| Year |
Citation |
Score |
| 2007 |
Li Y, Schmitz KR, Salerno JC, Koretz JF. The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality. Molecular Vision. 13: 1758-68. PMID 17960114 |
0.344 |
|
| 2005 |
Yang C, Salerno JC, Koretz JF. NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin. Molecular Vision. 11: 641-7. PMID 16145541 |
0.726 |
|
| 2005 |
Eifert C, Burgio MR, Bennett PM, Salerno JC, Koretz JF. N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function. Biochimica Et Biophysica Acta. 1748: 146-56. PMID 15769591 DOI: 10.1016/J.Bbapap.2004.12.015 |
0.698 |
|
| 2005 |
Strenk SA, Strenk LM, Koretz JF. The mechanism of presbyopia Progress in Retinal and Eye Research. 24: 379-393. PMID 15708834 DOI: 10.1016/J.Preteyeres.2004.11.001 |
0.309 |
|
| 2004 |
Regini JW, Grossmann JG, Burgio MR, Malik NS, Koretz JF, Hodson SA, Elliott GF. Structural Changes in α-Crystallin and Whole Eye Lens During Heating, Observed by Low-angle X-ray Diffraction Journal of Molecular Biology. 336: 1185-1194. PMID 15037078 DOI: 10.1016/S0022-2836(03)00814-3 |
0.729 |
|
| 2003 |
Salerno JC, Eifert CL, Salerno KM, Koretz JF. Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. Protein Engineering. 16: 847-51. PMID 14631074 DOI: 10.1093/Protein/Gzg102 |
0.434 |
|
| 2002 |
Tiffany JM, Koretz JF. Viscosity of alpha-crystallin solutions International Journal of Biological Macromolecules. 30: 179-185. PMID 12063120 DOI: 10.1016/S0141-8130(02)00018-1 |
0.374 |
|
| 2002 |
Koretz JF, Cook CA, Kaufman PL. Aging of the human lens: changes in lens shape upon accommodation and with accommodative loss. Journal of the Optical Society of America. a, Optics, Image Science, and Vision. 19: 144-51. PMID 11778717 DOI: 10.1364/Josaa.19.000144 |
0.312 |
|
| 2001 |
Burgio MR, Bennett PM, Koretz JF. Heat-induced quaternary transitions in hetero- and homo-polymers of α-crystallin Molecular Vision. 7: 228-233. PMID 11590365 |
0.737 |
|
| 2001 |
Koretz JF, Cook CA. Aging of the optics of the human eye: Lens refraction models and principal plane locations Optometry and Vision Science. 78: 396-404. PMID 11444628 DOI: 10.1097/00006324-200106000-00011 |
0.309 |
|
| 2001 |
Koretz JF, Cook CA, Kaufman PL. Aging of the human lens: changes in lens shape at zero-diopter accommodation. Journal of the Optical Society of America. a, Optics, Image Science, and Vision. 18: 265-72. PMID 11205971 DOI: 10.1364/Josaa.18.000265 |
0.319 |
|
| 2000 |
Burgio MR, Kim CJ, Dow CC, Koretz JF. Correlation between the chaperone-like activity and aggregate size of α-crystallin with increasing temperature Biochemical and Biophysical Research Communications. 268: 426-432. PMID 10679221 DOI: 10.1006/Bbrc.1999.2036 |
0.74 |
|
| 1999 |
Brown NP, Koretz JF, Bron AJ. The development and maintenance of emmetropia Eye. 13: 83-92. PMID 10396390 DOI: 10.1038/Eye.1999.16 |
0.318 |
|
| 1998 |
Doss-Pepe EW, Carew EL, Koretz JF. Studies of the denaturation patterns of bovine alpha-crystallin using an ionic denaturant, guanidine hydrochloride and a non-ionic denaturant, urea Experimental Eye Research. 67: 657-679. PMID 9990331 DOI: 10.1006/Exer.1998.0561 |
0.47 |
|
| 1998 |
Koretz JF, Doss EW, Labutti JN. Environmental factors influencing the chaperone-like activity of α-crystallin International Journal of Biological Macromolecules. 22: 283-294. PMID 9650083 DOI: 10.1016/S0141-8130(98)00026-9 |
0.452 |
|
| 1998 |
Doss EW, Ward KA, Koretz JF. Investigation of the 'fines' hypothesis of primary open-angle glaucoma: The possible role of alpha-crystallin Ophthalmic Research. 30: 142-156. PMID 9618718 DOI: 10.1159/000055468 |
0.479 |
|
| 1997 |
Doss EW, Ward KA, Koretz JF. Preliminary studies on the aggregation process of alpha-crystallin Experimental Eye Research. 65: 255-266. PMID 9268594 DOI: 10.1006/Exer.1997.0337 |
0.418 |
|
| 1997 |
Koretz JF, Doss EW, Reid GH. Analysis of the factors involved in the loss and restoration of the chaperone-like function of α-crystallin Biochemical and Biophysical Research Communications. 231: 270-276. PMID 9070262 DOI: 10.1006/Bbrc.1997.6079 |
0.497 |
|
| 1996 |
Ward KA, Green I, Reid G, Koretz JF. Alpha-crystallin incorporates to form proteoliposomes Investigative Ophthalmology and Visual Science. 37: S599. |
0.32 |
|
| 1992 |
Radlick LW, Koretz JF. Biophysical characterization of α-crystallin aggregates: validation of the micelle hypothesis Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1120: 193-200. PMID 1562586 DOI: 10.1016/0167-4838(92)90269-J |
0.513 |
|
| 1989 |
Clauwaert J, Ellerton HD, Koretz JF, Thomson K, Augusteyn RC. The effect of temperature on the renaturation of αcrystallin Current Eye Research. 8: 397-403. PMID 2721227 DOI: 10.3109/02713688908996387 |
0.411 |
|
| 1989 |
Koretz JF, Kaufman PL, Neider MW, Goeckner PA. Accommodation and presbyopia in the human eye--aging of the anterior segment. Vision Research. 29: 1685-92. PMID 2631389 DOI: 10.1016/0042-6989(89)90150-8 |
0.301 |
|
| 1989 |
Tumminia SJ, Koretz JF, Landau JV. Hydrostatic pressure studies of native and synthetic thick filaments: in vitro myosin aggregates at pH 7.0 with and without C-protein Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 999: 300-312. PMID 2574997 DOI: 10.1016/0167-4838(89)90013-7 |
0.344 |
|
| 1989 |
Augusteyn RC, Koretz JF, Schurtenberger P. The effect of phosphorylation on the structure of α-crystallin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 999: 293-299. PMID 2513887 DOI: 10.1016/0167-4838(89)90012-5 |
0.4 |
|
| 1988 |
Koretz JF, Augusteyn RC. Electron microscopy of native and reconstituted alpha crystallin aggregates Current Eye Research. 7: 25-30. PMID 3359802 DOI: 10.3109/02713688809047016 |
0.464 |
|
| 1987 |
Koretz JF, Bertasso AM, Neider MW, True-Gabelt BA, Kaufman PL. Slit-lamp studies of the rhesus monkey eye: II. Changes in crystalline lens shape, thickness and position during accommodation and aging. Experimental Eye Research. 45: 317-26. PMID 3653294 DOI: 10.1016/S0014-4835(87)80153-7 |
0.319 |
|
| 1987 |
Koretz JF, Neider MW, Kaufman PL, Bertasso AM, DeRousseau CJ, Bito LZ. Slit-lamp studies of the rhesus monkey eye. I. Survey of the anterior segment. Experimental Eye Research. 44: 307-18. PMID 3582515 DOI: 10.1016/S0014-4835(87)80014-3 |
0.302 |
|
| 1987 |
Augusteyn RC, Koretz JF. A possible structure for α-crystallin Febs Letters. 222: 1-5. PMID 3308513 DOI: 10.1016/0014-5793(87)80180-1 |
0.514 |
|
| 1984 |
Koretz JF, Handelman GH, Phelps Brown N. Analysis of human crystalline lens curvature as a function of accommodative state and age Vision Research. 24: 1141-1151. PMID 6523736 DOI: 10.1016/0042-6989(84)90168-8 |
0.331 |
|
| 1983 |
Koretz JF, Handelman GH. A model for accommodation in the young human eye: The effects of lens elastic anisotropy on the mechanism Vision Research. 23: 1679-1686. PMID 6666071 DOI: 10.1016/0042-6989(83)90183-9 |
0.319 |
|
| 1982 |
Koretz JF, Handelman GH. Model of the accommodative mechanism in the human eye Vision Research. 22: 917-927. PMID 7135854 DOI: 10.1016/0042-6989(82)90028-1 |
0.325 |
|
| 1982 |
Koretz JF, Coluccio LM, Bertasso AM. The aggregation characteristics of column-purified rabbit skeletal myosin in the presence and absence of C-protein at pH 7.0. Biophysical Journal. 37: 433-40. PMID 6895856 DOI: 10.1016/S0006-3495(82)84689-4 |
0.653 |
|
| 1979 |
Koretz JF. Effects of C-protein on synthetic myosin filament structure Biophysical Journal. 27: 433-446. PMID 263692 |
0.315 |
|
| 1975 |
Koretz JF, Taylor EW. Transient state kinetic studies of proton liberation by myosin and subfragment 1. The Journal of Biological Chemistry. 250: 6344-50. PMID 239944 |
0.445 |
|
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