| Year |
Citation |
Score |
| 2014 |
McKay DB, Xi L, Barthel KK, Cech TR. Structure and function of steroid receptor RNA activator protein, the proposed partner of SRA noncoding RNA. Journal of Molecular Biology. 426: 1766-85. PMID 24486609 DOI: 10.1016/J.Jmb.2014.01.006 |
0.447 |
|
| 2010 |
Hardin JW, Hu YX, McKay DB. Structure of the RNA binding domain of a DEAD-box helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif. Journal of Molecular Biology. 402: 412-27. PMID 20673833 DOI: 10.1016/J.Jmb.2010.07.040 |
0.444 |
|
| 2008 |
Wang S, Overgaard MT, Hu Y, McKay DB. The Bacillus subtilis RNA helicase YxiN is distended in solution. Biophysical Journal. 94: L01-3. PMID 17951299 DOI: 10.1529/Biophysj.107.120709 |
0.452 |
|
| 2007 |
Xu X, Wang S, Hu YX, McKay DB. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. Journal of Molecular Biology. 373: 367-81. PMID 17825319 DOI: 10.1016/J.Jmb.2007.07.069 |
0.495 |
|
| 2006 |
Caruthers JM, Hu Y, McKay DB. Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 1191-5. PMID 17142894 DOI: 10.1107/S1744309106044642 |
0.453 |
|
| 2006 |
Caruthers JM, Feng Y, McKay DB, Cohen SN. Retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation. The Journal of Biological Chemistry. 281: 27046-51. PMID 16854990 DOI: 10.1074/Jbc.M602467200 |
0.349 |
|
| 2006 |
Wang S, Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC, McKay DB. The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. Rna (New York, N.Y.). 12: 959-67. PMID 16611943 DOI: 10.1261/Rna.5906 |
0.474 |
|
| 2006 |
Wang S, Fleming RT, Westbrook EM, Matsumura P, McKay DB. Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription. Journal of Molecular Biology. 355: 798-808. PMID 16337229 DOI: 10.1016/J.Jmb.2005.11.020 |
0.44 |
|
| 2005 |
Karginov FV, Caruthers JM, Hu Y, McKay DB, Uhlenbeck OC. YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. The Journal of Biological Chemistry. 280: 35499-505. PMID 16118224 DOI: 10.1074/Jbc.M506815200 |
0.41 |
|
| 2004 |
Bitto E, McKay DB. Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins. Febs Letters. 568: 94-8. PMID 15196927 DOI: 10.1016/J.Febslet.2004.05.014 |
0.422 |
|
| 2004 |
Kwon AR, Trame CB, McKay DB. Kinetics of protein substrate degradation by HslUV. Journal of Structural Biology. 146: 141-7. PMID 15037245 DOI: 10.1016/J.Jsb.2003.11.003 |
0.38 |
|
| 2003 |
Bitto E, McKay DB. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. The Journal of Biological Chemistry. 278: 49316-22. PMID 14506253 DOI: 10.1074/Jbc.M308853200 |
0.398 |
|
| 2003 |
Wedekind JE, McKay DB. Crystal structure of the leadzyme at 1.8 A resolution: metal ion binding and the implications for catalytic mechanism and allo site ion regulation. Biochemistry. 42: 9554-63. PMID 12911297 DOI: 10.1021/Bi0300783 |
0.668 |
|
| 2003 |
Kwon AR, Kessler BM, Overkleeft HS, McKay DB. Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. Journal of Molecular Biology. 330: 185-95. PMID 12823960 DOI: 10.1016/S0022-2836(03)00580-1 |
0.473 |
|
| 2003 |
Trame CB, McKay DB. Structure of the Yersinia enterocolitica molecular-chaperone protein SycE. Acta Crystallographica. Section D, Biological Crystallography. 59: 389-92. PMID 12554962 DOI: 10.1107/S0907444902020826 |
0.481 |
|
| 2002 |
Bitto E, McKay DB. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure (London, England : 1993). 10: 1489-98. PMID 12429090 DOI: 10.1016/S0969-2126(02)00877-8 |
0.424 |
|
| 2002 |
Sousa MC, Kessler BM, Overkleeft HS, McKay DB. Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. Journal of Molecular Biology. 318: 779-85. PMID 12054822 DOI: 10.1016/S0022-2836(02)00145-6 |
0.647 |
|
| 2002 |
Caruthers JM, McKay DB. Helicase structure and mechanism. Current Opinion in Structural Biology. 12: 123-33. PMID 11839499 DOI: 10.1016/S0959-440X(02)00298-1 |
0.403 |
|
| 2001 |
Sousa MC, McKay DB. Structure of the universal stress protein of Haemophilus influenzae. Structure (London, England : 1993). 9: 1135-41. PMID 11738040 DOI: 10.1016/S0969-2126(01)00680-3 |
0.656 |
|
| 2001 |
Wedekind JE, Trame CB, Dorywalska M, Koehl P, Raschke TM, McKee M, FitzGerald D, Collier RJ, McKay DB. Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity. Journal of Molecular Biology. 314: 823-37. PMID 11734000 DOI: 10.1006/Jmbi.2001.5195 |
0.684 |
|
| 2001 |
Sousa MC, McKay DB. Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Acta Crystallographica. Section D, Biological Crystallography. 57: 1950-4. PMID 11717526 DOI: 10.1107/S090744490101575X |
0.654 |
|
| 2001 |
Trame CB, McKay DB. Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning. Acta Crystallographica. Section D, Biological Crystallography. 57: 1079-90. PMID 11468391 DOI: 10.1107/S0907444901007673 |
0.495 |
|
| 2000 |
Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB. Crystal and solution structures of an HslUV protease-chaperone complex. Cell. 103: 633-43. PMID 11106733 DOI: 10.1016/S0092-8674(00)00166-5 |
0.669 |
|
| 2000 |
Caruthers JM, Johnson ER, McKay DB. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proceedings of the National Academy of Sciences of the United States of America. 97: 13080-5. PMID 11087862 DOI: 10.1073/Pnas.97.24.13080 |
0.495 |
|
| 2000 |
Wedekind JE, McKay DB. Purification, crystallization, and X-ray diffraction analysis of small ribozymes. Methods in Enzymology. 317: 149-68. PMID 10829279 DOI: 10.1016/S0076-6879(00)17013-2 |
0.637 |
|
| 1999 |
Johnson ER, McKay DB. Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase. Rna (New York, N.Y.). 5: 1526-34. PMID 10606264 DOI: 10.1017/S1355838299991410 |
0.471 |
|
| 1999 |
Johnson ER, McKay DB. Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Biochemistry. 38: 10823-30. PMID 10451379 DOI: 10.1021/Bi990816G |
0.445 |
|
| 1999 |
Wedekind JE, McKay DB. Crystal structure of a lead-dependent ribozyme revealing metal binding sites relevant to catalysis. Nature Structural Biology. 6: 261-8. PMID 10074945 DOI: 10.1038/6700 |
0.68 |
|
| 1998 |
Sousa MC, McKay DB. The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change. Biochemistry. 37: 15392-9. PMID 9799500 DOI: 10.1021/Bi981510X |
0.662 |
|
| 1998 |
Wedekind JE, McKay DB. Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis. Annual Review of Biophysics and Biomolecular Structure. 27: 475-502. PMID 9646875 DOI: 10.1146/Annurev.Biophys.27.1.475 |
0.661 |
|
| 1998 |
Wilbanks SM, McKay DB. Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70. Biochemistry. 37: 7456-62. PMID 9585559 DOI: 10.1021/Bi973046M |
0.458 |
|
| 1997 |
Ha JH, Hellman U, Johnson ER, Li L, McKay DB, Sousa MC, Takeda S, Wernstedt C, Wilbanks SM. Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone Journal of Biological Chemistry. 272: 27796-27803. PMID 9346924 DOI: 10.1074/Jbc.272.44.27796 |
0.627 |
|
| 1997 |
Sousa MC, McKay DB. Structural and functional studies of the bovine 70 kda heat shock protein Protein Engineering. 10: 36. |
0.553 |
|
| 1996 |
Bode W, Grams F, Reinemer P, Gomis-Rüth FX, Baumann U, McKay DB, Stöcker W. The metzincin-superfamily of zinc-peptidases Advances in Experimental Medicine and Biology. 389: 1-11. PMID 8860988 DOI: 10.1007/978-1-4613-0335-0_1 |
0.318 |
|
| 1996 |
O'Brien MC, Flaherty KM, McKay DB. Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis Journal of Biological Chemistry. 271: 15874-15878. PMID 8663302 DOI: 10.1074/Jbc.271.27.15874 |
0.444 |
|
| 1996 |
Takeda S, McKay DB. Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone Biochemistry. 35: 4636-4644. PMID 8605215 DOI: 10.1021/Bi952903O |
0.392 |
|
| 1995 |
Wilbanks SM, McKay DB. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site Journal of Biological Chemistry. 270: 2251-2257. PMID 7836458 DOI: 10.1074/Jbc.270.5.2251 |
0.386 |
|
| 1995 |
O'Brien MC, McKay DB. How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity Journal of Biological Chemistry. 270: 2247-2250. PMID 7836457 DOI: 10.1074/Jbc.270.5.2247 |
0.346 |
|
| 1995 |
Stocker W, Grams F, Baumann U, Reinemer P, Gomis-Ruth FX, McKay DB, Bode W. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases Protein Science. 4: 823-840. PMID 7663339 DOI: 10.1002/Pro.5560040502 |
0.434 |
|
| 1995 |
Wilbanks SM, Chen L, Tsuruta H, Hodgson KO, McKay DB. Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments. Biochemistry. 34: 12095-106. PMID 7547949 DOI: 10.1021/Bi00038A002 |
0.427 |
|
| 1995 |
Ha JH, McKay DB. Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the atp-induced conformational change follows initial ATP binding Biochemistry. 34: 11635-11644. PMID 7547895 DOI: 10.1021/Bi00036A040 |
0.421 |
|
| 1994 |
Flaherty KM, Wilbanks SM, DeLuca-Flaherty C, McKay DB. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment Journal of Biological Chemistry. 269: 12899-12907. PMID 8175707 DOI: 10.2210/Pdb1Nga/Pdb |
0.464 |
|
| 1994 |
Wilbanks SM, DeLuca-Flaherty C, McKay DB. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants Journal of Biological Chemistry. 269: 12893-12898. PMID 8175706 |
0.376 |
|
| 1994 |
Ha JH, McKay DB. ATPase kinetics of recombinant bovine 70 KDA heat shock cognate protein and its amino-terminal ATPase domain Biochemistry®. 33: 14625-14635. PMID 7981225 DOI: 10.1021/Bi00252A031 |
0.364 |
|
| 1994 |
Pley HW, Flaherty KM, McKay DB. Three-dimensional structure of a hammerhead ribozyme Nature. 372: 68-74. PMID 7969422 DOI: 10.1038/372068A0 |
0.469 |
|
| 1994 |
Pley HW, Flaherty KM, McKay DB. Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix Nature. 372: 111-113. PMID 7526219 DOI: 10.1038/372111A0 |
0.367 |
|
| 1993 |
McKay DB. Structure and mechanism of 70-kDa heat-shock-related proteins Advances in Protein Chemistry. 44: 67-98. PMID 8317298 DOI: 10.1016/S0065-3233(08)60564-1 |
0.393 |
|
| 1993 |
Baumann U, Wu S, Flaherty KM, McKay DB. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif Embo Journal. 12: 3357-3364. PMID 8253063 DOI: 10.1002/J.1460-2075.1993.Tb06009.X |
0.45 |
|
| 1993 |
Flaherty KM, Zozulya S, Stryer L, McKay DB. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell. 75: 709-16. PMID 8242744 DOI: 10.1016/0092-8674(93)90491-8 |
0.329 |
|
| 1993 |
O'Brien MC, McKay DB. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis Journal of Biological Chemistry. 268: 24323-24329. PMID 8226982 DOI: 10.2210/Pdb1Atr/Pdb |
0.479 |
|
| 1992 |
McKay DB, Thayer MM, Flaherty KM, Pley H, Benvegnu D. Crystallographic structures of the elastase of Pseudomonas aeruginosa Matrix (Stuttgart, Germany). Supplement. 1: 112-115. PMID 1480011 |
0.415 |
|
| 1992 |
Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW. Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry. 31: 11310-6. PMID 1445869 DOI: 10.1021/Bi00161A008 |
0.456 |
|
| 1992 |
Ray S, Zozulya S, Niemi GA, Flaherty KM, Brolley D, Dizhoor AM, McKay DB, Hurley J, Stryer L. Cloning, expression, and crystallization of recoverin, a calcium sensor in vision. Proceedings of the National Academy of Sciences of the United States of America. 89: 5705-9. PMID 1385864 DOI: 10.1073/Pnas.89.13.5705 |
0.337 |
|
| 1991 |
Thayer MM, Flaherty KM, McKay DB. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-Å resolution Journal of Biological Chemistry. 266: 2864-2871. PMID 1899664 DOI: 10.2210/Pdb1Ezm/Pdb |
0.438 |
|
| 1991 |
Flaherty KM, McKay DB, Kabsch W, Holmes KC. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proceedings of the National Academy of Sciences of the United States of America. 88: 5041-5. PMID 1828889 DOI: 10.1073/Pnas.88.11.5041 |
0.485 |
|
| 1991 |
McKay DB. Structure of the 70-kiloDalton heat-shock-related proteins Springer Seminars in Immunopathology. 13: 1-9. PMID 1776119 DOI: 10.1007/Bf01225274 |
0.343 |
|
| 1990 |
DeLuca-Flaherty C, McKay DB. Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein Nucleic Acids Research. 18: 5569. PMID 2216746 DOI: 10.1093/Nar/18.18.5569 |
0.311 |
|
| 1990 |
Flaherty KM, DeLuca-Flaherty C, McKay DB. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein Nature. 346: 623-628. PMID 2143562 DOI: 10.1038/346623A0 |
0.445 |
|
| 1990 |
DeLuca-Flaherty C, McKay DB, Parham P, Hill BL. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis Cell. 62: 875-887. PMID 1975516 DOI: 10.1016/0092-8674(90)90263-E |
0.433 |
|
| 1988 |
Brandhuber BJ, Allured VS, Falbel TG, McKay DB. Mapping the enzymatic active site of Pseudomonas aeruginosa exotoxin A Proteins: Structure, Function and Genetics. 3: 146-154. PMID 3151219 DOI: 10.1002/Prot.340030303 |
0.456 |
|
| 1988 |
DeLuca-Flaherty C, Flaherty KM, McIntosh LJ, Bahrami B, McKay DB. Crystals of an ATPase fragment of bovine clathrin uncoating ATPase. Journal of Molecular Biology. 200: 749-50. PMID 2970553 DOI: 10.1016/0022-2836(88)90487-1 |
0.358 |
|
| 1986 |
Allured VS, Collier RJ, Carroll SF, McKay DB. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution Proceedings of the National Academy of Sciences of the United States of America. 83: 1320-1324. PMID 3006045 DOI: 10.1073/Pnas.83.5.1320 |
0.437 |
|
| 1985 |
Allured VS, Case LM, Leppla SH, McKay DB. Crystallization of the protective antigen protein of Bacillus anthracis Journal of Biological Chemistry. 260: 5012-5013. PMID 3921540 DOI: 10.21236/Ada148938 |
0.342 |
|
| 1982 |
McKay DB, Pickover CA, Steitz TA. Escherichia coli lac repressor is elongated with its operator DNA binding domains located at both ends. Journal of Molecular Biology. 156: 175-83. PMID 7047750 DOI: 10.1016/0022-2836(82)90465-X |
0.514 |
|
| 1982 |
Weber IT, McKay DB, Steitz TA. Two helix DNA binding motif of CAP found in lac repressor and gal repressor. Nucleic Acids Research. 10: 5085-102. PMID 6897114 DOI: 10.1093/nar/10.16.5085 |
0.516 |
|
| 1982 |
McKay DB, Weber IT, Steitz TA. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP. The Journal of Biological Chemistry. 257: 9518-24. PMID 6286624 |
0.598 |
|
| 1982 |
Steitz TA, Ohlendorf DH, McKay DB, Anderson WF, Matthews BW. Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins. Proceedings of the National Academy of Sciences of the United States of America. 79: 3097-100. PMID 6212926 DOI: 10.1073/Pnas.79.10.3097 |
0.556 |
|
| 1981 |
McKay DB, Steitz TA. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. Nature. 290: 744-9. PMID 6261152 DOI: 10.1107/S0108767381098942 |
0.589 |
|
| 1980 |
McKay DB, Steitz TA, Weber IT, West SC, Howard-Flanders P. Crystallization of monomeric recA protein. The Journal of Biological Chemistry. 255: 6662. PMID 6446560 |
0.479 |
|
| 1979 |
Pickover CA, McKay DB, Engelman DM, Steitz TA. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. The Journal of Biological Chemistry. 254: 11323-9. PMID 387770 |
0.496 |
|
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