| Year |
Citation |
Score |
| 2017 |
Srivastava OP, Srivastava K, Chaves JM, Gill AK. Post-translationally modified human lens crystallin fragments show aggregation in vitro. Biochemistry and Biophysics Reports. 10: 94-131. PMID 28955739 DOI: 10.1016/J.Bbrep.2017.01.011 |
0.664 |
|
| 2017 |
Chaves JM, Gupta R, Srivastava K, Srivastava O. Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin. Biochemical and Biophysical Research Communications. PMID 28935373 DOI: 10.1016/J.Bbrc.2017.09.088 |
0.688 |
|
| 2016 |
Hegde S, Kesterson RA, Srivastava OP. CRYβA3/A1-Crystallin Knockout Develops Nuclear Cataract and Causes Impaired Lysosomal Cargo Clearance and Calpain Activation. Plos One. 11: e0149027. PMID 26863613 DOI: 10.1371/Journal.Pone.0149027 |
0.321 |
|
| 2015 |
Tiwary E, Hegde S, Purushotham S, Deivanayagam C, Srivastava O. Interaction of βA3-Crystallin with Deamidated Mutants of αA- and αB-Crystallins. Plos One. 10: e0144621. PMID 26657544 DOI: 10.1371/Journal.Pone.0144621 |
0.335 |
|
| 2014 |
Hegde SM, Srivastava K, Tiwary E, Srivastava OP. Molecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice. Investigative Ophthalmology & Visual Science. 55: 6398-408. PMID 25146988 DOI: 10.1167/Iovs.14-14623 |
0.331 |
|
| 2011 |
Asomugha CO, Gupta R, Srivastava OP. Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin. Molecular Vision. 17: 2407-20. PMID 21976952 |
0.724 |
|
| 2011 |
Asomugha CO, Gupta R, Srivastava OP. Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins. Molecular Vision. 17: 2356-67. PMID 21921988 |
0.727 |
|
| 2011 |
Joseph R, Srivastava OP, Pfister RR. Differential epithelial and stromal protein profiles in keratoconus and normal human corneas Experimental Eye Research. 92: 282-298. PMID 21281627 DOI: 10.1016/J.Exer.2011.01.008 |
0.345 |
|
| 2011 |
Gupta R, Asomugha CO, Srivastava OP. The common modification in alphaA-crystallin in the lens, N101D, is associated with increased opacity in a mouse model. The Journal of Biological Chemistry. 286: 11579-92. PMID 21245144 DOI: 10.1074/Jbc.M110.148627 |
0.717 |
|
| 2010 |
Asomugha CO, Gupta R, Srivastava OP. Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling. Molecular Vision. 16: 476-94. PMID 20352024 |
0.718 |
|
| 2009 |
Srivastava K, Gupta R, Chaves JM, Srivastava OP. Truncated human betaB1-crystallin shows altered structural properties and interaction with human betaA3-crystallin. Biochemistry. 48: 7179-89. PMID 19548648 DOI: 10.1021/Bi900313C |
0.688 |
|
| 2009 |
Gupta R, Srivastava OP. Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods. The Journal of Biological Chemistry. 284: 18481-92. PMID 19401464 DOI: 10.1074/Jbc.M109.013789 |
0.345 |
|
| 2008 |
Srivastava OP, Srivastava K, Chaves JM. Isolation and characterization of betaA3-crystallin associated proteinase from alpha-crystallin fraction of human lenses. Molecular Vision. 14: 1872-85. PMID 18949065 |
0.636 |
|
| 2008 |
Barnes S, Shonsey EM, Eliuk SM, Stella D, Barrett K, Srivastava OP, Kim H, Renfrow MB. High-resolution mass spectrometry analysis of protein oxidations and resultant loss of function. Biochemical Society Transactions. 36: 1037-44. PMID 18793185 DOI: 10.1042/Bst0361037 |
0.305 |
|
| 2008 |
Chaves JM, Srivastava K, Gupta R, Srivastava OP. Structural and functional roles of deamidation and/or truncation of N- or C-termini in human alpha A-crystallin. Biochemistry. 47: 10069-83. PMID 18754677 DOI: 10.1021/Bi8001902 |
0.702 |
|
| 2008 |
Srivastava K, Chaves JM, Srivastava OP, Kirk M. Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses. Experimental Eye Research. 87: 356-66. PMID 18662688 DOI: 10.1016/J.Exer.2008.07.001 |
0.665 |
|
| 2004 |
Gupta R, Srivastava OP. Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin. The Journal of Biological Chemistry. 279: 44258-69. PMID 15284238 DOI: 10.1074/Jbc.M405648200 |
0.399 |
|
| 2004 |
Gupta R, Srivastava OP. Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin. Investigative Ophthalmology & Visual Science. 45: 206-14. PMID 14691175 DOI: 10.1167/Iovs.03-0720 |
0.378 |
|
| 2004 |
Srivastava OP, Kirk MC, Srivastava K. Characterization of covalent multimers of crystallins in aging human lenses. The Journal of Biological Chemistry. 279: 10901-9. PMID 14623886 DOI: 10.1074/Jbc.M308884200 |
0.388 |
|
| 2003 |
Srivastava OP, Srivastava K. β B2-crystallin undergoes extensive truncation during aging in human lenses Biochemical and Biophysical Research Communications. 301: 44-49. PMID 12535638 DOI: 10.1016/S0006-291X(02)02975-3 |
0.39 |
|
| 1999 |
Srivastava OP, Srivastava K, Harrington V. Age-related degradation of βA3/A1-crystallin in human lenses Biochemical and Biophysical Research Communications. 258: 632-638. PMID 10329436 DOI: 10.1006/Bbrc.1999.0506 |
0.367 |
|
| 1998 |
Srivastava OP, Srivastava K. Degradation of γD- and γs-crystallins in human lenses Biochemical and Biophysical Research Communications. 253: 288-294. PMID 9878530 DOI: 10.1006/Bbrc.1998.9728 |
0.383 |
|
| 1998 |
Srivastava OP, Srivastava K. Purification of γ-crystallin from human lenses by acetone precipitation method Current Eye Research. 17: 1074-1081. PMID 9846626 DOI: 10.1076/Ceyr.17.11.1074.5228 |
0.379 |
|
| 1996 |
Srivastava OP, Srivastava K. Characterization of three isoforms of a 9 kDa γD-crystallin fragment isolated from human lenses Experimental Eye Research. 62: 593-604. PMID 8983941 DOI: 10.1006/Exer.1996.0070 |
0.414 |
|
| 1996 |
Srivastava OP, Srivastava K, Silney C. Levels of crystallin fragments and identification of their origin in water soluble high molecular weight (HMW) proteins of human lenses Current Eye Research. 15: 511-520. PMID 8670752 DOI: 10.3109/02713689609000762 |
0.401 |
|
| 1994 |
Srivastava OP, Srivastava K, Silney C. Covalent modification at the C-terminal end of a 9 kDa γD-crystallin fragment in human lenses Experimental Eye Research. 58: 595-603. PMID 7925697 DOI: 10.1006/Exer.1994.1054 |
0.346 |
|
| 1992 |
Srivastava OP, McEntire JE, Srivastava K. Identification of a 9 kDa γ-crystallin fragment in human lenses Experimental Eye Research. 54: 893-901. PMID 1521581 DOI: 10.1016/0014-4835(92)90153-J |
0.377 |
|
| 1992 |
Srivastava O, McEntire J. Human lens membrane proteinase: Partial N-terminal amino acid sequence and activation Experimental Eye Research. 55: 155. DOI: 10.1016/0014-4835(92)90744-D |
0.327 |
|
| 1989 |
Srivastava OP, Ortwerth BJ. The effects of aging and cataract formation on the trypsin inhibitor activity of human lens Experimental Eye Research. 48: 25-36. PMID 2920782 DOI: 10.1016/0014-4835(89)90015-8 |
0.314 |
|
| 1989 |
Srivastava OP, Srivastava K. Human lens membrane proteinase: Purification and age-related distributional changes in the water-soluble and insoluble protein fractions Experimental Eye Research. 48: 161-175. PMID 2647500 DOI: 10.1016/S0014-4835(89)80067-3 |
0.361 |
|
| 1988 |
Srivastava OP. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses Experimental Eye Research. 47: 525-543. PMID 3181333 DOI: 10.1016/0014-4835(88)90092-9 |
0.372 |
|
| 1983 |
Srivastava OP, Ortwerth BJ. Purification and properties of a protein from bovine lens which inhibits trypsin and two endogenous lens proteinases Experimental Eye Research. 36: 363-379. PMID 6403363 DOI: 10.1016/0014-4835(83)90118-5 |
0.314 |
|
| 1983 |
Srivastava OP, Ortwerth BJ. Isolation and characterization of a 25K serine proteinase from bovine lens cortex Experimental Eye Research. 37: 597-612. PMID 6363110 DOI: 10.1016/0014-4835(83)90135-5 |
0.317 |
|
| 1977 |
Srivastava OP, Van Huystee RB. Iaa oxidase and polyphenol oxidase activities of peanut peroxidase isozymes Phytochemistry. 16: 1527-1530. DOI: 10.1016/0031-9422(77)84016-8 |
0.502 |
|
| 1977 |
Srivastava OP, van Huystee RB. Spectral and molecular properties of peanut peroxidase isozymes Phytochemistry. 16: 1657-1659. DOI: 10.1016/0031-9422(71)85064-1 |
0.537 |
|
| Show low-probability matches. |
