George D. Rose - Publications

Affiliations: 
1976 Biochemistry and Biophysics Oregon State University, Corvallis, OR 

100 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  1
2021 Rose GD. Protein folding - seeing is deceiving. Protein Science : a Publication of the Protein Society. PMID 33938055 DOI: 10.1002/pro.4096  0.01
2019 Rose GD. Ramachandran maps for side chains in globular proteins. Proteins. PMID 30629766 DOI: 10.1002/Prot.25656  0.01
2018 Rose GD. What is life? Part II. Proteins. PMID 30576005 DOI: 10.1002/Prot.25649  0.01
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  1
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  1
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  1
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  1
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  1
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  1
2012 Itzhaki LS, Rose GD. Folding and binding: lingering questions, emerging answers. Current Opinion in Structural Biology. 22: 1-3. PMID 22265341 DOI: 10.1016/J.Sbi.2012.01.001  0.01
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  0.04
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  1
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  1
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  1
2011 Perskie LL, Rose GD. Negative Design in Protein Coils Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.3035  1
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  1
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  1
2009 Rose GD. In Memoriam: Frederic M. Richards (1925-2009). Proteins. 75: 535-9. PMID 19226638 DOI: 10.1002/Prot.22400  0.01
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  0.01
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2006 Rose GD. Lifting the lid on helix-capping. Nature Chemical Biology. 2: 123-4. PMID 16484999 DOI: 10.1038/Nchembio0306-123  0.01
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  1
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  1
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  1
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  1
2005 Gong H, Rose GD. Does secondary structure determine tertiary structure in proteins? Proteins. 61: 338-43. PMID 16104021 DOI: 10.1002/Prot.20622  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2003 Sung NS, Gordon JI, Rose GD, Getzoff ED, Kron SJ, Mumford D, Onuchic JN, Scherer NF, Sumners DL, Kopell NJ. Science education. Educating future scientists. Science (New York, N.Y.). 301: 1485. PMID 12970550 DOI: 10.1126/Science.1086133  1
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  1
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  1
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  1
2002 Rose GD. Getting to know u. Advances in Protein Chemistry. 62: xv-xxi. PMID 12418098 DOI: 10.1016/S0065-3233(02)62001-7  0.01
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  1
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  1
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  1
2002 Srinivasan R, Rose GD. Ab initio prediction of protein structure using LINUS. Proteins. 47: 489-95. PMID 12001227 DOI: 10.1002/Prot.10103  1
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  1
2000 Murthy VL, Rose GD. Is counterion delocalization responsible for collapse in RNA folding Biochemistry. 39: 14365-14370. PMID 11087388 DOI: 10.1021/Bi001820R  1
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  1
2000 Rose GD. Lysozyme among the Lilliputians Proceedings of the National Academy of Sciences of the United States of America. 97: 526-528. PMID 10639110 DOI: 10.1073/Pnas.97.2.526  0.01
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  1
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  1
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  0.04
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  1
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  1
1997 Rose GD. Protein folding and the Paracelsus challenge Nature Structural & Molecular Biology. 4: 512-514. PMID 9228938 DOI: 10.1038/Nsb0797-512  0.01
1996 Rose GD. No Assembly Required Sciences-New York. 36: 26-31. DOI: 10.1002/J.2326-1951.1996.Tb03226.X  0.01
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  1
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  1
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  1
1994 Srinivasan R, Rose GD. The T-to-R transformation in hemoglobin: a reevaluation Proceedings of the National Academy of Sciences of the United States of America. 91: 11113-11117. PMID 7972019 DOI: 10.1073/Pnas.91.23.11113  1
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  1
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  1
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  1
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  1
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  1
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  0.01
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  1
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  1
1990 Lesser GJ, Rose GD. Hydrophobicity of amino acid subgroups in proteins. Proteins. 8: 6-13. PMID 2217164 DOI: 10.1002/Prot.340080104  1
1988 Presta LG, Rose GD. Helix signals in proteins Science. 240: 1632-1641. PMID 2837824 DOI: 10.1126/Science.2837824  0.01
1988 Rose GD. Response:Crystallographic Citations Science. 242: 347-347. DOI: 10.1126/Science.242.4877.347-A  0.01
1987 Rose GD. Protein hydrophobicity: is it the sum of its parts? Proteins. 2: 79-80. PMID 3447174 DOI: 10.1002/Prot.340020202  0.01
1987 Smith JA, Rose GD. Immune recognition of proteins: conclusions, dilemmas and enigmas. Bioessays. 6: 112-116. PMID 2437903 DOI: 10.1002/Bies.950060305  1
1986 Rose GD, Lee RH. Molecular recognition in macromolecules. Biophysical Journal. 49: 83-5. PMID 19431660 DOI: 10.1016/S0006-3495(86)83603-7  1
1986 Zehfus MH, Rose GD. Compact units in proteins Biochemistry. 25: 5759-5765. PMID 3778881 DOI: 10.1021/Bi00367A062  1
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  1
1986 Novotný J, Handschumacher M, Haber E, Bruccoleri RE, Carlson WB, Fanning DW, Smith JA, Rose GD. Antigenic determinants in proteins coincide with surface regions accessible to large probes (antibody domains). Proceedings of the National Academy of Sciences of the United States of America. 83: 226-30. PMID 2417241 DOI: 10.1073/Pnas.83.2.226  1
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  1
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  1
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  1
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  0.01
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  1
1983 Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins Nature. 304: 654-657. PMID 6877386 DOI: 10.1038/304654A0  1
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  1
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  0.01
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  1
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  0.01
1978 Rose GD. Prediction of chain turns in globular proteins on a hydrophobic basis. Nature. 272: 586-590. PMID 643051 DOI: 10.1038/272586A0  0.01
1977 Rose GD, Wetlaufer DB. The number of turns in globular proteins Nature. 268: 769-770. PMID 895883 DOI: 10.1038/268769A0  0.01
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  0.01
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  0.01
1976 Wetlaufer DB, Rose GD, Taaffe L. Orientation of structural segments in globular proteins. Biochemistry. 15: 5154-5157. PMID 990271 DOI: 10.1021/Bi00668A031  0.01
1975 Goldberg D, Saliterman S, Wetlaufer DB, Rose G, Hopkins TE. Minimization of construction errors in bent-wire protein models. Biopolymers. 14: 633-640. PMID 1174683 DOI: 10.1002/Bip.1975.360140315  0.01
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