Year |
Citation |
Score |
2022 |
Shoup D, Roth A, Puchalla J, Rye HS. The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones. Frontiers in Molecular Biosciences. 9: 915307. PMID 35874607 DOI: 10.3389/fmolb.2022.915307 |
0.34 |
|
2022 |
Naqvi MM, Avellaneda MJ, Roth A, Koers EJ, Roland A, Sunderlikova V, Kramer G, Rye HS, Tans SJ. Protein chain collapse modulation and folding stimulation by GroEL-ES. Science Advances. 8: eabl6293. PMID 35245117 DOI: 10.1126/sciadv.abl6293 |
0.354 |
|
2018 |
Roth A, Rye H. Abstract 294: Investigating the Small Heat Shock Proteins Impact on Aggregate Inhibition Circulation Research. 123. DOI: 10.1161/Res.123.Suppl_1.294 |
0.313 |
|
2017 |
Weaver J, Jiang M, Roth A, Puchalla J, Zhang J, Rye HS. GroEL actively stimulates folding of the endogenous substrate protein PepQ. Nature Communications. 8: 15934. PMID 28665408 DOI: 10.1038/Ncomms15934 |
0.444 |
|
2015 |
Brooks A, Shoup D, Kustigian L, Puchalla J, Carr CM, Rye HS. Single particle fluorescence burst analysis of epsin induced membrane fission. Plos One. 10: e0119563. PMID 25799353 DOI: 10.1371/Journal.Pone.0119563 |
0.374 |
|
2014 |
Weaver J, Watts T, Li P, Rye HS. Structural basis of substrate selectivity of E. coli prolidase. Plos One. 9: e111531. PMID 25354344 DOI: 10.1371/Journal.Pone.0111531 |
0.329 |
|
2014 |
Weaver J, Rye HS. The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein. The Journal of Biological Chemistry. 289: 23219-32. PMID 24970895 DOI: 10.1074/Jbc.M114.577205 |
0.492 |
|
2013 |
Lin Z, Puchalla J, Shoup D, Rye HS. Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding. The Journal of Biological Chemistry. 288: 30944-55. PMID 24022487 DOI: 10.1074/Jbc.M113.480178 |
0.518 |
|
2013 |
Krantz KC, Puchalla J, Thapa R, Kobayashi C, Bisher M, Viehweg J, Carr CM, Rye HS. Clathrin coat disassembly by the yeast Hsc70/Ssa1p and auxilin/Swa2p proteins observed by single-particle burst analysis spectroscopy. The Journal of Biological Chemistry. 288: 26721-30. PMID 23913685 DOI: 10.1074/Jbc.M113.491753 |
0.686 |
|
2013 |
Chen DH, Madan D, Weaver J, Lin Z, Schröder GF, Chiu W, Rye HS. Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell. 153: 1354-65. PMID 23746846 DOI: 10.1016/J.Cell.2013.04.052 |
0.778 |
|
2013 |
Weaver JS, Rye HS. The Persistent Effect of Initial Substrate Protein Conformation on Productive Folding by Groel-Groes Biophysical Journal. 104: 572a. DOI: 10.1016/J.Bpj.2012.11.3175 |
0.496 |
|
2013 |
Shoup DW, Rye H, Puchalla J. Development of Fluorescence assays for Studying Protein Disaggregation by Molecular Chaperones Biophysical Journal. 104: 570a. DOI: 10.1016/J.Bpj.2012.11.3164 |
0.475 |
|
2009 |
Karuri NW, Lin Z, Rye HS, Schwarzbauer JE. Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer. The Journal of Biological Chemistry. 284: 3445-52. PMID 19064996 DOI: 10.1074/Jbc.M805025200 |
0.399 |
|
2008 |
Madan D, Lin Z, Rye HS. Triggering protein folding within the GroEL-GroES complex. The Journal of Biological Chemistry. 283: 32003-13. PMID 18782766 DOI: 10.1074/Jbc.M802898200 |
0.793 |
|
2008 |
Puchalla J, Krantz K, Austin R, Rye H. Burst analysis spectroscopy: a versatile single-particle approach for studying distributions of protein aggregates and fluorescent assemblies. Proceedings of the National Academy of Sciences of the United States of America. 105: 14400-5. PMID 18780782 DOI: 10.1073/Pnas.0805969105 |
0.704 |
|
2008 |
Lin Z, Madan D, Rye HS. GroEL stimulates protein folding through forced unfolding. Nature Structural & Molecular Biology. 15: 303-11. PMID 18311152 DOI: 10.1038/Nsmb.1394 |
0.779 |
|
2006 |
Lin Z, Rye HS. GroEL-mediated protein folding: making the impossible, possible. Critical Reviews in Biochemistry and Molecular Biology. 41: 211-39. PMID 16849107 DOI: 10.1080/10409230600760382 |
0.47 |
|
2004 |
Lin Z, Rye HS. Expansion and compression of a protein folding intermediate by GroEL. Molecular Cell. 16: 23-34. PMID 15469819 DOI: 10.1016/J.Molcel.2004.09.003 |
0.468 |
|
2003 |
Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. The Embo Journal. 22: 4877-87. PMID 14517228 DOI: 10.1093/Emboj/Cdg477 |
0.604 |
|
2001 |
Rye HS. Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction. Methods (San Diego, Calif.). 24: 278-88. PMID 11403576 DOI: 10.1006/Meth.2001.1188 |
0.517 |
|
1999 |
Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell. 97: 325-38. PMID 10319813 DOI: 10.1016/S0092-8674(00)80742-4 |
0.627 |
|
1998 |
Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL. Structure and function in GroEL-mediated protein folding. Annual Review of Biochemistry. 67: 581-608. PMID 9759498 DOI: 10.1146/Annurev.Biochem.67.1.581 |
0.648 |
|
1998 |
Horwich AL, Burston SG, Rye HS, Weissman JS, Fenton WA. Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods in Enzymology. 290: 141-6. PMID 9534157 DOI: 10.1016/S0076-6879(98)90013-1 |
0.682 |
|
1997 |
Rye HS, Burston SG, Fenton WA, Beechem JM, Xu Z, Sigler PB, Horwich AL. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388: 792-8. PMID 9285593 DOI: 10.1038/42047 |
0.612 |
|
1996 |
Drees BL, Rye HS, Glazer AN, Nelson HC. Environment-sensitive labels in multiplex fluorescence analyses of protein-DNA complexes. The Journal of Biological Chemistry. 271: 32168-73. PMID 8943271 DOI: 10.1074/Jbc.271.50.32168 |
0.667 |
|
1996 |
Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84: 481-90. PMID 8608602 DOI: 10.1016/S0092-8674(00)81293-3 |
0.729 |
|
1995 |
Rye HS, Glazer AN. Interaction of dimeric intercalating dyes with single-stranded DNA. Nucleic Acids Research. 23: 1215-22. PMID 7739900 DOI: 10.1093/Nar/23.7.1215 |
0.62 |
|
1994 |
Zhu H, Clark SM, Benson SC, Rye HS, Glazer AN, Mathies RA. High-sensitivity capillary electrophoresis of double-stranded DNA fragments using monomeric and dimeric fluorescent intercalating dyes. Analytical Chemistry. 66: 1941-8. PMID 8067520 DOI: 10.1021/Ac00085A004 |
0.676 |
|
1994 |
Mathies RA, Scherer JR, Quesada MA, Rye HS, Glazer AN. Laser-excited confocal-fluorescence gel scanner Review of Scientific Instruments. 65: 807-812. DOI: 10.1063/1.1144905 |
0.633 |
|
1993 |
Rye HS, Yue S, Quesada MA, Haugland RP, Mathies RA, Glazer AN. Picogram detection of stable dye-DNA intercalation complexes with two-color laser-excited confocal fluorescence gel scanner. Methods in Enzymology. 217: 414-31. PMID 8474342 DOI: 10.1016/0076-6879(93)17080-O |
0.671 |
|
1993 |
Rye HS, Drees BL, Nelson HC, Glazer AN. Stable fluorescent dye-DNA complexes in high sensitivity detection of protein-DNA interactions. Application to heat shock transcription factor. The Journal of Biological Chemistry. 268: 25229-38. PMID 8227088 |
0.614 |
|
1993 |
Rye HS, Dabora JM, Quesada MA, Mathies RA, Glazer AN. Fluorometric assay using dimeric dyes for double- and single-stranded DNA and RNA with picogram sensitivity. Analytical Biochemistry. 208: 144-50. PMID 7679561 DOI: 10.1006/Abio.1993.1020 |
0.667 |
|
1992 |
Rye HS, Yue S, Wemmer DE, Quesada MA, Haugland RP, Mathies RA, Glazer AN. Stable fluorescent complexes of double-stranded DNA with bis-intercalating asymmetric cyanine dyes: properties and applications. Nucleic Acids Research. 20: 2803-12. PMID 1614866 DOI: 10.1093/Nar/20.11.2803 |
0.692 |
|
1992 |
Glazer AN, Rye HS. Stable dye-DNA intercalation complexes as reagents for high-sensitivity fluorescence detection. Nature. 359: 859-61. PMID 1436062 DOI: 10.1038/359859A0 |
0.623 |
|
1991 |
Rye HS, Quesada MA, Peck K, Mathies RA, Glazer AN. High-sensitivity two-color detection of double-stranded DNA with a confocal fluorescence gel scanner using ethidium homodimer and thiazole orange. Nucleic Acids Research. 19: 327-33. PMID 2014172 DOI: 10.1093/Nar/19.2.327 |
0.691 |
|
1991 |
Quesada MA, Rye HS, Gingrich JC, Glazer AN, Mathies RA. High-sensitivity DNA detection with a laser-excited confocal fluorescence gel scanner. Biotechniques. 10: 616-25. PMID 1910779 |
0.561 |
|
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