| Year |
Citation |
Score |
| 2019 |
Warmack RA, Shawa H, Liu K, Lopez K, Loo JA, Horwitz J, Clarke SG. The L-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation. The Journal of Biological Chemistry. PMID 31239355 DOI: 10.1074/Jbc.Ra119.009052 |
0.309 |
|
| 2012 |
Gangalum RK, Horwitz J, Kohan SA, Bhat SP. αA-crystallin and αB-crystallin reside in separate subcellular compartments in the developing ocular lens. The Journal of Biological Chemistry. 287: 42407-16. PMID 23071119 DOI: 10.1074/Jbc.M112.414854 |
0.339 |
|
| 2010 |
Cheng C, Xia CH, Huang Q, Ding L, Horwitz J, Gong X. Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis. The Journal of Biological Chemistry. 285: 41187-93. PMID 20959464 DOI: 10.1074/Jbc.M110.154534 |
0.305 |
|
| 2010 |
Benesch JL, Aquilina JA, Baldwin AJ, Rekas A, Stengel F, Lindner RA, Basha E, Devlin GL, Horwitz J, Vierling E, Carver JA, Robinson CV. The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chemistry & Biology. 17: 1008-17. PMID 20851350 DOI: 10.1016/J.Chembiol.2010.06.016 |
0.314 |
|
| 2010 |
Laganowsky A, Benesch JL, Landau M, Ding L, Sawaya MR, Cascio D, Huang Q, Robinson CV, Horwitz J, Eisenberg D. Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Science : a Publication of the Protein Society. 19: 1031-43. PMID 20440841 DOI: 10.1002/Pro.380 |
0.339 |
|
| 2009 |
Huang Q, Ding L, Phan KB, Cheng C, Xia CH, Gong X, Horwitz J. Mechanism of cataract formation in alphaA-crystallin Y118D mutation. Investigative Ophthalmology & Visual Science. 50: 2919-26. PMID 19151380 DOI: 10.1167/Iovs.08-3070 |
0.374 |
|
| 2009 |
Horwitz J. Alpha crystallin: the quest for a homogeneous quaternary structure. Experimental Eye Research. 88: 190-4. PMID 18703051 DOI: 10.1016/J.Exer.2008.07.007 |
0.352 |
|
| 2007 |
Zhang X, Dudek EJ, Liu B, Ding L, Fernandes AF, Liang JJ, Horwitz J, Taylor A, Shang F. Degradation of C-terminal truncated alpha A-crystallins by the ubiquitin-proteasome pathway. Investigative Ophthalmology & Visual Science. 48: 4200-8. PMID 17724207 DOI: 10.1167/Iovs.07-0196 |
0.365 |
|
| 2007 |
Wang K, Cheng C, Li L, Liu H, Huang Q, Xia CH, Yao K, Sun P, Horwitz J, Gong X. GammaD-crystallin associated protein aggregation and lens fiber cell denucleation. Investigative Ophthalmology & Visual Science. 48: 3719-28. PMID 17652744 DOI: 10.1167/Iovs.06-1487 |
0.318 |
|
| 2007 |
Ecroyd H, Meehan S, Horwitz J, Aquilina JA, Benesch JL, Robinson CV, Macphee CE, Carver JA. Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity. The Biochemical Journal. 401: 129-41. PMID 16928191 DOI: 10.1042/Bj20060981 |
0.316 |
|
| 2006 |
Xia CH, Liu H, Chang B, Cheng C, Cheung D, Wang M, Huang Q, Horwitz J, Gong X. Arginine 54 and Tyrosine 118 residues of {alpha}A-crystallin are crucial for lens formation and transparency. Investigative Ophthalmology & Visual Science. 47: 3004-10. PMID 16799046 DOI: 10.1167/Iovs.06-0178 |
0.345 |
|
| 2006 |
Xia CH, Cheng C, Huang Q, Cheung D, Li L, Dunia I, Benedetti LE, Horwitz J, Gong X. Absence of alpha3 (Cx46) and alpha8 (Cx50) connexins leads to cataracts by affecting lens inner fiber cells. Experimental Eye Research. 83: 688-96. PMID 16696970 DOI: 10.1016/J.Exer.2006.03.013 |
0.326 |
|
| 2006 |
Turk E, Gasymov OK, Lanza S, Horwitz J, Wright EM. A reinvestigation of the secondary structure of functionally active vSGLT, the vibrio sodium/galactose cotransporter. Biochemistry. 45: 1470-9. PMID 16445289 DOI: 10.1021/Bi052160Z |
0.394 |
|
| 2005 |
Liu H, Du X, Wang M, Huang Q, Ding L, McDonald HW, Yates JR, Beutler B, Horwitz J, Gong X. Crystallin {gamma}B-I4F mutant protein binds to {alpha}-crystallin and affects lens transparency. The Journal of Biological Chemistry. 280: 25071-8. PMID 15878859 DOI: 10.1074/Jbc.M502490200 |
0.367 |
|
| 2005 |
Cohen JH, Piatigorsky J, Ding L, Colley NJ, Ward R, Horwitz J. Vertebrate-like betagamma-crystallins in the ocular lenses of a copepod. Journal of Comparative Physiology. a, Neuroethology, Sensory, Neural, and Behavioral Physiology. 191: 291-8. PMID 15702356 DOI: 10.1007/S00359-004-0594-4 |
0.357 |
|
| 2005 |
Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation. The Journal of Biological Chemistry. 280: 14485-91. PMID 15701626 DOI: 10.1074/Jbc.M500135200 |
0.358 |
|
| 2005 |
Treweek TM, Rekas A, Lindner RA, Walker MJ, Aquilina JA, Robinson CV, Horwitz J, Perng MD, Quinlan RA, Carver JA. R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. The Febs Journal. 272: 711-24. PMID 15670152 DOI: 10.1111/J.1742-4658.2004.04507.X |
0.382 |
|
| 2004 |
Horwitz J, Huang Q, Ding L. The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function? Experimental Eye Research. 79: 817-21. PMID 15642318 DOI: 10.1016/J.Exer.2004.05.007 |
0.366 |
|
| 2004 |
Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. The Journal of Biological Chemistry. 279: 28675-80. PMID 15117944 DOI: 10.1074/Jbc.M403348200 |
0.315 |
|
| 2004 |
Crookes WJ, Ding LL, Huang QL, Kimbell JR, Horwitz J, McFall-Ngai MJ. Reflectins: the unusual proteins of squid reflective tissues. Science (New York, N.Y.). 303: 235-8. PMID 14716016 DOI: 10.1126/Science.1091288 |
0.558 |
|
| 2004 |
Bullard B, Ferguson C, Minajeva A, Leake MC, Gautel M, Labeit D, Ding L, Labeit S, Horwitz J, Leonard KR, Linke WA. Association of the chaperone alphaB-crystallin with titin in heart muscle. The Journal of Biological Chemistry. 279: 7917-24. PMID 14676215 DOI: 10.1074/Jbc.M307473200 |
0.304 |
|
| 2002 |
Bova MP, Huang Q, Ding L, Horwitz J. Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. The Journal of Biological Chemistry. 277: 38468-75. PMID 12176992 DOI: 10.1074/Jbc.M205594200 |
0.368 |
|
| 2001 |
Piatigorsky J, Norman B, Dishaw LJ, Kos L, Horwitz J, Steinbach PJ, Kozmik Z. J3-crystallin of the jellyfish lens: similarity to saposins. Proceedings of the National Academy of Sciences of the United States of America. 98: 12362-7. PMID 11675486 DOI: 10.1073/Pnas.231310698 |
0.354 |
|
| 2001 |
Derham BK, van Boekel MA, Muchowski PJ, Clark JI, Horwitz J, Hepburne-Scott HW, de Jong WW, Crabbe MJ, Harding JJ. Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites. European Journal of Biochemistry / Febs. 268: 713-21. PMID 11168410 DOI: 10.1046/J.1432-1327.2001.01929.X |
0.351 |
|
| 2000 |
Horwitz J. The function of alpha-crystallin in vision. Seminars in Cell & Developmental Biology. 11: 53-60. PMID 10736264 DOI: 10.1006/Scdb.1999.0351 |
0.354 |
|
| 1999 |
Horwitz J, Bova MP, Ding LL, Haley DA, Stewart PL. Lens alpha-crystallin: function and structure. Eye (London, England). 13: 403-8. PMID 10627817 DOI: 10.1038/Eye.1999.114 |
0.733 |
|
| 1999 |
Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proceedings of the National Academy of Sciences of the United States of America. 96: 6137-42. PMID 10339554 DOI: 10.1073/Pnas.96.11.6137 |
0.748 |
|
| 1999 |
Haley DA, Horwitz J, Stewart PL. Image restrained modeling of alphaB-crystallin. Experimental Eye Research. 68: 133-6. PMID 9986751 DOI: 10.1006/Exer.1998.0610 |
0.699 |
|
| 1998 |
Horwitz J, Bova M, Huang QL, Ding L, Yaron O, Lowman S. Mutation of alpha B-crystallin: effects on chaperone-like activity. International Journal of Biological Macromolecules. 22: 263-9. PMID 9650081 DOI: 10.1016/S0141-8130(98)00024-5 |
0.337 |
|
| 1998 |
Crabb JW, Carlson A, Chen Y, Goldflam S, Intres R, West KA, Hulmes JD, Kapron JT, Luck LA, Horwitz J, Bok D. Structural and functional characterization of recombinant human cellular retinaldehyde-binding protein. Protein Science : a Publication of the Protein Society. 7: 746-57. PMID 9541407 DOI: 10.1002/Pro.5560070324 |
0.329 |
|
| 1998 |
Haley DA, Horwitz J, Stewart PL. The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. Journal of Molecular Biology. 277: 27-35. PMID 9514758 DOI: 10.1006/Jmbi.1997.1611 |
0.742 |
|
| 1997 |
Gong X, Li E, Klier G, Huang Q, Wu Y, Lei H, Kumar NM, Horwitz J, Gilula NB. Disruption of alpha3 connexin gene leads to proteolysis and cataractogenesis in mice. Cell. 91: 833-43. PMID 9413992 DOI: 10.1016/S0092-8674(00)80471-7 |
0.323 |
|
| 1997 |
Bova MP, Ding LL, Horwitz J, Fung BK. Subunit exchange of alphaA-crystallin. The Journal of Biological Chemistry. 272: 29511-7. PMID 9368012 DOI: 10.1074/Jbc.272.47.29511 |
0.371 |
|
| 1995 |
Rao PV, Huang QL, Horwitz J, Zigler JS. Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochimica Et Biophysica Acta. 1245: 439-47. PMID 8541324 DOI: 10.1016/0304-4165(95)00125-5 |
0.398 |
|
| 1995 |
Farahbakhsh ZT, Huang QL, Ding LL, Altenbach C, Steinhoff HJ, Horwitz J, Hubbell WL. Interaction of alpha-crystallin with spin-labeled peptides. Biochemistry. 34: 509-16. PMID 7819243 DOI: 10.1021/Bi00002A015 |
0.358 |
|
| 1995 |
Kantorow M, Horwitz J, van Boekel MA, de Jong WW, Piatigorsky J. Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A- and alpha B-crystallin subunits. The Journal of Biological Chemistry. 270: 17215-20. PMID 7615520 DOI: 10.1074/Jbc.270.29.17215 |
0.331 |
|
| 1995 |
Smulders RH, Merck KB, Aendekerk J, Horwitz J, Takemoto L, Slingsby C, Bloemendal H, De Jong WW. The mutation Asp69-->Ser affects the chaperone-like activity of alpha A-crystallin. European Journal of Biochemistry / Febs. 232: 834-8. PMID 7588723 DOI: 10.1111/J.1432-1033.1995.834Zz.X |
0.356 |
|
| 1993 |
Takemoto L, Emmons T, Horwitz J. The C-terminal region of alpha-crystallin: involvement in protection against heat-induced denaturation. The Biochemical Journal. 294: 435-8. PMID 8373358 DOI: 10.1042/Bj2940435 |
0.346 |
|
| 1993 |
Dove S, Horwitz J, McFall-Ngai M. A biochemical characterization of the photophore lenses of the midshipman fish, Porichthys notatus Girard. Journal of Comparative Physiology. a, Sensory, Neural, and Behavioral Physiology. 172: 565-72. PMID 8331605 DOI: 10.1007/Bf00213679 |
0.593 |
|
| 1993 |
Merck KB, Horwitz J, Kersten M, Overkamp P, Gaestel M, Bloemendal H, de Jong WW. Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein. Molecular Biology Reports. 18: 209-15. PMID 8114688 DOI: 10.1007/Bf01674432 |
0.359 |
|
| 1993 |
Rao PV, Horwitz J, Zigler JS. Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation. Biochemical and Biophysical Research Communications. 190: 786-93. PMID 8094957 DOI: 10.1006/Bbrc.1993.1118 |
0.377 |
|
| 1992 |
Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proceedings of the National Academy of Sciences of the United States of America. 89: 10449-53. PMID 1438232 DOI: 10.1073/Pnas.89.21.10449 |
0.37 |
|
| 1992 |
Horwitz J, Emmons T, Takemoto L. The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent. Current Eye Research. 11: 817-22. PMID 1424725 DOI: 10.3109/02713689209000754 |
0.359 |
|
| 1991 |
Yu NT, Cai MZ, Lee BS, Kuck JF, McFall-Ngai M, Horwitz J. Resonance Raman detection of a carotenoid in the lens of the deep-sea hatchetfish. Experimental Eye Research. 52: 475-9. PMID 2037027 DOI: 10.1016/0014-4835(91)90045-G |
0.531 |
|
| 1991 |
Bhat SP, Horwitz J, Srinivasan A, Ding L. Alpha B-crystallin exists as an independent protein in the heart and in the lens. European Journal of Biochemistry / Febs. 202: 775-81. PMID 1765091 DOI: 10.1111/J.1432-1033.1991.Tb16432.X |
0.356 |
|
| 1990 |
McFall-Ngai MJ, Horwitz J. A comparative study of the thermal stability of the vertebrate eye lens: Antarctic ice fish to the desert iguana. Experimental Eye Research. 50: 703-9. PMID 2373164 DOI: 10.1016/0014-4835(90)90117-D |
0.55 |
|
| 1989 |
Piatigorsky J, Horwitz J, Kuwabara T, Cutress CE. The cellular eye lens and crystallins of cubomedusan jellyfish. Journal of Comparative Physiology. a, Sensory, Neural, and Behavioral Physiology. 164: 577-87. PMID 2565398 DOI: 10.1007/Bf00614500 |
0.358 |
|
| 1989 |
Takemoto L, Straatsma B, Horwitz J. Immunochemical characterization of the major low molecular weight polypeptide (10K) from human cataractous lenses. Experimental Eye Research. 48: 261-70. PMID 2466675 DOI: 10.1016/S0014-4835(89)80075-2 |
0.32 |
|
| 1988 |
MCFALL-NGAI M, DING L, CHILDRESS J, HORWITZ J. Biochemical Characteristics of the Pigmentation of Mesopelagic Fish Lenses The Biological Bulletin. 175: 397-402. DOI: 10.2307/1541731 |
0.564 |
|
| 1987 |
Shinohara T, Dietzschold B, Craft CM, Wistow G, Early JJ, Donoso LA, Horwitz J, Tao R. Primary and secondary structure of bovine retinal S antigen (48-kDa protein). Proceedings of the National Academy of Sciences of the United States of America. 84: 6975-9. PMID 3478675 DOI: 10.1073/Pnas.84.20.6975 |
0.307 |
|
| 1987 |
Horwitz J, Bok D. Conformational properties of the main intrinsic polypeptide (MIP26) isolated from lens plasma membranes. Biochemistry. 26: 8092-8. PMID 3442647 DOI: 10.1021/Bi00399A012 |
0.349 |
|
| 1986 |
McFall-Ngai M, Crescitelli F, Childress J, Horwitz J. Patterns of pigmentation in the eye lens of the deep-sea hatchetfish, Argyropelecus affinis Garman. Journal of Comparative Physiology. a, Sensory, Neural, and Behavioral Physiology. 159: 791-800. PMID 3806437 DOI: 10.1007/Bf00603732 |
0.56 |
|
| 1986 |
Zigler JS, Russell P, Horwitz J, Reddy VN, Kinoshita JH. Further studies on low molecular weight crystallins: relationship between the bovine beta s, the human 24kD protein and the gamma-crystallins. Current Eye Research. 5: 395-401. PMID 3720347 DOI: 10.3109/02713688609025179 |
0.337 |
|
| 1986 |
McFall-Ngai M, Horwitz J, Ding LL, Lacey L. Age-dependent changes in the heat-stable crystallin, beta Bp, of the human lens. Current Eye Research. 5: 387-94. PMID 3720346 DOI: 10.3109/02713688609025178 |
0.545 |
|
| 1985 |
Williams LA, Ding L, Horwitz J, Piatigorsky J. tau-Crystallin from the turtle lens: purification and partial characterization. Experimental Eye Research. 40: 741-9. PMID 4007081 DOI: 10.1016/0014-4835(85)90143-5 |
0.39 |
|
| 1985 |
Takemoto LJ, Hansen JS, Zigler JS, Horwitz J. Characterization of polypeptides from human nuclear cataracts by Western blot analysis. Experimental Eye Research. 40: 205-12. PMID 3979461 DOI: 10.1016/0014-4835(85)90005-3 |
0.315 |
|
| 1985 |
Crescitelli F, McFall-Ngai M, Horwitz J. The visual pigment sensitivity hypothesis: further evidence from fishes of varying habitats. Journal of Comparative Physiology. a, Sensory, Neural, and Behavioral Physiology. 157: 323-33. PMID 3837092 DOI: 10.1007/Bf00618122 |
0.525 |
|
| 1985 |
McFall-Ngai MJ, Ding LL, Takemoto LJ, Horwitz J. Spatial and temporal mapping of the age-related changes in human lens crystallins. Experimental Eye Research. 41: 745-58. PMID 3830737 DOI: 10.1016/0014-4835(85)90183-6 |
0.589 |
|
| 1984 |
Takemoto LJ, Hansen JS, Horwitz J. High molecular weight aggregates from human cataracts: characterization by Western blot analysis. Biochemical and Biophysical Research Communications. 122: 1028-33. PMID 6477547 DOI: 10.1016/0006-291X(84)91194-X |
0.334 |
|
| 1984 |
Gorin MB, Yancey SB, Cline J, Revel JP, Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell. 39: 49-59. PMID 6207938 DOI: 10.1016/0092-8674(84)90190-9 |
0.301 |
|
| 1983 |
McFadden PN, Horwitz J, Clarke S. Protein carboxyl methyltransferase from cow eye lens Biochemical and Biophysical Research Communications. 113: 418-424. PMID 6870865 DOI: 10.1016/0006-291X(83)91742-4 |
0.332 |
|
| 1982 |
Takemoto LJ, Hansen JS, Horwitz J. Biochemical analysis of microdissected sections from the normal and cataractous human Lens Current Eye Research. 2: 443-450. PMID 7182105 DOI: 10.3109/02713688208996347 |
0.308 |
|
| 1982 |
Williams LA, Piatigorsky J, Horwitz J. Structural features of δ-crystallin of turtle lens Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 708: 49-56. PMID 7171611 DOI: 10.1016/0167-4838(82)90202-3 |
0.377 |
|
| 1981 |
Zigler JS, Horwitz J, Kinoshita JH. Studies on the low molecular weight proteins of human lens. Experimental Eye Research. 32: 21-30. PMID 6783435 DOI: 10.1016/S0014-4835(81)80035-8 |
0.324 |
|
| 1980 |
Horwitz J, Piatigorsky J. Evolutionary and developmental differences in delta-crystallin from bird and reptile lenses. Circular dichroism and fluorescence studies Biochimica Et Biophysica Acta. 624: 21-29. PMID 7407233 DOI: 10.1016/0005-2795(80)90221-4 |
0.368 |
|
| 1980 |
Horwitz J, Wong MM. Peptide mapping by limited proteolysis in sodium dodecyl sulfate of the main intrinsic polypeptides isolated from human and bovine lens plasma membranes Bba - Protein Structure. 622: 134-143. PMID 6988013 DOI: 10.1016/0005-2795(80)90165-8 |
0.323 |
|
| 1979 |
Wong MM, Robertson NP, Horwitz J. Heat induced aggregation of the sodium dodecyl sulfate-solubilized main intrinsic polypeptide isolated from bovine lens plasma membrane. Biochemical and Biophysical Research Communications. 84: 158-65. PMID 728124 DOI: 10.1016/0006-291X(78)90277-2 |
0.305 |
|
| 1977 |
Horwitz J, Kabasawa I, Kinoshita JH. Conformation of gamma-crystallins of the calf lens: Effects of temperature and denaturing agents Experimental Eye Research. 25: 199-208. PMID 913511 DOI: 10.1016/0014-4835(77)90132-4 |
0.333 |
|
| 1977 |
Piatigorsky J, Horwitz J, Simpson RT. Partial dissociation and renaturation of embryonic chick delta-crystallin. Characterization by ultracentrifugation and circular dichroism. Biochimica Et Biophysica Acta. 490: 279-89. PMID 556957 DOI: 10.1016/0005-2795(77)90003-4 |
0.359 |
|
| 1976 |
Horwitz J. Some properties of the low molecular weight α-crystallin from normal human lens: Comparison with bovine lens Experimental Eye Research. 23: 471-481. PMID 1001375 DOI: 10.1016/0014-4835(76)90156-1 |
0.327 |
|
| 1972 |
Strickland EH, Wilchek M, Horwitz J, Billups C. Effects of hydrogen bonding and temperature upon the near ultraviolet circular dichroism and absorption spectra of tyrosine and O-methyl tyrosine derivatives. The Journal of Biological Chemistry. 247: 572-80. PMID 5009702 |
0.541 |
|
| 1971 |
Strickland EH, Horwitz J, Kay E, Shannon LM, Wilchek M, Billups C. Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester. Biochemistry. 10: 2631-8. PMID 5105033 |
0.548 |
|
| 1971 |
Horwitz J, Strickland EH. Absorption and circular dichroism spectra of ribonuclease-S at 77 degrees K Journal of Biological Chemistry. 246: 3749-3752. PMID 5103846 |
0.558 |
|
| 1970 |
Strickland EH, Wilchek M, Horwitz J, Billups C. Low temperature circular dichroism of tyrosyl and tryptophanyl diketopiperazines. The Journal of Biological Chemistry. 245: 4168-77. PMID 5503260 |
0.538 |
|
| 1970 |
Strickland EH, Horwitz J, Billups C. Near-ultraviolet absorption bands of tryptophan. Studies using indole and 3-methylindole as models Biochemistry. 9: 4914-4921. PMID 5480156 |
0.569 |
|
| 1970 |
Horwitz J, Strickland EH, Billups C. Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77°K Journal of the American Chemical Society. 92: 2119-2129. PMID 5435277 |
0.588 |
|
| 1970 |
Horwitz J, Strickland EH, Billups C. Analyse Der Schwingungsstruktur Im Nah‐Uv‐Zirkulardichroismus Und Absorptionsspektren Von Tyrosinderivaten Und Ribonuclease A Bei 77 Grad K Cheminform. 1. DOI: 10.1002/Chin.197027124 |
0.575 |
|
| 1969 |
Strickland EH, Horwitz J, Billups C. Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77°K Biochemistry. 8: 3205-3213. PMID 5817721 |
0.6 |
|
| 1969 |
Horwitz J, Strickland EH, Billups C. Analysis of vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of phenylalanine and its derivatives Journal of the American Chemical Society. 91: 184-190. PMID 5782812 DOI: 10.1021/Ja01029A034 |
0.604 |
|
| 1969 |
Strickland EH, Horwitz J, Billups C. Fine structure in the near ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77 degrees K. UCLA 12-724 Ucla [Reports]. U. S. Atomic Energy Commission. 85-86. PMID 5372506 |
0.576 |
|
| 1968 |
Horwitz J, Billups C, Strickland EH. Low temperature circular dichroism of proteins and amino acids. UCLA-12-686 Ucla [Reports]. U. S. Atomic Energy Commission. 82. PMID 5732290 |
0.564 |
|
| 1968 |
Strickland EH, Kay E, Shannon LM, Horwitz J. Circular dichroism of horseradish peroxidase isoenzymes and apoisoenzymes. UCLA-12-686. Ucla [Reports]. U.S. Atomic Energy Commission. 79-80. PMID 5732289 |
0.56 |
|
| 1968 |
Strickland EH, Kay E, Shannon LM, Horwitz J. Peroxidase isoenzymes from horseradish roots. 3. Circular dichroism of isoenzymes and apoisoenzymes. The Journal of Biological Chemistry. 243: 3560-5. PMID 5658539 |
0.534 |
|
| 1968 |
Horwitz J, Strickland EH, Kay E. Increased resolution of circular dichroic spectra using a computer of average transients Analytical Biochemistry. 23: 363-367. PMID 5657811 DOI: 10.1016/0003-2697(68)90373-4 |
0.601 |
|
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