| Year |
Citation |
Score |
| 2023 |
Rose GD. From propensities to patterns to principles in protein folding. Proteins. PMID 37353953 DOI: 10.1002/prot.26540 |
0.38 |
|
| 2022 |
Chen SJ, Hassan M, Jernigan RL, Jia K, Kihara D, Kloczkowski A, Kotelnikov S, Kozakov D, Liang J, Liwo A, Matysiak S, Meller J, Micheletti C, Mitchell JC, Mondal S, ... ... Rose GD, et al. Opinion: Protein folds vs. protein folding: Differing questions, different challenges. Proceedings of the National Academy of Sciences of the United States of America. 120: e2214423119. PMID 36580595 DOI: 10.1073/pnas.2214423119 |
0.363 |
|
| 2021 |
Rose GD. Reframing the Protein Folding Problem: Entropy as Organizer. Biochemistry. 60: 3753-3761. PMID 34855369 DOI: 10.1021/acs.biochem.1c00687 |
0.369 |
|
| 2021 |
Škrbić T, Maritan A, Giacometti A, Rose GD, Banavar JR. Building blocks of protein structures: Physics meets biology. Physical Review. E. 104: 014402. PMID 34412233 DOI: 10.1103/PhysRevE.104.014402 |
0.352 |
|
| 2021 |
Rose GD. Protein folding - seeing is deceiving. Protein Science : a Publication of the Protein Society. PMID 33938055 DOI: 10.1002/pro.4096 |
0.38 |
|
| 2019 |
Rose GD. Ramachandran maps for side chains in globular proteins. Proteins. PMID 30629766 DOI: 10.1002/Prot.25656 |
0.47 |
|
| 2016 |
Baldwin RL, Rose GD. How the hydrophobic factor drives protein folding. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791131 DOI: 10.1073/Pnas.1610541113 |
0.386 |
|
| 2015 |
Chellapa GD, Rose GD. On interpretation of protein X-ray structures: Planarity of the peptide unit. Proteins. 83: 1687-92. PMID 26148341 DOI: 10.1002/Prot.24854 |
0.413 |
|
| 2013 |
Baldwin RL, Rose GD. Molten globules, entropy-driven conformational change and protein folding. Current Opinion in Structural Biology. 23: 4-10. PMID 23237704 DOI: 10.1016/J.Sbi.2012.11.004 |
0.515 |
|
| 2013 |
Porter LL, Rose GD. 165 Protein domains: a thermodynamic definition Journal of Biomolecular Structure & Dynamics. 31: 107-107. DOI: 10.1080/07391102.2013.786407 |
0.46 |
|
| 2012 |
Chellapa GD, Rose GD. Reducing the dimensionality of the protein-folding search problem. Protein Science : a Publication of the Protein Society. 21: 1231-40. PMID 22692765 DOI: 10.1002/Pro.2106 |
0.507 |
|
| 2012 |
Porter LL, Rose GD. A thermodynamic definition of protein domains. Proceedings of the National Academy of Sciences of the United States of America. 109: 9420-5. PMID 22635268 DOI: 10.1073/Pnas.1202604109 |
0.476 |
|
| 2011 |
Tompa P, Rose GD. The Levinthal paradox of the interactome. Protein Science : a Publication of the Protein Society. 20: 2074-9. PMID 21987416 DOI: 10.1002/Pro.747 |
0.323 |
|
| 2011 |
Porter LL, Rose GD. Comment on "Revisiting the Ramachandran plot from a new angle". Protein Science : a Publication of the Protein Society. 20: 1771-3; author reply. PMID 21898646 DOI: 10.1002/Pro.724 |
0.384 |
|
| 2011 |
Gong H, Porter LL, Rose GD. Counting peptide-water hydrogen bonds in unfolded proteins. Protein Science : a Publication of the Protein Society. 20: 417-27. PMID 21280132 DOI: 10.1002/Pro.574 |
0.423 |
|
| 2011 |
Porter LL, Rose GD. Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints. Proceedings of the National Academy of Sciences of the United States of America. 108: 109-13. PMID 21148101 DOI: 10.1073/Pnas.1014674107 |
0.431 |
|
| 2011 |
Perskie LL, Rose GD. Negative Design in Protein Coils Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.3035 |
0.493 |
|
| 2010 |
Baldwin RL, Frieden C, Rose GD. Dry molten globule intermediates and the mechanism of protein unfolding. Proteins. 78: 2725-37. PMID 20635344 DOI: 10.1002/Prot.22803 |
0.528 |
|
| 2010 |
Perskie LL, Rose GD. Physical-chemical determinants of coil conformations in globular proteins. Protein Science : a Publication of the Protein Society. 19: 1127-36. PMID 20512968 DOI: 10.1002/pro.399 |
0.414 |
|
| 2009 |
Yuschok TJ, Rose GD. Hierarchic organization of globular proteins. A control study. International Journal of Peptide and Protein Research. 21: 479-484. PMID 6885237 DOI: 10.1111/J.1399-3011.1983.Tb02675.X |
0.495 |
|
| 2008 |
Bolen DW, Rose GD. Structure and energetics of the hydrogen-bonded backbone in protein folding. Annual Review of Biochemistry. 77: 339-62. PMID 18518824 DOI: 10.1146/Annurev.Biochem.77.061306.131357 |
0.491 |
|
| 2008 |
Perskie LL, Street TO, Rose GD. Structures, basins, and energies: a deconstruction of the Protein Coil Library. Protein Science : a Publication of the Protein Society. 17: 1151-61. PMID 18434497 DOI: 10.1110/Ps.035055.108 |
0.498 |
|
| 2008 |
Gong H, Rose GD. Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model. Proceedings of the National Academy of Sciences of the United States of America. 105: 3321-6. PMID 18305164 DOI: 10.1073/Pnas.0712240105 |
0.419 |
|
| 2007 |
Street TO, Fitzkee NC, Perskie LL, Rose GD. Physical-chemical determinants of turn conformations in globular proteins. Protein Science : a Publication of the Protein Society. 16: 1720-7. PMID 17656584 DOI: 10.1110/Ps.072898507 |
0.429 |
|
| 2007 |
Gong H, Shen Y, Rose GD. Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly. Protein Science : a Publication of the Protein Society. 16: 1515-21. PMID 17656574 DOI: 10.1110/Ps.072988407 |
0.518 |
|
| 2006 |
Rose GD, Fleming PJ, Banavar JR, Maritan A. A backbone-based theory of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 103: 16623-33. PMID 17075053 DOI: 10.1073/Pnas.0606843103 |
0.539 |
|
| 2006 |
Street TO, Bolen DW, Rose GD. A molecular mechanism for osmolyte-induced protein stability. Proceedings of the National Academy of Sciences of the United States of America. 103: 13997-4002. PMID 16968772 DOI: 10.1073/Pnas.0606236103 |
0.453 |
|
| 2006 |
Fleming PJ, Gong H, Rose GD. Secondary structure determines protein topology. Protein Science : a Publication of the Protein Society. 15: 1829-34. PMID 16823044 DOI: 10.1110/Ps.062305106 |
0.533 |
|
| 2006 |
Street TO, Rose GD, Barrick D. The Role of Introns in Repeat Protein Gene Formation Journal of Molecular Biology. 360: 258-266. PMID 16781737 DOI: 10.1016/J.Jmb.2006.05.024 |
0.361 |
|
| 2006 |
Rose GD. Lifting the lid on helix-capping. Nature Chemical Biology. 2: 123-4. PMID 16484999 DOI: 10.1038/Nchembio0306-123 |
0.433 |
|
| 2006 |
Street TO, Bolen DW, Rose GD. Erratum: A molecular mechanism for osmolyte-induced protein stability (Proceedings of the National Academy of Sciences of the United States of America (September 19, 2006) 38, 103 (13997-14002) DOI 10.1073/pnas.0606236103) Proceedings of the National Academy of Sciences of the United States of America. 103. DOI: 10.1073/Pnas.0608836103 |
0.351 |
|
| 2005 |
Panasik N, Fleming PJ, Rose GD. Hydrogen-bonded turns in proteins: the case for a recount. Protein Science : a Publication of the Protein Society. 14: 2910-4. PMID 16251367 DOI: 10.1110/Ps.051625305 |
0.421 |
|
| 2005 |
Gong H, Fleming PJ, Rose GD. Building native protein conformation from highly approximate backbone torsion angles. Proceedings of the National Academy of Sciences of the United States of America. 102: 16227-32. PMID 16251268 DOI: 10.1073/Pnas.0508415102 |
0.511 |
|
| 2005 |
Fitzkee NC, Rose GD. Sterics and solvation winnow accessible conformational space for unfolded proteins. Journal of Molecular Biology. 353: 873-87. PMID 16185713 DOI: 10.1016/J.Jmb.2005.08.062 |
0.474 |
|
| 2005 |
Gong H, Rose GD. Does secondary structure determine tertiary structure in proteins? Proteins. 61: 338-43. PMID 16104021 DOI: 10.1002/Prot.20622 |
0.471 |
|
| 2005 |
Fleming PJ, Rose GD. Do all backbone polar groups in proteins form hydrogen bonds? Protein Science : a Publication of the Protein Society. 14: 1911-7. PMID 15937286 DOI: 10.1110/Ps.051454805 |
0.397 |
|
| 2005 |
Fitzkee NC, Fleming PJ, Gong H, Panasik N, Street TO, Rose GD. Are proteins made from a limited parts list? Trends in Biochemical Sciences. 30: 73-80. PMID 15691652 DOI: 10.1016/J.Tibs.2004.12.005 |
0.419 |
|
| 2005 |
Fitzkee NC, Fleming PJ, Rose GD. The Protein Coil Library: a structural database of nonhelix, nonstrand fragments derived from the PDB. Proteins. 58: 852-4. PMID 15657933 DOI: 10.1002/Prot.20394 |
0.489 |
|
| 2005 |
Fleming PJ, Fitzkee NC, Mezei M, Srinivasan R, Rose GD. A novel method reveals that solvent water favors polyproline II over beta-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA). Protein Science : a Publication of the Protein Society. 14: 111-8. PMID 15576559 DOI: 10.1110/Ps.041047005 |
0.438 |
|
| 2004 |
Fitzkee NC, Rose GD. Reassessing random-coil statistics in unfolded proteins. Proceedings of the National Academy of Sciences of the United States of America. 101: 12497-502. PMID 15314216 DOI: 10.1073/Pnas.0404236101 |
0.508 |
|
| 2004 |
Mezei M, Fleming PJ, Srinivasan R, Rose GD. Polyproline II helix is the preferred conformation for unfolded polyalanine in water. Proteins. 55: 502-7. PMID 15103614 DOI: 10.1002/Prot.20050 |
0.367 |
|
| 2004 |
Srinivasan R, Fleming PJ, Rose GD. Ab initio protein folding using LINUS. Methods in Enzymology. 383: 48-66. PMID 15063646 DOI: 10.1016/S0076-6879(04)83003-9 |
0.548 |
|
| 2004 |
Fitzkee NC, Rose GD. Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand. Protein Science : a Publication of the Protein Society. 13: 633-9. PMID 14767081 DOI: 10.1110/Ps.03503304 |
0.461 |
|
| 2003 |
Gong H, Isom DG, Srinivasan R, Rose GD. Local secondary structure content predicts folding rates for simple, two-state proteins. Journal of Molecular Biology. 327: 1149-54. PMID 12662937 DOI: 10.1016/S0022-2836(03)00211-0 |
0.453 |
|
| 2003 |
Murthy VL, Rose GD. RNABase: an annotated database of RNA structures. Nucleic Acids Research. 31: 502-4. PMID 12520063 DOI: 10.1093/Nar/Gkg012 |
0.388 |
|
| 2002 |
Srinivasan R, Rose GD. Methinks it is like a folding curve. Biophysical Chemistry. 101: 167-71. PMID 12487998 DOI: 10.1016/S0301-4622(02)00147-3 |
0.452 |
|
| 2002 |
Rose GD. Getting to know u. Advances in Protein Chemistry. 62: xv-xxi. PMID 12418098 DOI: 10.1016/S0065-3233(02)62001-7 |
0.449 |
|
| 2002 |
Pappu RV, Rose GD. A simple model for polyproline II structure in unfolded states of alanine-based peptides. Protein Science : a Publication of the Protein Society. 11: 2437-55. PMID 12237465 DOI: 10.1110/Ps.0217402 |
0.618 |
|
| 2002 |
Zhu Y, Xu G, Patel A, McLaughlin MM, Silverman C, Knecht KA, Sweitzer S, Li X, McDonnell P, Mirabile R, Zimmerman D, Boyce R, Tierney LA, Hu E, Livi GP, ... ... Rose GD, et al. Cloning, expression, and initial characterization of a novel cytokine-like gene family Genomics. 80: 144-150. PMID 12160727 DOI: 10.1006/Geno.2002.6816 |
0.329 |
|
| 2002 |
Shi Z, Olson CA, Rose GD, Baldwin RL, Kallenbach NR. Polyproline II structure in a sequence of seven alanine residues. Proceedings of the National Academy of Sciences of the United States of America. 99: 9190-5. PMID 12091708 DOI: 10.1073/Pnas.112193999 |
0.464 |
|
| 2002 |
Srinivasan R, Rose GD. Ab initio prediction of protein structure using LINUS. Proteins. 47: 489-95. PMID 12001227 DOI: 10.1002/Prot.10103 |
0.392 |
|
| 2002 |
Przytycka T, Srinivasan R, Rose GD. Recursive domains in proteins. Protein Science : a Publication of the Protein Society. 11: 409-17. PMID 11790851 DOI: 10.1110/Ps.24701 |
0.443 |
|
| 2000 |
Murthy VL, Rose GD. Is counterion delocalization responsible for collapse in RNA folding Biochemistry. 39: 14365-14370. PMID 11087388 DOI: 10.1021/Bi001820R |
0.349 |
|
| 2000 |
Pappu RV, Srinivasan R, Rose GD. The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding Proceedings of the National Academy of Sciences of the United States of America. 97: 12565-12570. PMID 11070081 DOI: 10.1073/Pnas.97.23.12565 |
0.636 |
|
| 1999 |
Srinivasan R, Rose GD. A physical basis for protein secondary structure Proceedings of the National Academy of Sciences of the United States of America. 96: 14258-14263. PMID 10588693 DOI: 10.1073/Pnas.96.25.14258 |
0.507 |
|
| 1999 |
Murthy VL, Srinivasan R, Draper DE, Rose GD. A complete conformational map for RNA. Journal of Molecular Biology. 291: 313-27. PMID 10438623 DOI: 10.1006/Jmbi.1999.2958 |
0.327 |
|
| 1999 |
Xu H, Aurora R, Rose GD, White RH. Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Nature Structural Biology. 6: 750-4. PMID 10426953 DOI: 10.1038/11525 |
0.399 |
|
| 1999 |
Przytycka T, Aurora R, Rose GD. A protein taxonomy based on secondary structure. Nature Structural Biology. 6: 672-82. PMID 10404226 DOI: 10.1038/10728 |
0.485 |
|
| 1999 |
Baldwin RL, Rose GD. Is protein folding hierarchic? II. Folding intermediates and transition states Trends in Biochemical Sciences. 24: 77-83. PMID 10098403 DOI: 10.1016/S0968-0004(98)01345-0 |
0.473 |
|
| 1999 |
Baldwin RL, Rose GD. Is protein folding hierarchic? I. Local structure and peptide folding Trends in Biochemical Sciences. 24: 26-33. PMID 10087919 DOI: 10.1016/S0968-0004(98)01346-2 |
0.499 |
|
| 1998 |
Aurora R, Rose GD. Seeking an ancient enzyme in Methanococcus jannaschii using ORF, a program based on predicted secondary structure comparisons. Proceedings of the National Academy of Sciences of the United States of America. 95: 2818-23. PMID 9501173 DOI: 10.1073/Pnas.95.6.2818 |
0.381 |
|
| 1997 |
Rose GD. Protein folding and the Paracelsus challenge Nature Structural & Molecular Biology. 4: 512-514. PMID 9228938 DOI: 10.1038/Nsb0797-512 |
0.447 |
|
| 1997 |
Creamer TP, Srinivasan R, Rose GD. Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility. Biochemistry. 36: 2832-5. PMID 9062111 DOI: 10.1021/Bi962819O |
0.409 |
|
| 1997 |
Aurora R, Creamer TP, Srinivasan R, Rose GD. Local interactions in protein folding: lessons from the alpha-helix. The Journal of Biological Chemistry. 272: 1413-6. PMID 9019474 DOI: 10.1074/Jbc.272.3.1413 |
0.396 |
|
| 1996 |
Creamer TP, Srinivasan R, Rose GD. Modeling unfolded states of peptides and proteins. Biochemistry. 34: 16245-50. PMID 8845348 DOI: 10.1021/Bi00050A003 |
0.493 |
|
| 1996 |
Creamer TP, Rose GD. Simple force field for study of peptide and protein conformational properties. Methods in Enzymology. 259: 576-89. PMID 8538473 DOI: 10.1016/0076-6879(95)59062-5 |
0.439 |
|
| 1995 |
Nichols WL, Rose GD, Ten Eyck LF, Zimm BH. Rigid domains in proteins: an algorithmic approach to their identification. Proteins. 23: 38-48. PMID 8539249 DOI: 10.1002/Prot.340230106 |
0.472 |
|
| 1995 |
Creamer TP, Rose GD. Interactions between hydrophobic side chains within alpha-helices. Protein Science : a Publication of the Protein Society. 4: 1305-14. PMID 7670373 DOI: 10.1002/Pro.5560040706 |
0.407 |
|
| 1995 |
Srinivasan R, Rose GD. Linus: A Hierarchic Procedure To Predict The Fold Of A Protein Proteins. 22: 81-99. PMID 7567969 DOI: 10.1002/Prot.340220202 |
0.479 |
|
| 1995 |
Creamer TP, Srinivasan R, Rose GD. Evaluation of interactions between residues in α-helices by exhaustive conformational search Techniques in Protein Chemistry. 6: 443-450. DOI: 10.1016/S1080-8914(06)80054-2 |
0.458 |
|
| 1994 |
Aurora R, Srinivasan R, Rose GD. Rules for alpha-helix termination by glycine. Science (New York, N.Y.). 264: 1126-30. PMID 8178170 DOI: 10.1126/Science.8178170 |
0.482 |
|
| 1994 |
Creamer TP, Rose GD. Alpha-helix-forming propensities in peptides and proteins. Proteins. 19: 85-97. PMID 8090712 DOI: 10.1002/Prot.340190202 |
0.439 |
|
| 1994 |
Rose GD, Creamer TP. Protein folding: predicting predicting. Proteins. 19: 1-3. PMID 8066081 DOI: 10.1002/Prot.340190102 |
0.351 |
|
| 1994 |
Seale JW, Srinivasan R, Rose GD. Sequence determinants of the capping box, a stabilizing motif at the N‐termini of α‐helices Protein Science. 3: 1741-1745. PMID 7849592 DOI: 10.1002/Pro.5560031014 |
0.412 |
|
| 1994 |
Lin L, Pinker RJ, Forde K, Rose GD, Kallenbach NR. Molten globular characteristics of the native state of apomyoglobin. Nature Structural Biology. 1: 447-52. PMID 7664063 DOI: 10.1038/Nsb0794-447 |
0.392 |
|
| 1993 |
Lattman EE, Rose GD. Protein folding - What's the question? Proceedings of the National Academy of Sciences of the United States of America. 90: 439-441. PMID 8421673 DOI: 10.1073/Pnas.90.2.439 |
0.447 |
|
| 1993 |
Pinker RJ, Lin L, Rose GD, Kallenbach NR. Effects of alanine substitutions in alpha-helices of sperm whale myoglobin on protein stability. Protein Science : a Publication of the Protein Society. 2: 1099-105. PMID 8358293 DOI: 10.1002/Pro.5560020704 |
0.404 |
|
| 1993 |
Rose GD, Wolfenden R. Hydrogen bonding, hydrophobicity, packing, and protein folding Annual Review of Biophysics and Biomolecular Structure. 22: 381-415. PMID 8347995 DOI: 10.1146/Annurev.Bb.22.060193.002121 |
0.433 |
|
| 1993 |
Harper ET, Rose GD. Helix stop signals in proteins and peptides: the capping box. Biochemistry. 32: 7605-7609. PMID 8347570 DOI: 10.1021/Bi00081A001 |
0.432 |
|
| 1993 |
Pinker RJ, Kallenbach NR, Rose GD. Effect of alanine substitutions in alpha helices of sperm whale myoglobin on stability of the native protein Protein Engineering Design & Selection. 6. DOI: 10.1093/Protein/6.Supplement.21-B |
0.385 |
|
| 1992 |
Creamer TP, Rose GD. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proceedings of the National Academy of Sciences of the United States of America. 89: 5937-41. PMID 1631077 DOI: 10.1073/Pnas.89.13.5937 |
0.391 |
|
| 1992 |
Stickle DF, Presta LG, Dill KA, Rose GD. Hydrogen bonding in globular proteins. Journal of Molecular Biology. 226: 1143-59. PMID 1518048 DOI: 10.1016/0022-2836(92)91058-W |
0.379 |
|
| 1991 |
Behe MJ, Lattman EE, Rose GD. The protein-folding problem: The native fold determines packing, but does packing determine the native fold? Proceedings of the National Academy of Sciences of the United States of America. 88: 4195-4199. PMID 2034665 DOI: 10.1073/Pnas.88.10.4195 |
0.518 |
|
| 1990 |
Lesser GJ, Rose GD. Hydrophobicity of amino acid subgroups in proteins. Proteins. 8: 6-13. PMID 2217164 DOI: 10.1002/Prot.340080104 |
0.388 |
|
| 1988 |
Presta LG, Rose GD. Helix signals in proteins Science. 240: 1632-1641. PMID 2837824 DOI: 10.1126/Science.2837824 |
0.462 |
|
| 1988 |
Fetrow JS, Zehfus MH, Rose GD. Protein Folding: New Twists Nature Biotechnology. 6: 167-171. DOI: 10.1038/Nbt0288-167 |
0.481 |
|
| 1987 |
Rose GD. Protein hydrophobicity: is it the sum of its parts? Proteins. 2: 79-80. PMID 3447174 DOI: 10.1002/Prot.340020202 |
0.464 |
|
| 1986 |
Zehfus MH, Rose GD. Compact units in proteins Biochemistry. 25: 5759-5765. PMID 3778881 DOI: 10.1021/Bi00367A062 |
0.446 |
|
| 1986 |
Leszczynski JF, Rose GD. Loops in globular proteins: a novel category of secondary structure. Science (New York, N.Y.). 234: 849-55. PMID 3775366 DOI: 10.1126/Science.3775366 |
0.514 |
|
| 1986 |
Fanning DW, Smith JA, Rose GD. Molecular cartography of globular proteins with application to antigenic sites. Biopolymers. 25: 863-883. PMID 2424521 DOI: 10.1002/Bip.360250509 |
0.357 |
|
| 1985 |
Lee RH, Rose GD. Molecular recognition. I. Automatic identification of topographic surface features. Biopolymers. 24: 1613-27. PMID 4041553 DOI: 10.1002/Bip.360240814 |
0.318 |
|
| 1985 |
Rose GD, Geselowitz AR, Lesser GJ, Lee RH, Zehfus MH. Hydrophobicity of amino acid residues in globular proteins. Science (New York, N.Y.). 229: 834-8. PMID 4023714 DOI: 10.1126/Science.4023714 |
0.507 |
|
| 1985 |
Zehfus MH, Seltzer JP, Rose GD. Fast approximations for accessible surface area and molecular volume of protein segments Biopolymers. 24: 2511-2519. PMID 3841497 DOI: 10.1002/Bip.360241222 |
0.334 |
|
| 1985 |
Rose GD. Automatic recognition of domains in globular proteins. Methods in Enzymology. 115: 430-440. PMID 3841184 DOI: 10.1016/0076-6879(85)15031-7 |
0.425 |
|
| 1985 |
Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins Advances in Protein Chemistry. 37: 1-109. PMID 2865874 DOI: 10.1016/S0065-3233(08)60063-7 |
0.455 |
|
| 1983 |
Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins Nature. 304: 654-657. PMID 6877386 DOI: 10.1038/304654A0 |
0.531 |
|
| 1981 |
Lesk AM, Rose GD. Folding units in globular proteins Proceedings of the National Academy of Sciences of the United States of America. 78: 4304-4308. PMID 6945585 DOI: 10.1073/Pnas.78.7.4304 |
0.483 |
|
| 1980 |
Rose GD. A hierarchic model for the self-assembly of globular proteins. Biophysical Journal. 32: 419-422. PMID 19431377 DOI: 10.1016/S0006-3495(80)84965-4 |
0.405 |
|
| 1980 |
Rose GD, Roy S. Hydrophobic basis of packing in globular proteins Proceedings of the National Academy of Sciences of the United States of America. 77: 4643-4647. PMID 6933513 DOI: 10.1073/Pnas.77.8.4643 |
0.511 |
|
| 1979 |
Rose GD. Hierarchic organization of domains in globular proteins Journal of Molecular Biology. 134: 447-470. PMID 537072 DOI: 10.1016/0022-2836(79)90363-2 |
0.406 |
|
| 1978 |
Rose GD. Prediction of chain turns in globular proteins on a hydrophobic basis. Nature. 272: 586-590. PMID 643051 DOI: 10.1038/272586A0 |
0.489 |
|
| 1977 |
Rose GD, Wetlaufer DB. The number of turns in globular proteins Nature. 268: 769-770. PMID 895883 DOI: 10.1038/268769A0 |
0.443 |
|
| 1977 |
Rose GD, Seltzer JP. A new algorithm for finding the peptide chain turns in a globular protein Journal of Molecular Biology. 113: 153-164. PMID 881732 DOI: 10.1016/0022-2836(77)90046-8 |
0.454 |
|
| 1976 |
Rose GD, Winters RH, Wetlaufer DB. A testable model for protein folding. Febs Letters. 63: 10-16. PMID 1261670 DOI: 10.1016/0014-5793(76)80184-6 |
0.445 |
|
| 1976 |
Wetlaufer DB, Rose GD, Taaffe L. Orientation of structural segments in globular proteins. Biochemistry. 15: 5154-5157. PMID 990271 DOI: 10.1021/Bi00668A031 |
0.439 |
|
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