| Year |
Citation |
Score |
| 2021 |
Hwang S, Pan C, Garcia B, Davidson AR, Moraes TF, Maxwell KL. Structural and mechanistic insight into CRISPR-Cas9 inhibition by anti-CRISPR protein AcrIIC4. Journal of Molecular Biology. 167420. PMID 34954237 DOI: 10.1016/j.jmb.2021.167420 |
0.316 |
|
| 2021 |
Shah M, Taylor VL, Bona D, Tsao Y, Stanley SY, Pimentel-Elardo SM, McCallum M, Bondy-Denomy J, Howell PL, Nodwell JR, Davidson AR, Moraes TF, Maxwell KL. A phage-encoded anti-activator inhibits quorum sensing in Pseudomonas aeruginosa. Molecular Cell. PMID 33412111 DOI: 10.1016/j.molcel.2020.12.011 |
0.308 |
|
| 2020 |
North OI, Davidson AR. Phage proteins required for tail fiber assembly also bind specifically to the surface of host bacterial strains. Journal of Bacteriology. PMID 33139482 DOI: 10.1128/JB.00406-20 |
0.314 |
|
| 2020 |
Osuna BA, Karambelkar S, Mahendra C, Christie KA, Garcia B, Davidson AR, Kleinstiver BP, Kilcher S, Bondy-Denomy J. Listeria Phages Induce Cas9 Degradation to Protect Lysogenic Genomes. Cell Host & Microbe. PMID 32325050 DOI: 10.1016/j.chom.2020.04.001 |
0.374 |
|
| 2019 |
North OI, Sakai K, Yamashita E, Nakagawa A, Iwazaki T, Büttner CR, Takeda S, Davidson AR. Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres. Nature Microbiology. PMID 31209305 DOI: 10.1038/s41564-019-0477-7 |
0.389 |
|
| 2018 |
Ben-David M, Huang H, Sun MGF, Corbi-Verge C, Petsalaki E, Liu K, Gfeller D, Garg P, Tempel W, Sochirca I, Shifman JM, Davidson A, Min J, Kim PM, Sidhu SS. Allosteric Modulation of Binding Specificity by Alternative Packing of Protein Cores. Journal of Molecular Biology. PMID 30471255 DOI: 10.1016/J.Jmb.2018.11.018 |
0.447 |
|
| 2015 |
Lam MH, Snider J, Rehal M, Wong V, Aboualizadeh F, Drecun L, Wong O, Jubran B, Li M, Ali M, Jessulat M, Deineko V, Miller R, Lee Me, Park HO, ... Davidson A, et al. A Comprehensive Membrane Interactome Mapping of Sho1p Reveals Fps1p as a Novel Key Player in the Regulation of the HOG Pathway in S. cerevisiae. Journal of Molecular Biology. 427: 2088-103. PMID 25644660 DOI: 10.1016/J.Jmb.2015.01.016 |
0.447 |
|
| 2015 |
Cumby N, Reimer K, Mengin-Lecreulx D, Davidson AR, Maxwell KL. The phage tail tape measure protein, an inner membrane protein and a periplasmic chaperone play connected roles in the genome injection process of E. coli phage HK97. Molecular Microbiology. 96: 437-47. PMID 25532427 DOI: 10.1111/mmi.12918 |
0.77 |
|
| 2014 |
Kala S, Cumby N, Sadowski PD, Hyder BZ, Kanelis V, Davidson AR, Maxwell KL. HNH proteins are a widespread component of phage DNA packaging machines. Proceedings of the National Academy of Sciences of the United States of America. 111: 6022-7. PMID 24711378 DOI: 10.1073/Pnas.1320952111 |
0.774 |
|
| 2013 |
Maxwell KL, Fatehi Hassanabad M, Chang T, Paul VD, Pirani N, Bona D, Edwards AM, Davidson AR. Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages. Journal of Bacteriology. 195: 5461-8. PMID 24097944 DOI: 10.1128/JB.00805-13 |
0.468 |
|
| 2013 |
Pell LG, Cumby N, Clark TE, Tuite A, Battaile KP, Edwards AM, Chirgadze NY, Davidson AR, Maxwell KL. A conserved spiral structure for highly diverged phage tail assembly chaperones. Journal of Molecular Biology. 425: 2436-49. PMID 23542344 DOI: 10.1016/j.jmb.2013.03.035 |
0.775 |
|
| 2012 |
Cumby N, Davidson AR, Maxwell KL. The moron comes of age. Bacteriophage. 2: 225-228. PMID 23739268 DOI: 10.4161/bact.23146 |
0.763 |
|
| 2012 |
Stollar EJ, Lin H, Davidson AR, Forman-Kay JD. Differential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysis. Plos One. 7: e51282. PMID 23251481 DOI: 10.1371/journal.pone.0051282 |
0.389 |
|
| 2012 |
Popovic A, Wu B, Arrowsmith CH, Edwards AM, Davidson AR, Maxwell KL. Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity. The Journal of Biological Chemistry. 287: 32085-95. PMID 22801427 DOI: 10.1074/jbc.M112.378349 |
0.478 |
|
| 2012 |
Cumby N, Edwards AM, Davidson AR, Maxwell KL. The bacteriophage HK97 gp15 moron element encodes a novel superinfection exclusion protein. Journal of Bacteriology. 194: 5012-9. PMID 22797755 DOI: 10.1128/JB.00843-12 |
0.775 |
|
| 2012 |
Garcia B, Stollar EJ, Davidson AR. The importance of conserved features of yeast actin-binding protein 1 (Abp1p): the conditional nature of essentiality. Genetics. 191: 1199-211. PMID 22661326 DOI: 10.1534/genetics.112.141739 |
0.418 |
|
| 2012 |
Stanger K, Gorelik M, Davidson AR. Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways. The Journal of Biological Chemistry. 287: 22133-41. PMID 22570491 DOI: 10.1074/Jbc.M112.348052 |
0.786 |
|
| 2012 |
Nguyen Ba AN, Yeh BJ, van Dyk D, Davidson AR, Andrews BJ, Weiss EL, Moses AM. Proteome-wide discovery of evolutionary conserved sequences in disordered regions. Science Signaling. 5: rs1. PMID 22416277 DOI: 10.1126/Scisignal.2002515 |
0.326 |
|
| 2012 |
Davidson AR, Cardarelli L, Pell LG, Radford DR, Maxwell KL. Long noncontractile tail machines of bacteriophages. Advances in Experimental Medicine and Biology. 726: 115-42. PMID 22297512 DOI: 10.1007/978-1-4614-0980-9_6 |
0.328 |
|
| 2012 |
Gorelik M, Davidson AR. Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface. The Journal of Biological Chemistry. 287: 9168-77. PMID 22277653 DOI: 10.1074/Jbc.M111.330753 |
0.775 |
|
| 2012 |
Gorelik M, Davidson A. Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Lcs/Pdb |
0.756 |
|
| 2011 |
Gorelik M, Stanger K, Davidson AR. A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function. The Journal of Biological Chemistry. 286: 19470-7. PMID 21489982 DOI: 10.1074/Jbc.M111.229294 |
0.797 |
|
| 2010 |
Pell LG, Gasmi-Seabrook GM, Morais M, Neudecker P, Kanelis V, Bona D, Donaldson LW, Edwards AM, Howell PL, Davidson AR, Maxwell KL. The solution structure of the C-terminal Ig-like domain of the bacteriophage λ tail tube protein. Journal of Molecular Biology. 403: 468-79. PMID 20826161 DOI: 10.1016/J.Jmb.2010.08.044 |
0.4 |
|
| 2010 |
Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. Proceedings of the National Academy of Sciences of the United States of America. 107: 14384-9. PMID 20660769 DOI: 10.1073/Pnas.1005822107 |
0.385 |
|
| 2010 |
Yu Z, Reichheld SE, Savchenko A, Parkinson J, Davidson AR. A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators. Journal of Molecular Biology. 400: 847-64. PMID 20595046 DOI: 10.1016/j.jmb.2010.05.062 |
0.329 |
|
| 2010 |
Cardarelli L, Lam R, Tuite A, Baker LA, Sadowski PD, Radford DR, Rubinstein JL, Battaile KP, Chirgadze N, Maxwell KL, Davidson AR. The crystal structure of bacteriophage HK97 gp6: defining a large family of head-tail connector proteins. Journal of Molecular Biology. 395: 754-68. PMID 19895817 DOI: 10.1016/J.Jmb.2009.10.067 |
0.31 |
|
| 2010 |
Gorelik M, Muhandiram R, Davidson A. Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p peptide Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16970 |
0.743 |
|
| 2010 |
Gorelik M, Muhandiram R, Davidson A. Structural and Functional Characterization of an Unusual SH3 Domain from the Fungal Adaptor Protein Bem1 Biophysical Journal. 98: 249a. DOI: 10.1016/J.Bpj.2009.12.1354 |
0.805 |
|
| 2009 |
Reichheld SE, Yu Z, Davidson AR. The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor. Proceedings of the National Academy of Sciences of the United States of America. 106: 22263-8. PMID 20080791 DOI: 10.1073/pnas.0911566106 |
0.354 |
|
| 2009 |
Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, Forman-Kay JD, Davidson AR. Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p. The Journal of Biological Chemistry. 284: 26918-27. PMID 19590096 DOI: 10.1074/Jbc.M109.028431 |
0.751 |
|
| 2009 |
Pell LG, Liu A, Edmonds L, Donaldson LW, Howell PL, Davidson AR. The X-ray crystal structure of the phage lambda tail terminator protein reveals the biologically relevant hexameric ring structure and demonstrates a conserved mechanism of tail termination among diverse long-tailed phages. Journal of Molecular Biology. 389: 938-51. PMID 19426744 DOI: 10.1016/J.Jmb.2009.04.072 |
0.354 |
|
| 2009 |
Pell LG, Kanelis V, Donaldson LW, Howell PL, Davidson AR. The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proceedings of the National Academy of Sciences of the United States of America. 106: 4160-5. PMID 19251647 DOI: 10.1073/Pnas.0900044106 |
0.367 |
|
| 2008 |
Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR, Chan HS. Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 105: 9999-10004. PMID 18626019 DOI: 10.1073/pnas.0801874105 |
0.302 |
|
| 2008 |
Kim J, Lee CD, Rath A, Davidson AR. Recognition of non-canonical peptides by the yeast Fus1p SH3 domain: elucidation of a common mechanism for diverse SH3 domain specificities. Journal of Molecular Biology. 377: 889-901. PMID 18280496 DOI: 10.1016/J.Jmb.2008.01.063 |
0.742 |
|
| 2007 |
Zarrine-Afsar A, Dahesh S, Davidson AR. Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain. Journal of Molecular Biology. 373: 764-74. PMID 17850820 DOI: 10.1016/j.jmb.2007.07.059 |
0.311 |
|
| 2007 |
Fraser JS, Maxwell KL, Davidson AR. Immunoglobulin-like domains on bacteriophage: weapons of modest damage? Current Opinion in Microbiology. 10: 382-7. PMID 17765600 DOI: 10.1016/J.Mib.2007.05.018 |
0.386 |
|
| 2007 |
Haynes J, Garcia B, Stollar EJ, Rath A, Andrews BJ, Davidson AR. The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context. Genetics. 176: 193-208. PMID 17409071 DOI: 10.1534/Genetics.106.070300 |
0.748 |
|
| 2007 |
Edmonds L, Liu A, Kwan JJ, Avanessy A, Caracoglia M, Yang I, Maxwell KL, Rubenstein J, Davidson AR, Donaldson LW. The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function. Journal of Molecular Biology. 365: 175-86. PMID 17056065 DOI: 10.1016/j.jmb.2006.09.068 |
0.316 |
|
| 2006 |
Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry. 45: 10175-83. PMID 16922492 DOI: 10.1021/Bi0611560 |
0.335 |
|
| 2006 |
Reichheld SE, Davidson AR. Two-way interdomain signal transduction in tetracycline repressor. Journal of Molecular Biology. 361: 382-9. PMID 16844141 DOI: 10.1016/j.jmb.2006.06.035 |
0.392 |
|
| 2006 |
Fraser JS, Yu Z, Maxwell KL, Davidson AR. Ig-like domains on bacteriophages: a tale of promiscuity and deceit. Journal of Molecular Biology. 359: 496-507. PMID 16631788 DOI: 10.1016/J.Jmb.2006.03.043 |
0.437 |
|
| 2006 |
Zarrine-Afsar A, Mittermaier A, Kay LE, Davidson AR. Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain. Protein Science : a Publication of the Protein Society. 15: 162-70. PMID 16373478 DOI: 10.1110/Ps.051829106 |
0.431 |
|
| 2005 |
Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L. NMR assignment of the gpU tail protein from lambda bacteriophage. Journal of Biomolecular Nmr. 32: 91-2. PMID 16041488 DOI: 10.1007/S10858-005-3659-Y |
0.368 |
|
| 2005 |
Rath A, Davidson AR, Deber CM. The structure of "unstructured" regions in peptides and proteins: role of the polyproline II helix in protein folding and recognition. Biopolymers. 80: 179-85. PMID 15700296 DOI: 10.1002/Bip.20227 |
0.738 |
|
| 2004 |
Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature. 430: 586-90. PMID 15282609 DOI: 10.1038/Nature02655 |
0.713 |
|
| 2004 |
Marles JA, Dahesh S, Haynes J, Andrews BJ, Davidson AR. Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast. Molecular Cell. 14: 813-23. PMID 15200958 DOI: 10.1016/j.molcel.2004.05.024 |
0.366 |
|
| 2004 |
Di Nardo AA, Korzhnev DM, Stogios PJ, Zarrine-Afsar A, Kay LE, Davidson AR. Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 7954-9. PMID 15148398 DOI: 10.1073/Pnas.0400550101 |
0.719 |
|
| 2003 |
Mittermaier A, Davidson AR, Kay LE. Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins. Journal of the American Chemical Society. 125: 9004-5. PMID 15369343 DOI: 10.1021/Ja034856Q |
0.326 |
|
| 2003 |
Di Nardo AA, Larson SM, Davidson AR. The relationship between conservation, thermodynamic stability, and function in the SH3 domain hydrophobic core. Journal of Molecular Biology. 333: 641-55. PMID 14556750 DOI: 10.1016/J.Jmb.2003.08.035 |
0.754 |
|
| 2002 |
Leung GC, Hudson JW, Kozarova A, Davidson A, Dennis JW, Sicheri F. The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localization Nature Structural Biology. 9: 719-724. PMID 12352953 DOI: 10.1038/Nsb848 |
0.471 |
|
| 2002 |
Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR. The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. Journal of Molecular Biology. 318: 1395-404. PMID 12083526 DOI: 10.1016/S0022-2836(02)00276-0 |
0.379 |
|
| 2002 |
Northey JG, Maxwell KL, Davidson AR. Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. Journal of Molecular Biology. 320: 389-402. PMID 12079394 DOI: 10.1016/S0022-2836(02)00445-X |
0.342 |
|
| 2002 |
Larson SM, Ruczinski I, Davidson AR, Baker D, Plaxco KW. Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation. Journal of Molecular Biology. 316: 225-33. PMID 11851333 DOI: 10.1006/Jmbi.2001.5344 |
0.363 |
|
| 2002 |
Northey JG, Di Nardo AA, Davidson AR. Hydrophobic core packing in the SH3 domain folding transition state. Nature Structural Biology. 9: 126-30. PMID 11786916 DOI: 10.1038/nsb748 |
0.719 |
|
| 2001 |
Maxwell KL, Yee AA, Booth V, Arrowsmith CH, Gold M, Davidson AR. The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold. Journal of Molecular Biology. 308: 9-14. PMID 11302702 DOI: 10.1006/Jmbi.2001.4582 |
0.334 |
|
| 2001 |
Mok YK, Elisseeva EL, Davidson AR, Forman-Kay JD. Dramatic stabilization of an SH3 domain by a single substitution: Roles of the folded and unfolded states Journal of Molecular Biology. 307: 913-928. PMID 11273710 DOI: 10.1006/jmbi.2001.4521 |
0.384 |
|
| 2001 |
Larson SM, Davidson AR. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Science : a Publication of the Protein Society. 9: 2170-80. PMID 11152127 DOI: 10.1110/Ps.9.11.2170 |
0.473 |
|
| 2000 |
Rath A, Davidson AR. The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis. Protein Science : a Publication of the Protein Society. 9: 2457-69. PMID 11206067 DOI: 10.1110/Ps.9.12.2457 |
0.746 |
|
| 2000 |
Yuen CTK, Davidson AR, Deber CM. Role of aromatic residues at the lipid-water interface in micelle-bound bacteriophage M13 major coat protein Biochemistry. 39: 16155-16162. PMID 11123944 DOI: 10.1021/bi0016117 |
0.327 |
|
| 2000 |
Larson SM, Di Nardo AA, Davidson AR. Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions. Journal of Molecular Biology. 303: 433-46. PMID 11031119 DOI: 10.1006/Jmbi.2000.4146 |
0.722 |
|
| 2000 |
Cruickshank J, Shire K, Davidson AR, Edwards AM, Frappier L. Two domains of the Epstein-Barr virus origin DNA-binding protein, EBNA1, orchestrate sequence-specific DNA binding Journal of Biological Chemistry. 275: 22273-22277. PMID 10801810 DOI: 10.1074/Jbc.M001414200 |
0.395 |
|
| 2000 |
Maxwell KL, Davidson AR, Murialdo H, Gold M. Thermodynamic and functional characterization of protein W from bacteriophage lambda. The three C-terminal residues are critical for activity. The Journal of Biological Chemistry. 275: 18879-86. PMID 10770927 DOI: 10.1074/jbc.M001178200 |
0.361 |
|
| 2000 |
Plaxco KW, Larson S, Ruczinski I, Riddle DS, Thayer EC, Buchwitz B, Davidson AR, Baker D. Evolutionary conservation in protein folding kinetics. Journal of Molecular Biology. 298: 303-12. PMID 10764599 DOI: 10.1006/Jmbi.1999.3663 |
0.317 |
|
| 1999 |
Maxwell KL, Mittermaier AK, Forman-Kay JD, Davidson AR. A simple in vivo assay for increased protein solubility. Protein Science : a Publication of the Protein Society. 8: 1908-11. PMID 10493593 DOI: 10.1110/Ps.8.9.1908 |
0.358 |
|
| 1999 |
Sampaleanu LM, Davidson AR, Graham C, Wistow GJ, Howell PL. Domain exchange experiments in duck delta-crystallins: functional and evolutionary implications. Protein Science : a Publication of the Protein Society. 8: 529-37. PMID 10091655 DOI: 10.1110/ps.8.3.529 |
0.429 |
|
| 1998 |
Maxwell KL, Davidson AR. Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects. Biochemistry. 37: 16172-82. PMID 9819209 DOI: 10.1021/bi981788p |
0.406 |
|
| 1998 |
Hoedemaeker FJ, Davidson AR, Rose DR. A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase. Proteins. 30: 275-86. PMID 9517543 DOI: 10.1002/(SICI)1097-0134(19980215)30:3<275::AID-PROT7>3.0.CO;2-J |
0.3 |
|
| 1996 |
Hong E, Davidson AR, Kaiser CA. A pathway for targeting soluble misfolded proteins to the yeast vacuole. The Journal of Cell Biology. 135: 623-33. PMID 8909538 DOI: 10.1083/jcb.135.3.623 |
0.363 |
|
| 1996 |
Cordes MHJ, Davidson AR, Sauer RT. Sequence space, folding and protein design Current Opinion in Structural Biology. 6: 3-10. PMID 8696970 DOI: 10.1016/S0959-440X(96)80088-1 |
0.336 |
|
| 1995 |
Davidson AR, Lumb KJ, Sauer RT. Cooperatively folded proteins in random sequence libraries Nature Structural Biology. 2: 856-864. PMID 7552709 DOI: 10.1038/Nsb1095-856 |
0.346 |
|
| 1994 |
Davidson AR, Sauer RT. Folded proteins occur frequently in libraries of random amino acid sequences. Proceedings of the National Academy of Sciences of the United States of America. 91: 2146-50. PMID 8134363 DOI: 10.1073/Pnas.91.6.2146 |
0.32 |
|
| 1991 |
Davidson A, Yau P, Murialdo H, Gold M. Isolation and characterization of mutations in the bacteriophage lambda terminase genes. Journal of Bacteriology. 173: 5086-5096. PMID 1830578 DOI: 10.1128/Jb.173.16.5086-5096.1991 |
0.303 |
|
| 1988 |
Davidson A, Gold M. A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage lambda FI gene product. Virology. 161: 305-14. PMID 2961121 DOI: 10.1016/0042-6822(87)90122-X |
0.315 |
|
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