| Year |
Citation |
Score |
| 2022 |
Venturini C, Pang J, Tamuri AU, Roy S, Atkinson C, Griffiths P, Breuer J, Goldstein RA. Haplotype assignment of longitudinal viral deep sequencing data using covariation of variant frequencies. Virus Evolution. 8: veac093. PMID 36478783 DOI: 10.1093/ve/veac093 |
0.726 |
|
| 2020 |
Ruis C, Lindesmith LC, Mallory ML, Brewer-Jensen PD, Bryant JM, Costantini V, Monit C, Vinjé J, Baric RS, Goldstein RA, Breuer J. Preadaptation of pandemic GII.4 noroviruses in unsampled virus reservoirs years before emergence. Virus Evolution. 6: veaa067. PMID 33381305 DOI: 10.1093/Ve/Veaa067 |
0.31 |
|
| 2020 |
Pollock DD, Castoe TA, Perry BW, Lytras S, Wade KJ, Robertson DL, Holmes EC, Boni MF, Kosakovsky Pond SL, Parry R, Carlton EJ, Wood JLN, Pennings PS, Goldstein RA. Viral CpG deficiency provides no evidence that dogs were intermediate hosts for SARS-CoV-2. Molecular Biology and Evolution. PMID 32658964 DOI: 10.1093/Molbev/Msaa178 |
0.31 |
|
| 2020 |
Lassalle F, Beale MA, Bharucha T, Williams CA, Williams RJ, Cudini J, Goldstein R, Haque T, Depledge DP, Breuer J. Whole genome sequencing of Herpes Simplex Virus 1 directly from human cerebrospinal fluid reveals selective constraints in neurotropic viruses. Virus Evolution. 6: veaa012. PMID 32099667 DOI: 10.1093/Ve/Veaa012 |
0.362 |
|
| 2019 |
Monit C, Goldstein RA, Towers GJ. ChromaClade: combined visualisation of phylogenetic and sequence data. Bmc Evolutionary Biology. 19: 186. PMID 31615393 DOI: 10.1186/S12862-019-1518-9 |
0.37 |
|
| 2019 |
Monit C, Morris ER, Ruis C, Szafran B, Thiltgen G, Tsai MC, Mitchison NA, Bishop KN, Stoye JP, Taylor IA, Fassati A, Goldstein RA. Positive selection in dNTPase SAMHD1 throughout mammalian evolution. Proceedings of the National Academy of Sciences of the United States of America. PMID 31451672 DOI: 10.1073/Pnas.1908755116 |
0.379 |
|
| 2019 |
Khatri BS, Goldstein RA. Biophysics and population size constrains speciation in an evolutionary model of developmental system drift. Plos Computational Biology. 15: e1007177. PMID 31335870 DOI: 10.1371/Journal.Pcbi.1007177 |
0.311 |
|
| 2019 |
Cudini J, Roy S, Houldcroft CJ, Bryant JM, Depledge DP, Tutill H, Veys P, Williams R, Worth AJJ, Tamuri AU, Goldstein RA, Breuer J. Human cytomegalovirus haplotype reconstruction reveals high diversity due to superinfection and evidence of within-host recombination. Proceedings of the National Academy of Sciences of the United States of America. PMID 30819890 DOI: 10.1073/Pnas.1818130116 |
0.733 |
|
| 2018 |
Monit C, Goldstein RA. SubRecon: Ancestral Reconstruction of Amino Acid Substitutions Along a Branch in a Phylogeny. Bioinformatics (Oxford, England). PMID 29506148 DOI: 10.1093/Bioinformatics/Bty101 |
0.326 |
|
| 2017 |
Goldstein RA, Pollock DD. Sequence entropy of folding and the absolute rate of amino acid substitutions. Nature Ecology & Evolution. PMID 29062121 DOI: 10.1038/S41559-017-0338-9 |
0.448 |
|
| 2016 |
Thiltgen G, Dos Reis M, Goldstein RA. Finding Direction in the Search for Selection. Journal of Molecular Evolution. PMID 27913840 DOI: 10.1007/S00239-016-9765-5 |
0.56 |
|
| 2016 |
Goldstein RA, Pollock DD. The tangled bank of amino acids. Protein Science : a Publication of the Protein Society. PMID 27028523 DOI: 10.1002/Pro.2930 |
0.445 |
|
| 2015 |
Khatri BS, Goldstein RA. Simple Biophysical Model Predicts Faster Accumulation of Hybrid Incompatibilities in Small Populations Under Stabilising Selection. Genetics. PMID 26434721 DOI: 10.1534/Genetics.115.181685 |
0.34 |
|
| 2015 |
Khatri BS, Goldstein RA. A coarse-grained biophysical model of sequence evolution and the population size dependence of the speciation rate. Journal of Theoretical Biology. 378: 56-64. PMID 25936759 DOI: 10.1016/J.Jtbi.2015.04.027 |
0.371 |
|
| 2015 |
Goldstein RA, Pollard ST, Shah SD, Pollock DD. Nonadaptive Amino Acid Convergence Rates Decrease over Time. Molecular Biology and Evolution. 32: 1373-81. PMID 25737491 DOI: 10.1093/Molbev/Msv041 |
0.379 |
|
| 2014 |
Pollock DD, Goldstein RA. Strong evidence for protein epistasis, weak evidence against it. Proceedings of the National Academy of Sciences of the United States of America. 111: E1450. PMID 24706894 DOI: 10.1073/Pnas.1401112111 |
0.374 |
|
| 2013 |
Goldstein RA. Population size dependence of fitness effect distribution and substitution rate probed by biophysical model of protein thermostability Genome Biology and Evolution. 5: 1584-1593. PMID 23884461 DOI: 10.1093/Gbe/Evt110 |
0.334 |
|
| 2012 |
Thiltgen G, Goldstein RA. Assessing Predictors of Changes in Protein Stability upon Mutation Using Self-Consistency Plos One. 7. PMID 23144695 DOI: 10.1371/Journal.Pone.0046084 |
0.35 |
|
| 2012 |
Coluzza I, MacDonald JT, Sadowski MI, Taylor WR, Goldstein RA. Analytic markovian rates for generalized protein structure evolution. Plos One. 7: e34228. PMID 22693543 DOI: 10.1371/Journal.Pone.0034228 |
0.407 |
|
| 2012 |
Pollock DD, Thiltgen G, Goldstein RA. Amino acid coevolution induces an evolutionary Stokes shift. Proceedings of the National Academy of Sciences of the United States of America. 109: E1352-9. PMID 22547823 DOI: 10.1073/Pnas.1120084109 |
0.355 |
|
| 2012 |
Liberles DA, Teichmann SA, Bahar I, Bastolla U, Bloom J, Bornberg-Bauer E, Colwell LJ, de Koning AP, Dokholyan NV, Echave J, Elofsson A, Gerloff DL, Goldstein RA, Grahnen JA, Holder MT, et al. The interface of protein structure, protein biophysics, and molecular evolution. Protein Science : a Publication of the Protein Society. 21: 769-85. PMID 22528593 DOI: 10.1002/Pro.2071 |
0.45 |
|
| 2012 |
Tamuri AU, dos Reis M, Goldstein RA. Estimating the distribution of selection coefficients from phylogenetic data using sitewise mutation-selection models Genetics. 190: 1101-1115. PMID 22209901 DOI: 10.1534/Genetics.111.136432 |
0.773 |
|
| 2011 |
Soyer OS, Goldstein RA. Evolution of response dynamics underlying bacterial chemotaxis. Bmc Evolutionary Biology. 11: 240. PMID 21846396 DOI: 10.1186/1471-2148-11-240 |
0.63 |
|
| 2011 |
Goldstein RA. The evolution and evolutionary consequences of marginal thermostability in proteins Proteins: Structure, Function and Bioinformatics. 79: 1396-1407. PMID 21337623 DOI: 10.1002/Prot.22964 |
0.379 |
|
| 2011 |
dos Reis M, Tamuri AU, Hay AJ, Goldstein RA. Charting the host adaptation of influenza viruses. Molecular Biology and Evolution. 28: 1755-67. PMID 21109586 DOI: 10.1093/Molbev/Msq317 |
0.759 |
|
| 2009 |
Tamuri AU, Dos Reis M, Hay AJ, Goldstein RA. Identifying changes in selective constraints: host shifts in influenza. Plos Computational Biology. 5: e1000564. PMID 19911053 DOI: 10.1371/Journal.Pcbi.1000564 |
0.779 |
|
| 2009 |
dos Reis M, Hay AJ, Goldstein RA. Using non-homogeneous models of nucleotide substitution to identify host shift events: application to the origin of the 1918 'Spanish' influenza pandemic virus. Journal of Molecular Evolution. 69: 333-45. PMID 19787384 DOI: 10.1007/S00239-009-9282-X |
0.574 |
|
| 2008 |
Goldstein RA, Soyer OS. Evolution of taxis responses in virtual bacteria: non-adaptive dynamics. Plos Computational Biology. 4: e1000084. PMID 18483577 DOI: 10.1371/Journal.Pcbi.1000084 |
0.623 |
|
| 2008 |
Blackburne BP, Hay AJ, Goldstein RA. Changing selective pressure during antigenic changes in human influenza H3. Plos Pathogens. 4: e1000058. PMID 18451985 DOI: 10.1371/Journal.Ppat.1000058 |
0.323 |
|
| 2008 |
Goldstein RA. The structure of protein evolution and the evolution of protein structure Current Opinion in Structural Biology. 18: 170-177. PMID 18328690 DOI: 10.1016/J.Sbi.2008.01.006 |
0.411 |
|
| 2007 |
Goldstein RA. Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation Protein Science. 16: 1887-1895. PMID 17766385 DOI: 10.1110/Ps.072947007 |
0.322 |
|
| 2006 |
Williams PD, Pollock DD, Goldstein RA. SELECTIVE ADVANTAGE OF RECOMBINATION IN EVOLVING PROTEIN POPULATIONS: A LATTICE MODEL STUDY. International Journal of Modern Physics. C, Physics and Computers. 17: 75-90. PMID 25473139 DOI: 10.1142/S0129183106008959 |
0.424 |
|
| 2006 |
Williams PD, Pollock DD, Goldstein RA. Functionality and the evolution of marginal stability in proteins: inferences from lattice simulations. Evolutionary Bioinformatics Online. 2: 91-101. PMID 19455204 DOI: 10.4137/Ebo.S0 |
0.403 |
|
| 2006 |
Williams PD, Pollock DD, Blackburne BP, Goldstein RA. Assessing the accuracy of ancestral protein reconstruction methods. Plos Computational Biology. 2: e69. PMID 16789817 DOI: 10.1371/Journal.Pcbi.0020069 |
0.44 |
|
| 2006 |
Goldstein RA, Pollock DD. Observations of amino acid gain and loss during protein evolution are explained by statistical bias. Molecular Biology and Evolution. 23: 1444-9. PMID 16698770 DOI: 10.1093/Molbev/Msl010 |
0.403 |
|
| 2005 |
Xu YO, Hall RW, Goldstein RA, Pollock DD. Divergence, recombination and retention of functionality during protein evolution. Human Genomics. 2: 158-67. PMID 16197733 DOI: 10.1186/1479-7364-2-3-158 |
0.655 |
|
| 2004 |
Soyer OS, Goldstein RA. Predicting functional sites in proteins: site-specific evolutionary models and their application to neurotransmitter transporters. Journal of Molecular Biology. 339: 227-42. PMID 15123434 DOI: 10.1016/J.Jmb.2004.03.025 |
0.692 |
|
| 2004 |
Qian B, Goldstein RA. Performance of an iterated T-HMM for homology detection Bioinformatics. 20: 2175-2180. PMID 15044240 DOI: 10.1093/Bioinformatics/Bth181 |
0.581 |
|
| 2003 |
Soyer OS, Dimmic MW, Neubig RR, Goldstein RA. Dimerization in aminergic G-protein-coupled receptors: application of a hidden-site class model of evolution. Biochemistry. 42: 14522-31. PMID 14661965 DOI: 10.1021/Bi035097R |
0.784 |
|
| 2003 |
Goldberg NR, Beuming T, Soyer OS, Goldstein RA, Weinstein H, Javitch JA. Probing conformational changes in neurotransmitter transporters: a structural context. European Journal of Pharmacology. 479: 3-12. PMID 14612133 DOI: 10.1016/J.Ejphar.2003.08.052 |
0.62 |
|
| 2003 |
Qian B, Soyer OS, Neubig RR, Goldstein RA. Depicting a protein's two faces: GPCR classification by phylogenetic tree-based HMMs. Febs Letters. 554: 95-9. PMID 14596921 DOI: 10.1016/S0014-5793(03)01112-8 |
0.746 |
|
| 2003 |
Qian B, Goldstein RA. Detecting distant homologs using phylogenetic tree-based HMMS Proteins: Structure, Function and Genetics. 52: 446-453. PMID 12866055 DOI: 10.1002/Prot.10373 |
0.585 |
|
| 2002 |
Qian B, Goldstein RA. Optimization of a new score function for the generation of accurate alignments Proteins: Structure, Function and Genetics. 48: 605-610. PMID 12211027 DOI: 10.1002/Prot.10132 |
0.559 |
|
| 2002 |
Dimmic MW, Rest JS, Mindell DP, Goldstein RA. rtREV: an amino acid substitution matrix for inference of retrovirus and reverse transcriptase phylogeny. Journal of Molecular Evolution. 55: 65-73. PMID 12165843 DOI: 10.1007/S00239-001-2304-Y |
0.788 |
|
| 2002 |
Kann MG, Goldstein RA. Performance evaluation of a new algorithm for the detection of remote homologs with sequence comparison. Proteins. 48: 367-76. PMID 12112703 DOI: 10.1002/Prot.10117 |
0.669 |
|
| 2002 |
Soyer O, Dimmic MW, Neubig RR, Goldstein RA. Using evolutionary methods to study G-protein coupled receptors. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 625-36. PMID 11928514 |
0.787 |
|
| 2002 |
Taverna DM, Goldstein RA. Why are proteins so robust to site mutations? Journal of Molecular Biology. 315: 479-484. PMID 11786027 DOI: 10.1006/Jmbi.2001.5226 |
0.747 |
|
| 2002 |
Taverna DM, Goldstein RA. Why are proteins marginally stable? Proteins: Structure, Function and Genetics. 46: 105-109. PMID 11746707 DOI: 10.1002/Prot.10016 |
0.731 |
|
| 2001 |
Qian B, Goldstein RA. Distribution of Indel lengths. Proteins. 45: 102-4. PMID 11536366 DOI: 10.1002/Prot.1129 |
0.61 |
|
| 2001 |
Williams PD, Pollock DD, Goldstein RA. Evolution of functionality in lattice proteins. Journal of Molecular Graphics & Modelling. 19: 150-6. PMID 11381526 DOI: 10.1016/S1093-3263(00)00125-X |
0.392 |
|
| 2001 |
Koshi JM, Goldstein RA. Analyzing site heterogeneity during protein evolution. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 191-202. PMID 11262940 |
0.31 |
|
| 2000 |
Kann M, Qian B, Goldstein RA. Optimization of a new score function for the detection of remote homologs Proteins: Structure, Function and Genetics. 41: 498-503. PMID 11056037 DOI: 10.1002/1097-0134(20001201)41:4<498::Aid-Prot70>3.0.Co;2-3 |
0.745 |
|
| 2000 |
Chiu TL, Goldstein RA. How to generate improved potentials for protein tertiary structure prediction: A lattice model study Proteins: Structure, Function and Genetics. 41: 157-163. PMID 10966569 DOI: 10.1002/1097-0134(20001101)41:2<157::Aid-Prot10>3.0.Co;2-W |
0.39 |
|
| 2000 |
Dimmic MW, Mindell DP, Goldstein RA. Modeling evolution at the protein level using an adjustable amino acid fitness model. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 18-29. PMID 10902153 |
0.79 |
|
| 2000 |
Taverna DM, Goldstein RA. The distribution of structures in evolving protein populations Biopolymers. 53: 1-8. PMID 10644946 DOI: 10.1002/(Sici)1097-0282(200001)53:1<1::Aid-Bip1>3.0.Co;2-X |
0.718 |
|
| 2000 |
Buchler NEG, Goldstein RA. Surveying determinants of protein structure designability across different energy models and amino-acid alphabets: A consensus Journal of Chemical Physics. 112: 2533-2547. DOI: 10.1063/1.480893 |
0.389 |
|
| 2000 |
Williams PD, Goldstein RA. Population and functional effects on protein flexibility Journal of Molecular Graphics and Modelling. 18: 557. DOI: 10.1016/S1093-3263(00)80139-4 |
0.328 |
|
| 2000 |
Goldstein RA. Evolutionary perspectives on protein folding and stability Journal of Molecular Graphics and Modelling. 18: 552-553. DOI: 10.1016/S1093-3263(00)80121-7 |
0.341 |
|
| 2000 |
Taverna D, Goldstein R. Optimized and evolved protein residue interactions Journal of Molecular Graphics and Modelling. 18: 552. DOI: 10.1016/S1093-3263(00)80119-9 |
0.689 |
|
| 1999 |
Govindarajan S, Recabarren R, Goldstein RA. Estimating the total number of protein folds. Proteins. 35: 408-14. PMID 10382668 DOI: 10.1002/(Sici)1097-0134(19990601)35:4<408::Aid-Prot4>3.0.Co;2-A |
0.395 |
|
| 1999 |
Buchler NE, Goldstein RA. Effect of alphabet size and foldability requirements on protein structure designability. Proteins. 34: 113-24. PMID 10336377 DOI: 10.1002/(Sici)1097-0134(19990101)34:1<113::Aid-Prot9>3.0.Co;2-J |
0.708 |
|
| 1999 |
Koshi JM, Mindell DP, Goldstein RA. Using physical-chemistry-based substitution models in phylogenetic analyses of HIV-1 subtypes. Molecular Biology and Evolution. 16: 173-9. PMID 10028285 DOI: 10.1093/Oxfordjournals.Molbev.A026100 |
0.379 |
|
| 1999 |
Buchler NEG, Goldstein RA. Universal correlation between energy gap and foldability for the random energy model and lattice proteins Journal of Chemical Physics. 111: 6599-6609. DOI: 10.1063/1.479951 |
0.306 |
|
| 1998 |
Chiu TL, Goldstein RA. Optimizing potentials for the inverse protein folding problem Protein Engineering. 11: 749-752. PMID 9796822 DOI: 10.1093/Protein/11.9.749 |
0.393 |
|
| 1998 |
Koshi JM, Goldstein RA. Models of natural mutations including site heterogeneity. Proteins. 32: 289-95. PMID 9715905 DOI: 10.1002/(Sici)1097-0134(19980815)32:3<289::Aid-Prot4>3.0.Co;2-D |
0.415 |
|
| 1998 |
Chiu TL, Goldstein RA. Optimizing energy potentials for success in protein tertiary structure prediction Folding and Design. 3: 223-228. PMID 9669880 DOI: 10.1016/S1359-0278(98)00030-3 |
0.368 |
|
| 1998 |
Govindarajan S, Goldstein RA. On the thermodynamic hypothesis of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 95: 5545-9. PMID 9576919 DOI: 10.1073/Pnas.95.10.5545 |
0.409 |
|
| 1997 |
Koshi JM, Mindell DP, Goldstein RA. Beyond Mutation Matrices: Physical-Chemistry Based Evolutionary Models. Genome Informatics. Workshop On Genome Informatics. 8: 80-89. PMID 11072308 DOI: 10.11234/Gi1990.8.80 |
0.397 |
|
| 1997 |
Govindarajan S, Goldstein RA. Evolution of model proteins on a foldability landscape. Proteins. 29: 461-6. PMID 9408943 DOI: 10.1002/(Sici)1097-0134(199712)29:4<461::Aid-Prot6>3.0.Co;2-B |
0.394 |
|
| 1997 |
Thompson MJ, Goldstein RA. Predicting protein secondary structure with probabilistic schemata of evolutionarily derived information Protein Science. 6: 1963-1975. PMID 9300496 DOI: 10.1002/Pro.5560060917 |
0.428 |
|
| 1997 |
Govindarajan S, Goldstein RA. The foldability landscape of model proteins. Biopolymers. 42: 427-38. PMID 9283292 DOI: 10.1002/(Sici)1097-0282(19971005)42:4<427::Aid-Bip6>3.0.Co;2-S |
0.468 |
|
| 1997 |
Buchler NE, Zuiderweg ER, Wang H, Goldstein RA. Protein heteronuclear NMR assignments using mean-field simulated annealing. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 125: 34-42. PMID 9245358 DOI: 10.1006/Jmre.1997.1106 |
0.664 |
|
| 1997 |
Koshi JM, Goldstein RA. Mutation matrices and physical-chemical properties: correlations and implications. Proteins. 27: 336-44. PMID 9094736 DOI: 10.1002/(Sici)1097-0134(199703)27:3<336::Aid-Prot2>3.0.Co;2-B |
0.391 |
|
| 1997 |
Chiu TL, Goldstein RA. Compaction and folding in model proteins Journal of Chemical Physics. 107: 4408-4415. DOI: 10.1063/1.474782 |
0.35 |
|
| 1996 |
Koshi JM, Goldstein RA. Probabilistic reconstruction of ancestral protein sequences. Journal of Molecular Evolution. 42: 313-20. PMID 8919883 DOI: 10.1007/Bf02198858 |
0.445 |
|
| 1996 |
Thompson MJ, Goldstein RA. Predicting solvent accessibility: higher accuracy using Bayesian statistics and optimized residue substitution classes. Proteins. 25: 38-47. PMID 8727318 DOI: 10.1002/(Sici)1097-0134(199605)25:1<38::Aid-Prot4>3.0.Co;2-G |
0.394 |
|
| 1996 |
Thompson MJ, Goldstein RA. Constructing amino acid residue substitution classes maximally indicative of local protein structure. Proteins. 25: 28-37. PMID 8727317 DOI: 10.1002/(Sici)1097-0134(199605)25:1<28::Aid-Prot3>3.0.Co;2-G |
0.416 |
|
| 1996 |
Govindarajan S, Goldstein RA. Why are some proteins structures so common? Proceedings of the National Academy of Sciences of the United States of America. 93: 3341-5. PMID 8622938 DOI: 10.1073/Pnas.93.8.3341 |
0.425 |
|
| 1995 |
Koshi JM, Goldstein RA. Context-dependent optimal substitution matrices. Protein Engineering. 8: 641-5. PMID 8577693 DOI: 10.1093/Protein/8.7.641 |
0.415 |
|
| 1995 |
Govindarajan S, Goldstein RA. Optimal local propensities for model proteins. Proteins. 22: 413-8. PMID 7479714 DOI: 10.1002/Prot.340220411 |
0.341 |
|
| 1995 |
Govindarajan S, Goldstein RA. Searching for foldable protein structures using optimized energy functions Biopolymers. 36: 43-51. DOI: 10.1002/Bip.360360105 |
0.387 |
|
| 1993 |
Goldstein RA, Katzenellenbogen JA, Luthey-Schulten ZA, Seielstad DA, Wolynes PG. Three-dimensional model for the hormone binding domains of steroid receptors. Proceedings of the National Academy of Sciences of the United States of America. 90: 9949-53. PMID 8234340 DOI: 10.1073/Pnas.90.21.9949 |
0.514 |
|
| 1992 |
Goldstein RA, Luthey-Schulten ZA, Wolynes PG. Optimal protein-folding codes from spin-glass theory. Proceedings of the National Academy of Sciences of the United States of America. 89: 4918-22. PMID 1594594 DOI: 10.1073/Pnas.89.11.4918 |
0.529 |
|
| 1992 |
Goldstein RA, Luthey-Schulten ZA, Wolynes PG. Protein tertiary structure recognition using optimized Hamiltonians with local interactions. Proceedings of the National Academy of Sciences of the United States of America. 89: 9029-33. PMID 1409599 DOI: 10.1073/Pnas.89.19.9029 |
0.557 |
|
| 1991 |
Friedrichs MS, Goldstein RA, Wolynes PG. Generalized protein tertiary structure recognition using associative memory Hamiltonians. Journal of Molecular Biology. 222: 1013-34. PMID 1762143 DOI: 10.1016/0022-2836(91)90591-S |
0.567 |
|
| 1989 |
Arthur M, Campanelli C, Arbeit RD, Kim C, Steinbach S, Johnson CE, Rubin RH, Goldstein R. Structure and copy number of gene clusters related to the pap P-adhesin operon of uropathogenic Escherichia coli. Infection and Immunity. 57: 314-321. PMID 2563255 DOI: 10.1128/Iai.57.2.314-321.1989 |
0.301 |
|
| 1989 |
Boxer SG, Goldstein RA, Lockhart DJ, Middendorf TR, Takiff L. Excited states, electron-transfer reactions, and intermediates in bacterial photosynthetic reaction centers The Journal of Physical Chemistry. 93: 8280-8294. DOI: 10.1021/J100363A004 |
0.468 |
|
| 1989 |
Goldstein RA, Boxer SG. The effect of very high magnetic fields on the reaction dynamics in bacterial reaction centers: Implications for the reaction mechanism Bba - Bioenergetics. 977: 78-86. DOI: 10.1016/S0005-2728(89)80011-8 |
0.46 |
|
| 1989 |
Goldstein RA, Boxer SG. The effect of very high magnetic fields on the delayed fluorescence from oriented bacterial reaction centers Bba - Bioenergetics. 977: 70-77. DOI: 10.1016/S0005-2728(89)80010-6 |
0.449 |
|
| 1987 |
Goldstein RA, Boxer SG. Effects of nuclear spin polarization on reaction dynamics in photosynthetic bacterial reaction centers. Biophysical Journal. 51: 937-46. PMID 19431700 DOI: 10.1016/S0006-3495(87)83421-5 |
0.45 |
|
| 1985 |
Chidsey CE, Takiff L, Goldstein RA, Boxer SG. Effect of magnetic fields on the triplet state lifetime in photosynthetic reaction centers: Evidence for thermal repopulation of the initial radical pair. Proceedings of the National Academy of Sciences of the United States of America. 82: 6850-4. PMID 16593615 DOI: 10.1073/Pnas.82.20.6850 |
0.687 |
|
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