| Year |
Citation |
Score |
| 2020 |
Wang MS, Hecht MH. A Completely ATPase from Combinatorial Protein Design. Journal of the American Chemical Society. 142: 15230-15234. PMID 32833456 DOI: 10.1021/Jacs.0C02954 |
0.413 |
|
| 2020 |
Mancini JA, Pike DH, Tyryshkin AM, Haramaty L, Wang M, Poudel S, Hecht M, Nanda V. Design of a Fe S Cluster into the Core of a De Novo 4-Helix Bundle. Biotechnology and Applied Biochemistry. PMID 32770861 DOI: 10.1002/Bab.2003 |
0.401 |
|
| 2020 |
Zarzhitsky S, Jiang A, Stanley E, Hecht M. Harnessing Synthetic Biology to Enhance Heterologous Protein Expression. Protein Science : a Publication of the Protein Society. PMID 32567134 DOI: 10.1002/Pro.3907 |
0.427 |
|
| 2020 |
Karas C, Hecht M. A Strategy for Combinatorial Cavity Design in De Novo Proteins. Life (Basel, Switzerland). 10. PMID 31979320 DOI: 10.3390/Life10020009 |
0.514 |
|
| 2020 |
Kimura N, Mochizuki K, Umezawa K, Hecht MH, Arai R. Hyperstable Protein with a Dimeric Bisecting Topology. Acs Synthetic Biology. PMID 31951376 DOI: 10.1021/Acssynbio.9B00501 |
0.409 |
|
| 2019 |
Wang MS, Hoegler KJ, Hecht MH. Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals. Life (Basel, Switzerland). 9. PMID 30634485 DOI: 10.3390/Life9010008 |
0.781 |
|
| 2018 |
Kobayashi N, Inano K, Sasahara K, Sato T, Miyazawa K, Fukuma T, Hecht MH, Song C, Murata K, Arai R. Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks. Acs Synthetic Biology. PMID 29690759 DOI: 10.1021/Acssynbio.8B00007 |
0.392 |
|
| 2018 |
Hoegler KJ, Hecht MH. Artificial Gene Amplification in Escherichia coli Reveals Numerous Determinants for Resistance to Metal Toxicity. Journal of Molecular Evolution. PMID 29356848 DOI: 10.1007/S00239-018-9830-3 |
0.749 |
|
| 2018 |
Hecht MH, Zarzhitsky S, Karas C, Chari S. Are natural proteins special? Can we do that? Current Opinion in Structural Biology. 48: 124-132. PMID 29306103 DOI: 10.1016/J.Sbi.2017.11.009 |
0.45 |
|
| 2017 |
Digianantonio KM, Korolev M, Hecht MH. A Non-Natural Protein Rescues Cells Deleted for a Key Enzyme in Central Metabolism. Acs Synthetic Biology. PMID 28055179 DOI: 10.1021/Acssynbio.6B00336 |
0.667 |
|
| 2016 |
Digianantonio KM, Hecht MH. A protein constructed de novo enables cell growth by altering gene regulation. Proceedings of the National Academy of Sciences of the United States of America. PMID 26884172 DOI: 10.1073/Pnas.1600566113 |
0.438 |
|
| 2016 |
Hoegler KJ, Hecht MH. A De Novo Protein Confers Copper Resistance in Escherichia Coli. Protein Science : a Publication of the Protein Society. PMID 26748884 DOI: 10.1002/Pro.2871 |
0.794 |
|
| 2015 |
Murphy GS, Greisman JB, Hecht MH. De Novo Proteins with Life-Sustaining Functions are Structurally Dynamic. Journal of Molecular Biology. PMID 26707197 DOI: 10.1016/J.Jmb.2015.12.008 |
0.462 |
|
| 2015 |
Kobayashi N, Yasase K, Sato T, Unzai S, Hecht MH, Arai R. Self-Assembling Nano-Architectures Created from a Protein Nano-Building Block Using an Intermolecularly Folded Dimeric De Novo Protein. Journal of the American Chemical Society. PMID 26120734 DOI: 10.1021/Jacs.5B03593 |
0.404 |
|
| 2015 |
Smith BA, Mularz AE, Hecht MH. Divergent evolution of a bifunctional de novo protein. Protein Science : a Publication of the Protein Society. 24: 246-52. PMID 25420677 DOI: 10.1002/Pro.2611 |
0.435 |
|
| 2014 |
McKoy AF, Chen J, Schupbach T, Hecht MH. Structure-activity relationships for a series of compounds that inhibit aggregation of the Alzheimer's peptide, Aβ42. Chemical Biology & Drug Design. 84: 505-12. PMID 24751138 DOI: 10.1111/Cbdd.12341 |
0.761 |
|
| 2012 |
Cherny I, Korolev M, Koehler AN, Hecht MH. Proteins from an unevolved library of de novo designed sequences bind a range of small molecules. Acs Synthetic Biology. 1: 130-8. PMID 23651114 DOI: 10.1021/Sb200018E |
0.693 |
|
| 2012 |
McKoy AF, Chen J, Schupbach T, Hecht MH. A novel inhibitor of amyloid β (Aβ) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimer disease. The Journal of Biological Chemistry. 287: 38992-9000. PMID 22992731 DOI: 10.1074/Jbc.M112.348037 |
0.761 |
|
| 2012 |
Patel SC, Hecht MH. Directed evolution of the peroxidase activity of a de novo-designed protein. Protein Engineering, Design & Selection : Peds. 25: 445-52. PMID 22665824 DOI: 10.1093/Protein/Gzs025 |
0.684 |
|
| 2012 |
Arai R, Kobayashi N, Kimura A, Sato T, Matsuo K, Wang AF, Platt JM, Bradley LH, Hecht MH. Domain-swapped dimeric structure of a stable and functional de novo four-helix bundle protein, WA20. The Journal of Physical Chemistry. B. 116: 6789-97. PMID 22397676 DOI: 10.1021/Jp212438H |
0.772 |
|
| 2011 |
Armstrong AH, Chen J, McKoy AF, Hecht MH. Mutations that replace aromatic side chains promote aggregation of the Alzheimer's Aβ peptide. Biochemistry. 50: 4058-67. PMID 21513285 DOI: 10.1021/Bi200268W |
0.762 |
|
| 2011 |
Smith BA, Hecht MH. Novel proteins: from fold to function. Current Opinion in Chemical Biology. 15: 421-6. PMID 21474363 DOI: 10.1016/J.Cbpa.2011.03.006 |
0.432 |
|
| 2011 |
Das A, Wei Y, Pelczer I, Hecht MH. Binding of small molecules to cavity forming mutants of a de novo designed protein. Protein Science : a Publication of the Protein Society. 20: 702-11. PMID 21328630 DOI: 10.1002/Pro.601 |
0.687 |
|
| 2011 |
Fisher MA, McKinley KL, Bradley LH, Viola SR, Hecht MH. De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth. Plos One. 6: e15364. PMID 21245923 DOI: 10.1371/Journal.Pone.0015364 |
0.752 |
|
| 2011 |
Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell. 144: 67-78. PMID 21215370 DOI: 10.1016/J.Cell.2010.11.050 |
0.48 |
|
| 2011 |
McKoy A, Hecht M. P2-481: A high throughput screen identifies compounds that inhibit Alzheimer's peptide aggregation and reduce toxicity in vitro and in drosophila melanogaster Alzheimer's & Dementia. 7: S466-S466. DOI: 10.1016/j.jalz.2011.05.1352 |
0.792 |
|
| 2010 |
Chen J, Armstrong AH, Koehler AN, Hecht MH. Small molecule microarrays enable the discovery of compounds that bind the Alzheimer's Aβ peptide and reduce its cytotoxicity. Journal of the American Chemical Society. 132: 17015-22. PMID 21062056 DOI: 10.1021/Ja107552S |
0.796 |
|
| 2010 |
McKoy AF, Hecht M. P3-270: A high throughput screen identifies compounds that inhibit Abeta peptide aggregation and reduce Abeta toxicity in vitro
and in drosophila melanogaster Alzheimer's & Dementia. 6: S531-S531. DOI: 10.1016/J.Jalz.2010.05.1770 |
0.785 |
|
| 2009 |
Patel SC, Bradley LH, Jinadasa SP, Hecht MH. Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins. Protein Science : a Publication of the Protein Society. 18: 1388-400. PMID 19544578 DOI: 10.1002/Pro.147 |
0.817 |
|
| 2008 |
Go A, Kim S, Baum J, Hecht MH. Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles. Protein Science : a Publication of the Protein Society. 17: 821-32. PMID 18436954 DOI: 10.1110/Ps.073377908 |
0.77 |
|
| 2008 |
Kim W, Hecht MH. Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide. Journal of Molecular Biology. 377: 565-74. PMID 18258258 DOI: 10.1016/J.Jmb.2007.12.079 |
0.576 |
|
| 2008 |
Hecht M. S1-02-04: Aggregation of Abeta: Molecular underpinnings and the search for novel inhibitors Alzheimer's & Dementia. 4: T102-T102. DOI: 10.1016/J.Jalz.2008.05.193 |
0.363 |
|
| 2007 |
Go A, Kim S, Hecht M, Baum J. NMR assignment of S836: A de novo protein from a designed superfamily Biomolecular Nmr Assignments. 1: 213-215. PMID 19636868 DOI: 10.1007/S12104-007-9059-3 |
0.761 |
|
| 2007 |
Das A, Hecht MH. Peroxidase activity of de novo heme proteins immobilized on electrodes. Journal of Inorganic Biochemistry. 101: 1820-6. PMID 17765314 DOI: 10.1016/J.Jinorgbio.2007.07.024 |
0.583 |
|
| 2007 |
Bradley LH, Wei Y, Thumfort P, Wurth C, Hecht MH. Protein design by binary patterning of polar and nonpolar amino acids. Methods in Molecular Biology (Clifton, N.J.). 352: 155-66. PMID 17041264 DOI: 10.1385/1-59745-187-8:155 |
0.788 |
|
| 2006 |
Kim W, Kim Y, Min J, Kim DJ, Chang YT, Hecht MH. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. Acs Chemical Biology. 1: 461-9. PMID 17168524 DOI: 10.1021/Cb600135W |
0.591 |
|
| 2006 |
Kim W, Hecht MH. Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide. Proceedings of the National Academy of Sciences of the United States of America. 103: 15824-9. PMID 17038501 DOI: 10.1073/Pnas.0605629103 |
0.586 |
|
| 2006 |
Bradley LH, Thumfort PP, Hecht MH. De novo proteins from binary-patterned combinatorial libraries. Methods in Molecular Biology (Clifton, N.J.). 340: 53-69. PMID 16957332 DOI: 10.1385/1-59745-116-9:53 |
0.769 |
|
| 2006 |
Das A, Trammell SA, Hecht MH. Electrochemical and ligand binding studies of a de novo heme protein. Biophysical Chemistry. 123: 102-12. PMID 16730114 DOI: 10.1016/J.Bpc.2006.04.011 |
0.567 |
|
| 2006 |
Wurth C, Kim W, Hecht MH. Combinatorial approaches to probe the sequence determinants of protein aggregation and amyloidogenicity. Protein and Peptide Letters. 13: 279-86. PMID 16515456 DOI: 10.2174/092986606775338506 |
0.637 |
|
| 2005 |
Hu Y, Das A, Hecht MH, Scoles G. Nanografting de novo proteins onto gold surfaces. Langmuir : the Acs Journal of Surfaces and Colloids. 21: 9103-9. PMID 16171339 DOI: 10.1021/La046857H |
0.566 |
|
| 2005 |
Kim W, Hecht MH. Sequence determinants of enhanced amyloidogenicity of Alzheimer A{beta}42 peptide relative to A{beta}40. The Journal of Biological Chemistry. 280: 35069-76. PMID 16079141 DOI: 10.1074/Jbc.M505763200 |
0.567 |
|
| 2005 |
Bradley LH, Kleiner RE, Wang AF, Hecht MH, Wood DW. An intein-based genetic selection allows the construction of a high-quality library of binary patterned de novo protein sequences. Protein Engineering, Design & Selection : Peds. 18: 201-7. PMID 15849217 DOI: 10.1093/Protein/Gzi020 |
0.757 |
|
| 2005 |
Klepeis JL, Wei Y, Hecht MH, Floudas CA. Ab initio prediction of the three-dimensional structure of a de novo designed protein: a double-blind case study. Proteins. 58: 560-70. PMID 15609306 DOI: 10.1002/Prot.20338 |
0.591 |
|
| 2004 |
Hecht MH, Das A, Go A, Bradley LH, Wei Y. De novo proteins from designed combinatorial libraries. Protein Science : a Publication of the Protein Society. 13: 1711-23. PMID 15215517 DOI: 10.1110/Ps.04690804 |
0.822 |
|
| 2004 |
Wei Y, Hecht MH. Enzyme-like proteins from an unselected library of designed amino acid sequences. Protein Engineering, Design & Selection : Peds. 17: 67-75. PMID 14985539 DOI: 10.1093/Protein/Gzh007 |
0.635 |
|
| 2003 |
Wei Y, Kim S, Fela D, Baum J, Hecht MH. Solution structure of a de novo protein from a designed combinatorial library. Proceedings of the National Academy of Sciences of the United States of America. 100: 13270-3. PMID 14593201 DOI: 10.1073/Pnas.1835644100 |
0.632 |
|
| 2003 |
Wei Y, Fela D, Kim S, Hecht M, Baum J. 1H, 13C and 15N resonance assignments of S-824, a de novo four-helix bundle from a designed combinatorial library. Journal of Biomolecular Nmr. 27: 395-6. PMID 14512738 DOI: 10.1023/A:1025842221022 |
0.471 |
|
| 2003 |
Moffet DA, Foley J, Hecht MH. Midpoint reduction potentials and heme binding stoichiometries of de novo proteins from designed combinatorial libraries. Biophysical Chemistry. 105: 231-9. PMID 14499895 DOI: 10.1016/S0301-4622(03)00072-3 |
0.798 |
|
| 2003 |
Wei Y, Liu T, Sazinsky SL, Moffet DA, Pelczer I, Hecht MH. Stably folded de novo proteins from a designed combinatorial library. Protein Science : a Publication of the Protein Society. 12: 92-102. PMID 12493832 DOI: 10.1110/Ps.0228003 |
0.823 |
|
| 2002 |
Wurth C, Guimard NK, Hecht MH. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. Journal of Molecular Biology. 319: 1279-90. PMID 12079364 DOI: 10.1016/S0022-2836(02)00399-6 |
0.425 |
|
| 2002 |
Brown CL, Aksay IA, Saville DA, Hecht MH. Template-directed assembly of a de novo designed protein. Journal of the American Chemical Society. 124: 6846-8. PMID 12059204 DOI: 10.1021/Ja0261271 |
0.425 |
|
| 2002 |
Wu Q, Li F, Wang W, Hecht MH, Spiro TG. UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin. Journal of Inorganic Biochemistry. 88: 381-7. PMID 11897354 DOI: 10.1016/S0162-0134(01)00354-3 |
0.687 |
|
| 2002 |
Wang W, Hecht MH. Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proceedings of the National Academy of Sciences of the United States of America. 99: 2760-5. PMID 11880628 DOI: 10.1073/Pnas.052706199 |
0.753 |
|
| 2001 |
Moffet DA, Hecht MH. De novo proteins from combinatorial libraries. Chemical Reviews. 101: 3191-203. PMID 11710068 DOI: 10.1021/Cr000051E |
0.787 |
|
| 2001 |
Moffet DA, Case MA, House JC, Vogel K, Williams RD, Spiro TG, McLendon GL, Hecht MH. Carbon monoxide binding by de novo heme proteins derived from designed combinatorial libraries. Journal of the American Chemical Society. 123: 2109-15. PMID 11456855 DOI: 10.1021/Ja0036007 |
0.79 |
|
| 2001 |
Xu G, Wang W, Groves JT, Hecht MH. Self-assembled monolayers from a designed combinatorial library of de novo beta-sheet proteins. Proceedings of the National Academy of Sciences of the United States of America. 98: 3652-7. PMID 11274383 DOI: 10.1073/Pnas.071400098 |
0.77 |
|
| 2000 |
Roy S, Hecht MH. Cooperative thermal denaturation of proteins designed by binary patterning of polar and nonpolar amino acids. Biochemistry. 39: 4603-7. PMID 10769115 DOI: 10.1021/Bi992328E |
0.439 |
|
| 2000 |
Broome BM, Hecht MH. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. Journal of Molecular Biology. 296: 961-8. PMID 10686095 DOI: 10.1006/Jmbi.2000.3514 |
0.424 |
|
| 2000 |
Moffet DA, Certain LK, Smith AJ, Kessel AJ, Beckwith KA, Hecht MH. Peroxidase activity in heme proteins derived from a designed combinatorial library [11] Journal of the American Chemical Society. 122: 7612-7613. DOI: 10.1021/Ja001198Q |
0.782 |
|
| 1999 |
West MW, Wang W, Patterson J, Mancias JD, Beasley JR, Hecht MH. De novo amyloid proteins from designed combinatorial libraries. Proceedings of the National Academy of Sciences of the United States of America. 96: 11211-6. PMID 10500156 DOI: 10.1073/Pnas.96.20.11211 |
0.791 |
|
| 1999 |
Dong S, Ybe JA, Hecht MH, Spiro TG. H-bonding maintains the active site of type 1 copper proteins: site-directed mutagenesis of Asn38 in poplar plastocyanin. Biochemistry. 38: 3379-85. PMID 10079082 DOI: 10.1021/Bi981999U |
0.31 |
|
| 1999 |
Rosenbaum DM, Roy S, Hecht MH. Screening combinatorial libraries of de Novo proteins by hydrogen- deuterium exchange and electrospray mass spectrometry Journal of the American Chemical Society. 121: 9509-9513. DOI: 10.1021/Ja991843X |
0.441 |
|
| 1997 |
Rojas NR, Kamtekar S, Simons CT, McLean JE, Vogel KM, Spiro TG, Farid RS, Hecht MH. De novo heme proteins from designed combinatorial libraries. Protein Science : a Publication of the Protein Society. 6: 2512-24. PMID 9416601 DOI: 10.1002/pro.5560061204 |
0.37 |
|
| 1997 |
Nedwidek MN, Hecht MH. Minimized protein structures: a little goes a long way. Proceedings of the National Academy of Sciences of the United States of America. 94: 10010-1. PMID 9294152 DOI: 10.1073/Pnas.94.19.10010 |
0.486 |
|
| 1997 |
Roy S, Helmer KJ, Hecht MH. Detecting native-like properties in combinatorial libraries of de novo proteins. Folding & Design. 2: 89-92. PMID 9135980 DOI: 10.1016/S1359-0278(97)00012-6 |
0.464 |
|
| 1997 |
Beasley JR, Hecht MH. Protein design: the choice of de novo sequences. The Journal of Biological Chemistry. 272: 2031-4. PMID 9036150 DOI: 10.1074/Jbc.272.4.2031 |
0.445 |
|
| 1997 |
Roy S, Ratnaswamy G, Boice JA, Fairman R, McLendon G, Hecht MH. A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties Journal of the American Chemical Society. 119: 5302-5306. DOI: 10.1021/Ja9700717 |
0.461 |
|
| 1996 |
Ybe JA, Hecht MH. Sequence replacements in the central beta-turn of plastocyanin. Protein Science : a Publication of the Protein Society. 5: 814-24. PMID 8732753 DOI: 10.1002/Pro.5560050503 |
0.429 |
|
| 1995 |
West MW, Hecht MH. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Science : a Publication of the Protein Society. 4: 2032-9. PMID 8535239 DOI: 10.1002/Pro.5560041008 |
0.388 |
|
| 1995 |
Kamtekar S, Hecht MH. Protein Motifs. 7. The four-helix bundle: what determines a fold? Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1013-22. PMID 7649401 DOI: 10.1096/Fasebj.9.11.7649401 |
0.447 |
|
| 1995 |
Xiong H, Buckwalter BL, Shieh HM, Hecht MH. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proceedings of the National Academy of Sciences of the United States of America. 92: 6349-53. PMID 7603994 DOI: 10.1073/Pnas.92.14.6349 |
0.4 |
|
| 1994 |
Hecht MH. De novo design of beta-sheet proteins. Proceedings of the National Academy of Sciences of the United States of America. 91: 8729-30. PMID 8090714 DOI: 10.1073/Pnas.91.19.8729 |
0.373 |
|
| 1994 |
Johnson BH, Hecht MH. Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Bio/Technology (Nature Publishing Company). 12: 1357-60. PMID 7765566 DOI: 10.1038/Nbt1294-1357 |
0.385 |
|
| 1993 |
Brunet AP, Huang ES, Huffine ME, Loeb JE, Weltman RJ, Hecht MH. The role of turns in the structure of an alpha-helical protein. Nature. 364: 355-8. PMID 8332196 DOI: 10.1038/364355A0 |
0.394 |
|
| 1993 |
Kamtekar S, Schiffer JM, Xiong H, Babik JM, Hecht MH. Protein design by binary patterning of polar and nonpolar amino acids. Science (New York, N.Y.). 262: 1680-5. PMID 8259512 DOI: 10.1126/Science.8259512 |
0.468 |
|
| 1992 |
Richardson JS, Richardson DC, Tweedy NB, Gernert KM, Quinn TP, Hecht MH, Erickson BW, Yan Y, McClain RD, Donlan ME. Looking at proteins: representations, folding, packing, and design. Biophysical Society National Lecture, 1992. Biophysical Journal. 63: 1185-209. PMID 1477272 |
0.658 |
|
| 1990 |
Hecht MH, Richardson JS, Richardson DC, Ogden RC. De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence. Science (New York, N.Y.). 249: 884-91. PMID 2392678 DOI: 10.1126/Science.2392678 |
0.678 |
|
| 1986 |
Hecht MH, Sturtevant JM, Sauer RT. Stabilization of lambda repressor against thermal denaturation by site-directed Gly----Ala changes in alpha-helix 3. Proteins. 1: 43-6. PMID 3449850 DOI: 10.1002/Prot.340010108 |
0.41 |
|
| 1985 |
Hecht MH, Hehir KM, Nelson HC, Sturtevant JM, Sauer RT. Increasing and decreasing protein stability: effects of revertant substitutions on the thermal denaturation of phage lambda repressor. Journal of Cellular Biochemistry. 29: 217-24. PMID 4077930 DOI: 10.1002/Jcb.240290306 |
0.5 |
|
| 1985 |
Hecht MH, Sauer RT. Phage lambda repressor revertants. Amino acid substitutions that restore activity to mutant proteins. Journal of Molecular Biology. 186: 53-63. PMID 2934554 DOI: 10.1016/0022-2836(85)90256-6 |
0.473 |
|
| 1984 |
Hecht MH, Sturtevant JM, Sauer RT. Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor. Proceedings of the National Academy of Sciences of the United States of America. 81: 5685-9. PMID 6237363 DOI: 10.1073/Pnas.81.18.5685 |
0.435 |
|
| 1983 |
Sauer RT, Nelson HC, Hehir K, Hecht MH, Gimble FS, DeAnda J, Poteete AR. The lambda and P22 phage repressors. Journal of Biomolecular Structure & Dynamics. 1: 1011-22. PMID 6242868 DOI: 10.1080/07391102.1983.10507499 |
0.448 |
|
| 1983 |
Nelson HC, Hecht MH, Sauer RT. Mutations defining the operator-binding sites of bacteriophage lambda repressor. Cold Spring Harbor Symposia On Quantitative Biology. 47: 441-9. PMID 6222865 DOI: 10.1101/Sqb.1983.047.01.052 |
0.43 |
|
| 1983 |
Hecht MH, Nelson HC, Sauer RT. Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding. Proceedings of the National Academy of Sciences of the United States of America. 80: 2676-80. PMID 6221342 DOI: 10.1073/Pnas.80.9.2676 |
0.475 |
|
| 1978 |
Hecht MH, Zweifel BO, Scheraga HA. Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. 17. Threonine Parameters from Random Poly(hydroxylbutylglutamine-co-L-threonine) Macromolecules. 11: 545-551. DOI: 10.1021/ma60063a024 |
0.303 |
|
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