http://dx.doi.org/10.1016/j.exer.2010.02.007.
Full textMuranov, K. O., N. B. Poliansky, N. A. Chebotareva, S. Yu Kleimenov, A. E. Bugrova, M. I. Indeykina, A. S. Kononikhin, E. N. Nikolaev, and M. A. Ostrovsky. "The mechanism of the interaction of α-crystallin and UV-damaged βL-crystallin." International Journal of Biological Macromolecules 140 (November 2019): 736–48. http://dx.doi.org/10.1016/j.ijbiomac.2019.08.178.
Full textRoman, Svetlana G., Natalia A. Chebotareva, and Boris I. Kurganov. "Concentration dependence of chaperone-like activities of α-crystallin, αB-crystallin and proline." International Journal of Biological Macromolecules 50, no. 5 (June 2012): 1341–45. http://dx.doi.org/10.1016/j.ijbiomac.2012.03.015.
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 textKumar, M. Satish, Mili Kapoor, Sharmistha Sinha, and G. Bhanuprakash Reddy. "Insights into Hydrophobicity and the Chaperone-like Function of αA- and αB-crystallins." Journal of Biological Chemistry 280, no. 23 (April 6, 2005): 21726–30. http://dx.doi.org/10.1074/jbc.m500405200.
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 text