| Year |
Citation |
Score |
| 2000 |
Blow D. So do we understand how enzymes work? Structure. 8: R77-R81. PMID 10801479 DOI: 10.1016/S0969-2126(00)00125-8 |
0.353 |
|
| 1998 |
De Meester P, Brick P, Lloyd LF, Blow DM, Onesti S. Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator. Acta Crystallographica. Section D, Biological Crystallography. 54: 589-97. PMID 9761854 DOI: 10.1107/S0907444997015849 |
0.637 |
|
| 1997 |
Blow DM. The tortuous story of Asp ... His ... Ser: structural analysis of alpha-chymotrypsin. Trends in Biochemical Sciences. 22: 405-8. PMID 9357317 DOI: 10.1016/S0968-0004(97)01115-8 |
0.329 |
|
| 1997 |
Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure (London, England : 1993). 5: 337-47. PMID 9083113 DOI: 10.1016/S0969-2126(97)00191-3 |
0.637 |
|
| 1997 |
Riès-Kautt M, Broutin I, Ducruix A, Shepard W, Kahn R, Chayen N, Blow D, Paal K, Littke W, Lorber B, Théobald-Dietrich A, Giegé R. Crystallogenesis studies in microgravity with the advanced protein crystallization facility on spaceHab-01 Journal of Crystal Growth. 181: 79-96. DOI: 10.1016/S0022-0248(97)00280-7 |
0.359 |
|
| 1996 |
Rowsell S, Pauptit RA, Tucker AD, Brick P, Lloyd LF, Melton RG, Blow DM. Crystal structure of carboxypeptidase G2and comparison with other zinc-containing exopeptidases Acta Crystallographica Section a Foundations of Crystallography. 52: C138-C138. DOI: 10.1107/S0108767396093725 |
0.637 |
|
| 1995 |
Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE, Blow DM. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller Structure. 3: 541-549. PMID 8590015 DOI: 10.1016/S0969-2126(01)00188-5 |
0.61 |
|
| 1994 |
Saridakis EE, Stewart PD, Lloyd LF, Blow DM. Phase diagram and dilution experiments in the crystallization of carboxypeptidase G2. Acta Crystallographica. Section D, Biological Crystallography. 50: 293-7. PMID 15299442 DOI: 10.1107/S0907444993013186 |
0.364 |
|
| 1993 |
Varsani L, Cui T, Rangarajan M, Hartley BS, Goldberg J, Collyer C, Blow DM. Arthrobacter D-xylose isomerase: protein-engineered subunit interfaces. The Biochemical Journal. 291: 575-83. PMID 8484737 DOI: 10.1042/Bj2910575 |
0.35 |
|
| 1993 |
Chayen NE, Radcliffe JW, Blow DM. Control of nucleation in the crystallization of lysozyme. Protein Science : a Publication of the Protein Society. 2: 113-8. PMID 8443584 DOI: 10.1002/Pro.5560020112 |
0.328 |
|
| 1993 |
Li J, Vrielink A, Brick P, Blow DM. Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases. Biochemistry. 32: 11507-15. PMID 8218217 DOI: 10.1021/Bi00094A006 |
0.752 |
|
| 1992 |
Collyer CA, Goldberg JD, Viehmann H, Blow DM, Ramsden NG, Fleet GW, Montgomery FJ, Grice P. Anomeric specificity of D-xylose isomerase. Biochemistry. 31: 12211-8. PMID 1457418 DOI: 10.1021/Bi00163A034 |
0.416 |
|
| 1992 |
Blow DM, Collyer CA, Goldberg JD, Smart OS. Structure and mechanism of D-xylose isomerase. Faraday Discussions. 67-73. PMID 1290940 DOI: 10.1039/Fd9929300067 |
0.4 |
|
| 1992 |
Blow DM, Brick P, Collyer CA, Goldberg JD, Smart O. Conventional X-ray diffraction approaches to the study of enzyme mechanism: serine proteinases, aminoacyl-tRNA synthetases and xylose isomerase Philosophical Transactions of the Royal Society A. 340: 311-321. DOI: 10.1098/Rsta.1992.0069 |
0.618 |
|
| 1992 |
Eisenberg D, Perutz MF, Buckingham AD, Graf L, Thornton J, Blow DM, Fersht AR, Karplus M, Johnson LN, Rippmann F, Dodson GG, Edwards PN, Halling P, Wüthrich K, Symons MCR, et al. General discussion Faraday Discussions. 93: 107-129. DOI: 10.1039/FD9929300107 |
0.37 |
|
| 1992 |
Lloyd LF, Brick P, Blow DM, Mei-Zhen L. Crystallization studies on HIV-1 reverse transcriptase Journal of Crystal Growth. 122: 355-359. DOI: 10.1016/0022-0248(92)90269-O |
0.603 |
|
| 1992 |
Chayen NE, Shaw Stewart PD, Blow DM. Microbatch crystallization under oil - a new technique allowing many small-volume crystallization trials Journal of Crystal Growth. 122: 176-180. DOI: 10.1016/0022-0248(92)90241-A |
0.321 |
|
| 1991 |
Vrielink A, Lloyd LF, Blow DM. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution. Journal of Molecular Biology. 219: 533-54. PMID 2051487 DOI: 10.1016/0022-2836(91)90192-9 |
0.67 |
|
| 1991 |
Onesti S, Brick P, Blow DM. Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. Journal of Molecular Biology. 217: 153-76. PMID 1988676 DOI: 10.1016/0022-2836(91)90618-G |
0.649 |
|
| 1991 |
Lloyd LF, Brick P, Lou MZ, Chayen NE, Blow DM. Many crystal forms of human immunodeficiency virus reverse transcriptase. Journal of Molecular Biology. 217: 19-22. PMID 1703235 DOI: 10.1016/0022-2836(91)90607-8 |
0.594 |
|
| 1990 |
Collyer CA, Henrick K, Blow DM. Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift. Journal of Molecular Biology. 212: 211-35. PMID 2319597 DOI: 10.1016/0022-2836(90)90316-E |
0.332 |
|
| 1990 |
Chayen NE, Stewart PDS, Maeder DL, Blow DM. An Automated System for Micro-Batch Protein Crystallization and Screening Journal of Applied Crystallography. 23: 297-302. DOI: 10.1107/S0021889890003260 |
0.335 |
|
| 1989 |
Henrick K, Collyer CA, Blow DM. Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution, respectively. Journal of Molecular Biology. 208: 129-57. PMID 2769749 DOI: 10.1016/0022-2836(89)90092-2 |
0.462 |
|
| 1989 |
Onesti S, Lloyd LF, Maeder D, Mistry A, Brick P, Blow D, Blow DM. Crystallization and preliminary diffraction studies of Erythrina trypsin inhibitor. Journal of Molecular Biology. 210: 241-2. PMID 2511330 DOI: 10.1016/0022-2836(89)90306-9 |
0.611 |
|
| 1989 |
Brick P, Bhat TN, Blow DM. Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. Journal of Molecular Biology. 208: 83-98. PMID 2504923 DOI: 10.1016/0022-2836(89)90090-9 |
0.657 |
|
| 1989 |
Chayen NE, Lloyd LF, Collyer CA, Blow DM. Trigonal crystals of glucose isomerase require thymol for their growth and stability Journal of Crystal Growth. 97: 367-374. DOI: 10.1016/0022-0248(89)90218-2 |
0.36 |
|
| 1987 |
Brick P, Blow DM. Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. Journal of Molecular Biology. 194: 287-97. PMID 3612807 DOI: 10.1016/0022-2836(87)90376-7 |
0.669 |
|
| 1987 |
Brown KA, Brick P, Blow DM. Structure of a mutant of tyrosyl-tRNA synthetase with enhanced catalytic properties. Nature. 326: 416-8. PMID 3104791 DOI: 10.1038/326416A0 |
0.612 |
|
| 1986 |
Brown KA, Vrielink A, Blow DM. Crystal structures of two factitious mutants of tyrosyl-tRNA synthetase Biochemical Society Transactions. 14: 1228-1229. DOI: 10.1042/Bst0141228 |
0.409 |
|
| 1986 |
Akins J, Brick P, Jones HB, Hirayama N, Shaw PC, Blow DM. The crystallization of glucose isomerase from Arthrobacter B3728 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 874: 375-377. DOI: 10.1016/0167-4838(86)90039-7 |
0.589 |
|
| 1985 |
Tsukada H, Blow DM. Structure of alpha-chymotrypsin refined at 1.68 A resolution. Journal of Molecular Biology. 184: 703-11. PMID 4046030 DOI: 10.1016/0022-2836(85)90314-6 |
0.424 |
|
| 1985 |
Fersht AR, Shi JP, Knill-Jones J, Lowe DM, Wilkinson AJ, Blow DM, Brick P, Carter P, Waye MM, Winter G. Hydrogen bonding and biological specificity analysed by protein engineering. Nature. 314: 235-8. PMID 3845322 DOI: 10.1038/314235A0 |
0.577 |
|
| 1984 |
Wilkinson AJ, Fersht AR, Blow DM, Carter P, Winter G. A large increase in enzyme-substrate affinity by protein engineering. Nature. 307: 187-8. PMID 6690998 DOI: 10.1038/307187A0 |
0.403 |
|
| 1984 |
Monteilhet C, Blow DM, Brick P. Interaction of crystalline tyrosyl-tRNA synthetase with adenosine, adenosine monophosphate, adenosine triphosphate and pyrophosphate in the presence of tyrosinol. Journal of Molecular Biology. 173: 477-85. PMID 6323720 DOI: 10.1016/0022-2836(84)90392-9 |
0.604 |
|
| 1984 |
Fersht AR, Shi J, Wilkinson AJ, Blow DM, Carter P, Waye MMY, Winter GP. Analysis of Enzyme Structure and Activity by Protein Engineering Angewandte Chemie International Edition in English. 23: 467-473. DOI: 10.1002/Anie.198404673 |
0.419 |
|
| 1983 |
Wilkinson AJ, Fersht AR, Blow DM, Winter G. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry. 22: 3581-6. PMID 6615786 DOI: 10.1021/Bi00284A007 |
0.374 |
|
| 1983 |
Blow DM, Bhat TN, Metcalfe A, Risler JL, Brunie S, Zelwer C. Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases. Journal of Molecular Biology. 171: 571-6. PMID 6363712 DOI: 10.1016/0022-2836(83)90044-X |
0.378 |
|
| 1982 |
Bhat TN, Blow DM, Brick P, Nyborg J. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold. Journal of Molecular Biology. 158: 699-709. PMID 7120416 DOI: 10.1016/0022-2836(82)90255-8 |
0.694 |
|
| 1981 |
Rubin J, Blow DM. Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilus. Journal of Molecular Biology. 145: 489-500. PMID 7265210 DOI: 10.1016/0022-2836(81)90541-6 |
0.439 |
|
| 1981 |
Brick P, Bhat TN, Blow DM. Tyrosyl-tRNA synthetase forms a nucleotide binding fold Acta Crystallographica Section a Foundations of Crystallography. 37: C38-C38. DOI: 10.1107/S0108767381098474 |
0.588 |
|
| 1977 |
Blow DM, Irwin MJ, Nyborg J. The peptide chain of tyrosyl tRNA synthetase: no evidence for a super-secondary structure of four alpha-helices. Biochemical and Biophysical Research Communications. 76: 728-34. PMID 901445 DOI: 10.1016/0006-291X(77)91560-1 |
0.537 |
|
| 1976 |
Irwin MJ, Nyborg J, Reid BR, Blow DM. The crystal structure of tyrosyl-transfer RNA synthetase at 2-7 A resolution. Journal of Molecular Biology. 105: 577-86. PMID 972395 DOI: 10.1016/0022-2836(76)90236-9 |
0.554 |
|
| 1974 |
Blow DM, Janin J, Sweet RM. Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein-protein interactions. Nature. 249: 54-7. PMID 4857322 DOI: 10.1038/249054A0 |
0.527 |
|
| 1974 |
Sweet RM, Wright HT, Janin J, Chothia CH, Blow DM. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. Biochemistry. 13: 4212-28. PMID 4472048 DOI: 10.1021/Bi00717A024 |
0.68 |
|
| 1973 |
Reid BR, Koch GL, Boulanger Y, Hartley BS, Blow DM. Letter: Crystallization and preliminary x-ray diffraction studies on tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus. Journal of Molecular Biology. 80: 199-201. PMID 4784896 DOI: 10.1016/0022-2836(73)90241-6 |
0.301 |
|
| 1973 |
Blow DM, Matthews BW. Parameter refinement in the multiple isomorphous‐replacement method Acta Crystallographica Section A. 29: 56-62. DOI: 10.1107/S0567739473000124 |
0.351 |
|
| 1972 |
Wright CS, Hess GP, Blow DM. Structure of crystalline methyl-chymotrypsin. Journal of Molecular Biology. 63: 295-303. PMID 4634509 DOI: 10.1016/0022-2836(72)90376-2 |
0.472 |
|
| 1972 |
Henderson R, Wright CS, Hess GP, Blow DM. -Chymotrypsin: what can we learn about catalysis from x-ray diffraction? Cold Spring Harbor Symposia On Quantitative Biology. 36: 63-70. PMID 4508173 DOI: 10.1101/Sqb.1972.036.01.011 |
0.563 |
|
| 1970 |
Blow DM, Steitz TA. X-ray diffraction studies of enzymes. Annual Review of Biochemistry. 39: 63-100. PMID 5479039 DOI: 10.1146/annurev.bi.39.070170.000431 |
0.464 |
|
| 1970 |
Birktoft JJ, Blow DM, Henderson R, Steitz TA. I. Serine proteinases. The structure of alpha-chymotrypsin. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257: 67-76. PMID 4399050 DOI: 10.1098/Rstb.1970.0009 |
0.624 |
|
| 1969 |
Birktoft JJ, Matthews BW, Blow DM. Atomic co-ordinates for tosyl-alpha-chymotrypsin. Biochemical and Biophysical Research Communications. 36: 131-7. PMID 5796747 DOI: 10.1016/0006-291X(69)90659-7 |
0.398 |
|
| 1969 |
Steitz TA, Henderson R, Blow DM. Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin. Journal of Molecular Biology. 46: 337-48. PMID 5360043 DOI: 10.1016/0022-2836(69)90426-4 |
0.603 |
|
| 1968 |
Sigler PB, Blow DM, Matthews BW, Henderson R. Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. Journal of Molecular Biology. 35: 143-64. PMID 5760561 DOI: 10.1016/S0022-2836(68)80043-9 |
0.668 |
|
| 1967 |
Matthews BW, Sigler PB, Henderson R, Blow DM. Three-dimensional structure of tosyl-alpha-chymotrypsin. Nature. 214: 652-6. PMID 6049071 DOI: 10.1038/214652A0 |
0.706 |
|
| 1966 |
Sigler PB, Jeffery BA, Matthews BW, Blow DM. An x-ray diffraction study of inhibited derivatives of alpha-chymotrypsin. Journal of Molecular Biology. 15: 175-92. PMID 5912039 DOI: 10.1016/S0022-2836(66)80219-X |
0.607 |
|
| 1965 |
Sigler PB, Blow DM. A means of promoting heavy-atom binding in protein crystals. Journal of Molecular Biology. 14: 640-4. PMID 5880874 |
0.54 |
|
| 1960 |
Blow DM, Rich A. Formation of a Helical Complex by a Sulfonphthalein Dye1 Journal of the American Chemical Society. 82: 3572-3574. DOI: 10.1021/Ja01499A024 |
0.422 |
|
| 1960 |
Blow DM, Rich A. Studies on the Formation of Helical Deoxycholate Complexes1,2 Journal of the American Chemical Society. 82: 3566-3571. DOI: 10.1021/Ja01499A023 |
0.432 |
|
| 1958 |
RICH A, BLOW DM. Formation of a helical steroid complex. Nature. 182: 423-6. PMID 13577868 DOI: 10.1038/182423A0 |
0.426 |
|
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