| Year |
Citation |
Score |
| 2006 |
Ren H, Bandyopadhyay S, Allison WS. The alpha3(betaMet222Ser/Tyr345Trp)3gamma subcomplex of the TF1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity. Biochemistry. 45: 6222-30. PMID 16681395 DOI: 10.1021/Bi060232W |
0.395 |
|
| 2005 |
Bandyopadhyay S, Muneyuki E, Allison WS. The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site containing inhibitory MgADP. Biochemistry. 44: 2441-8. PMID 15709756 DOI: 10.1021/Bi047694Z |
0.422 |
|
| 2004 |
Bandyopadhyay S, Allison WS. GammaM23K, gammaM232K, and gammaL77K single substitutions in the TF1-ATPase lower ATPase activity by disrupting a cluster of hydrophobic side chains. Biochemistry. 43: 9495-501. PMID 15260492 DOI: 10.1021/Bi0493012 |
0.396 |
|
| 2004 |
Bandyopadhyay S, Allison WS. The ionic track in the F1-ATPase from the thermophilic Bacillus PS3. Biochemistry. 43: 2533-40. PMID 14992590 DOI: 10.1021/Bi036058I |
0.435 |
|
| 2002 |
Bandyopadhyay S, Valder CR, Huynh HG, Ren H, Allison WS. The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site. Biochemistry. 41: 14421-9. PMID 12450409 DOI: 10.1021/Bi026243G |
0.431 |
|
| 2002 |
Bandyopadhyay S, Ren H, Wang CS, Allison WS. The (alpha F(357)C)(3)(beta R(372)C)(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 has altered ATPase activity after cross-linking alpha and beta subunits at noncatalytic site interfaces. Biochemistry. 41: 3226-34. PMID 11863461 DOI: 10.1021/Bi0120291 |
0.451 |
|
| 2002 |
Dong K, Ren H, Allison WS. The fluorescence spectrum of the introduced tryptophans in the alpha 3(beta F155W)3gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 cannot be used to distinguish between the number of nucleoside di- and triphosphates bound to catalytic sites. The Journal of Biological Chemistry. 277: 9540-7. PMID 11779852 DOI: 10.1074/Jbc.M106911200 |
0.409 |
|
| 2000 |
Allison WS, Ren H, Dou C. Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F(1)-ATPases: are they ground-state or transition-state analogs? Journal of Bioenergetics and Biomembranes. 32: 531-8. PMID 15254389 DOI: 10.1023/A:1005677310791 |
0.397 |
|
| 2000 |
Ren H, Allison WS. On what makes the gamma subunit spin during ATP hydrolysis by F(1). Biochimica Et Biophysica Acta. 1458: 221-33. PMID 10838039 DOI: 10.1016/S0005-2728(00)00075-X |
0.328 |
|
| 2000 |
Ren H, Allison WS. Substitution of betaGlu(201) in the alpha(3)beta(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. The Journal of Biological Chemistry. 275: 10057-63. PMID 10744684 DOI: 10.1074/Jbc.275.14.10057 |
0.45 |
|
| 1999 |
Grodsky NB, Allison WS. The adenine pocket of a single catalytic site is derivatized when the bovine heart mitochondrial F1-ATPase is photoinactivated with 4-amino-1-octylquinaldinium. Cell Biochemistry and Biophysics. 31: 285-94. PMID 10736751 DOI: 10.1007/Bf02738243 |
0.44 |
|
| 1999 |
Ren H, Dou C, Stelzer MS, Allison WS. Oxidation of the alpha(3)(betaD311C/R333C)(3)gamma subcomplex of the thermophilic Bacillus PS3 F(1)-ATPase indicates that only two beta subunits can exist in the closed conformation simultaneously. The Journal of Biological Chemistry. 274: 31366-72. PMID 10531337 DOI: 10.1074/Jbc.274.44.31366 |
0.428 |
|
| 1998 |
Dou C, Fortes PA, Allison WS. The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP. Biochemistry. 37: 16757-64. PMID 9843446 DOI: 10.1021/bi981717q |
0.333 |
|
| 1998 |
Grodsky NB, Dou C, Allison WS. Mutations in the nucleotide binding domain of the alpha subunits of the F1-ATPase from thermophilic Bacillus PS3 that affect cross-talk between nucleotide binding sites. Biochemistry. 37: 1007-14. PMID 9454591 DOI: 10.1021/Bi972349D |
0.392 |
|
| 1997 |
Ren HM, Allison WS. Photoinactivation of the F1-ATPase from spinach chloroplasts by dequalinium is accompanied by derivatization of methionine beta183. The Journal of Biological Chemistry. 272: 32294-300. PMID 9405435 DOI: 10.1074/Jbc.272.51.32294 |
0.384 |
|
| 1997 |
Dou C, Grodsky NB, Matsui T, Yoshida M, Allison WS. ADP-fluoroaluminate complexes are formed cooperatively at two catalytic sites of wild-type and mutant alpha3beta3gamma subcomplexes of the F1-ATPase from the thermophilic Bacillus PS3. Biochemistry. 36: 3719-27. PMID 9132025 DOI: 10.1021/Bi962353+ |
0.397 |
|
| 1997 |
Matsui T, Muneyuki E, Honda M, Allison WS, Dou C, Yoshida M. Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site. The Journal of Biological Chemistry. 272: 8215-21. PMID 9079639 DOI: 10.1074/Jbc.272.13.8215 |
0.417 |
|
| 1996 |
Allison WS, Jault JM, Dou C, Grodsky NB. Does the gamma subunit move to an abortive position of ATP hydrolysis when the F1.ADP.Mg complex isomerizes to the inactive F1*.ADP.Mg complex? Journal of Bioenergetics and Biomembranes. 28: 433-8. PMID 8951090 DOI: 10.1007/Bf02113985 |
0.452 |
|
| 1996 |
Jault JM, Dou C, Grodsky NB, Matsui T, Yoshida M, Allison WS. The alpha3beta3gamma subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the betaT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover. The Journal of Biological Chemistry. 271: 28818-24. PMID 8910526 DOI: 10.1074/Jbc.271.46.28818 |
0.358 |
|
| 1996 |
Matsui T, Jault JM, Allison WS, Yoshida M. An attempt to convert noncatalytic nucleotide binding site of F1-ATPase to the catalytic site: hydrolysis of tethered ATP by mutated alpha subunits in the enzyme. Biochemical and Biophysical Research Communications. 220: 94-7. PMID 8602864 DOI: 10.1006/Bbrc.1996.0362 |
0.453 |
|
| 1995 |
Jault JM, Matsui T, Jault FM, Kaibara C, Muneyuki E, Yoshida M, Kagawa Y, Allison WS. The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites. Biochemistry. 34: 16412-8. PMID 8845368 DOI: 10.1021/Bi00050A023 |
0.397 |
|
| 1995 |
Allison WS, Jault JM, Grodsky NB, Dou C. A model for ATP hydrolysis catalysed by F1-ATPases based on kinetic and structural considerations. Biochemical Society Transactions. 23: 752-6. PMID 8654831 DOI: 10.1042/Bst0230752 |
0.35 |
|
| 1994 |
Paik SR, Jault JM, Allison WS. Inhibition and inactivation of the F1 adenosinetriphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide. Biochemistry. 33: 126-33. PMID 8286329 DOI: 10.1021/Bi00167A016 |
0.37 |
|
| 1994 |
Jault JM, Allison WS. Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP. The Journal of Biological Chemistry. 269: 319-25. PMID 8276813 |
0.351 |
|
| 1994 |
Jault JM, Kaibara C, Yoshida M, Garrod S, Allison WS. Probing the specificity of nucleotide binding to the F1-ATPase from thermophilic Bacillus PS3 and its isolated alpha and beta subunits with 2-N3-[beta, gamma-32P]ATP. Archives of Biochemistry and Biophysics. 310: 282-8. PMID 8161217 DOI: 10.1006/Abbi.1994.1168 |
0.418 |
|
| 1994 |
Jault JM, Allison WS. ADP tethered to tyrosine-beta 345 at the catalytic site of the bovine heart F1-ATPase is converted to tethered AMP by Mg(2+)-dependent hydrolysis when the enzyme is photoinactivated with 2-N3-ADP. Febs Letters. 347: 13-6. PMID 8013653 DOI: 10.1016/0014-5793(94)00497-8 |
0.403 |
|
| 1994 |
Jault JM, Paik SR, Grodsky NB, Allison WS. Lowered temperature or binding of pyrophosphate to sites for noncatalytic nucleotides modulates the ATPase activity of the beef heart mitochondrial F1-ATPase by decreasing the affinity of a catalytic site for inhibitory MgADP. Biochemistry. 33: 14979-85. PMID 7999754 DOI: 10.1021/Bi00254A005 |
0.394 |
|
| 1994 |
Muneyuki E, Hisabori T, Allison WS, Jault JM, Sasayama T, Yoshida M. Catalytic cooperativity of beef heart mitochondrial F1-ATPase revealed by using 2',3'-O-(2,4,6-trinitrophenyl)-ATP as a substrate; an indication of mutually activating catalytic sites. Biochimica Et Biophysica Acta. 1188: 108-16. PMID 7947899 DOI: 10.1016/0005-2728(94)90028-0 |
0.436 |
|
| 1993 |
Zhuo S, Paik SR, Register JA, Allison WS. Photoinactivation of the bovine heart mitochondrial F1-ATPase by [14C]dequalinium cross-links phenylalanine-403 or phenylalanine-406 of an alpha subunit to a site or sites contained within residues 440-459 of a beta subunit. Biochemistry. 32: 2219-27. PMID 8443163 DOI: 10.1021/Bi00060A013 |
0.43 |
|
| 1993 |
Kasho VN, Allison WS, Boyer PD. Study of the mechanism of MF1 ATPase inhibition by fluorosulfonylbenzoyl inosine, quinacrine mustard, and efrapeptin using intermediate 18O exchange as a probe. Archives of Biochemistry and Biophysics. 300: 293-301. PMID 8424665 DOI: 10.1006/abbi.1993.1041 |
0.343 |
|
| 1993 |
Jault JM, Divita G, Allison WS, Di Pietro A. Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 beta-subunit increases catalytic site interaction with GDP and IDP and produces negative cooperativity of GTP and ITP hydrolysis. The Journal of Biological Chemistry. 268: 20762-7. PMID 8407901 |
0.335 |
|
| 1993 |
Odaka M, Kiribuchi K, Allison WS, Yoshida M. In vivo affinity label of a protein expressed in Escherichia coli. Coenzyme A occupied the AT(D)P binding site of the mutant F1-ATPase beta subunit (Y307C) through a disulfide bond. Febs Letters. 336: 231-5. PMID 8262235 DOI: 10.1016/0014-5793(93)80809-9 |
0.401 |
|
| 1993 |
Paik SR, Yokoyama K, Yoshida M, Ohta T, Kagawa Y, Allison WS. The TF1-ATPase and ATPase activities of assembled alpha 3 beta 3 gamma, alpha 3 beta 3 gamma delta, and alpha 3 beta 3 gamma epsilon complexes are stimulated by low and inhibited by high concentrations of rhodamine 6G whereas the dye only inhibits the alpha 3 beta 3, and alpha 3 beta 3 delta complexes. Journal of Bioenergetics and Biomembranes. 25: 679-84. PMID 8144495 DOI: 10.1007/Bf00770254 |
0.37 |
|
| 1992 |
Mileykovskaya EI, Kormer SS, Allison WS. Significant quantities of endogenous GDP and ADP are present on catalytic sites of the F1-ATPase isolated from M. lysodeikticus in the absence of added nucleotides. Biochimica Et Biophysica Acta. 1099: 219-25. PMID 1532327 DOI: 10.1016/0005-2728(92)90030-6 |
0.461 |
|
| 1992 |
Allison WS, Jault JM, Zhuo S, Paik SR. Functional sites in F1-ATPases: location and interactions. Journal of Bioenergetics and Biomembranes. 24: 469-77. PMID 1429541 DOI: 10.1007/Bf00762364 |
0.421 |
|
| 1992 |
Noer AS, Marzuki S, Allison WS. Antipeptide antibodies to the carboxy terminal and the DCCD binding region of the human mitochondrial ATP synthase beta-subunit. Biochimica Et Biophysica Acta. 1099: 123-30. PMID 1371933 DOI: 10.1016/0005-2728(92)90208-J |
0.422 |
|
| 1991 |
Muneyuki E, Yoshida M, Bullough DA, Allison WS. Heterogeneous hydrolysis of substoichiometric ATP by the F1-ATPase from Escherichia coli. Biochimica Et Biophysica Acta. 1058: 304-11. PMID 1828699 DOI: 10.1016/S0005-2728(05)80251-8 |
0.449 |
|
| 1991 |
Bullough DA, Zhuo SQ, Allison WS. Separate beta subunits are derivatized with 14C and 3H when the bovine heart mitochondrial F1-ATPase is doubly labeled with 7-chloro-4-nitro[14C]benzofurazan and 5'-p-fluorosulfonylbenzoyl[3H]inosine. Biochimica Et Biophysica Acta. 1057: 208-14. PMID 1826610 DOI: 10.1016/S0005-2728(05)80103-3 |
0.411 |
|
| 1990 |
Verburg JG, Allison WS. Tyrosine alpha 244 is derivatized when the bovine heart mitochondrial F1-ATPase is inactivated with 5'-p-fluorosulfonylbenzoylethenoadenosine. The Journal of Biological Chemistry. 265: 8065-74. PMID 2139876 |
0.375 |
|
| 1989 |
Bullough DA, Ceccarelli EA, Roise D, Allison WS. Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides. Biochimica Et Biophysica Acta. 975: 377-83. PMID 2527062 DOI: 10.1016/S0005-2728(89)80346-9 |
0.356 |
|
| 1989 |
Ceccarelli EA, Verburg JG, Zhuo SQ, Allison WS. Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan. Archives of Biochemistry and Biophysics. 272: 400-11. PMID 2526617 DOI: 10.1016/0003-9861(89)90234-8 |
0.444 |
|
| 1989 |
Bullough DA, Ceccarelli EA, Verburg JG, Allison WS. Localization of sites modified during inactivation of the bovine heart mitochondrial F1-ATPase by quinacrine mustard using [3H]aniline as a probe. The Journal of Biological Chemistry. 264: 9155-63. PMID 2524484 |
0.395 |
|
| 1988 |
Bullough DA, Brown EL, Saario JD, Allison WS. On the location and function of the noncatalytic sites on the bovine heart mitochondrial F1-ATPase. The Journal of Biological Chemistry. 263: 14053-60. PMID 2902078 |
0.342 |
|
| 1988 |
Bullough DA, Allison WS. Inactivation of the F1-ATPase from the thermophilic bacterium PS3 by 5'-p-fluorosulfonylbenzoylinosine at 65 degrees C is accompanied by modification of beta-tyrosine-364. Biochimica Et Biophysica Acta. 934: 397-400. PMID 2899441 DOI: 10.1016/0005-2728(88)90097-7 |
0.338 |
|
| 1987 |
Bullough DA, Verburg JG, Yoshida M, Allison WS. Evidence for functional heterogeneity among the catalytic sites of the bovine heart mitochondrial F1-ATPase. The Journal of Biological Chemistry. 262: 11675-83. PMID 2887560 |
0.349 |
|
| 1986 |
Allison WS, Bullough DA, Andrews WW. Identification of essential residues in the F1-ATPases by chemical modification. Methods in Enzymology. 126: 741-61. PMID 2908480 DOI: 10.1016/S0076-6879(86)26074-7 |
0.39 |
|
| 1986 |
Bullough DA, Allison WS. Inactivation of the bovine heart mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyl[3H]inosine is accompanied by modification of tyrosine 345 in a single beta subunit. The Journal of Biological Chemistry. 261: 14171-7. PMID 2876984 |
0.369 |
|
| 1986 |
Bullough DA, Allison WS. Three copies of the beta subunit must be modified to achieve complete inactivation of the bovine mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyladenosine. The Journal of Biological Chemistry. 261: 5722-30. PMID 2871017 |
0.302 |
|
| 1986 |
Yoshida M, Allison WS. Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic bacterium, PS3. The Journal of Biological Chemistry. 261: 5714-21. PMID 2871016 |
0.336 |
|
| 1986 |
Verburg JG, Yoshida M, Allison WS. The use of dithionite reduction to identify the essential tyrosine residue in the F1-ATPase from the thermophilic bacterium, PS3, that reacts with 7-chloro-4-nitrobenzofurazan. Archives of Biochemistry and Biophysics. 245: 8-13. PMID 2868697 DOI: 10.1016/0003-9861(86)90184-0 |
0.38 |
|
| 1986 |
Bullough DA, Yoshida M, Allison WS. Sequence of the radioactive tryptic peptide obtained after inactivating the F1-ATPase of the thermophilic bacterium PS3 with 5'-p-fluorosulfonylbenzoyl[3H]adenosine at 65 degrees C. Archives of Biochemistry and Biophysics. 244: 865-71. PMID 2868693 DOI: 10.1016/0003-9861(86)90656-9 |
0.438 |
|
| 1985 |
Laikind PK, Hill FC, Allison WS. The use of [3H]aniline to identify the essential carboxyl group in the bovine mitochondrial F1-ATPase that reacts with 1-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline. Archives of Biochemistry and Biophysics. 240: 904-20. PMID 2862844 DOI: 10.1016/0003-9861(85)90100-6 |
0.441 |
|
| 1985 |
Bullough DA, Kwan M, Laikind PK, Yoshida M, Allison WS. The varied responses of different F1-ATPases to chlorpromazine. Archives of Biochemistry and Biophysics. 236: 567-75. PMID 2857548 DOI: 10.1016/0003-9861(85)90660-5 |
0.355 |
|
| 1984 |
Andrews WW, Hill FC, Allison WS. Identification of the lysine residue to which the 4-nitrobenzofurazan group migrates after the bovine mitochondrial F1-ATPase is inactivated with 7-chloro-4-nitro[14C]benzofurazan. The Journal of Biological Chemistry. 259: 14378-82. PMID 6238961 |
0.343 |
|
| 1984 |
Andrews WW, Yoshida M, Hill FC, Allison WS. Identification of an essential lysine residue in the beta subunit of the F1-ATPase from the thermophilic bacterium, PS3, using 7-chloro-4-nitro[14C]benzofurazan. Biochemical and Biophysical Research Communications. 123: 1040-6. PMID 6237650 DOI: 10.1016/S0006-291X(84)80238-7 |
0.409 |
|
| 1984 |
Andrews WW, Hill FC, Allison WS. Identification of the essential tyrosine residue in the beta subunit of bovine heart mitochondrial F1-ATPase that is modified by 7-chloro-4-nitro[14C]benzofurazan. The Journal of Biological Chemistry. 259: 8219-25. PMID 6234310 |
0.36 |
|
| 1983 |
Mai MS, Allison WS. Inhibition of an oligomycin-sensitive ATPase by cationic dyes, some of which are atypical uncouplers of intact mitochondria. Archives of Biochemistry and Biophysics. 221: 467-76. PMID 6188413 DOI: 10.1016/0003-9861(83)90165-0 |
0.321 |
|
| 1982 |
Laikind PK, Goldenberg TM, Allison WS. On the mechanism of inhibition of the bovine heart F1-ATPase by local anesthetics. Biochemical and Biophysical Research Communications. 109: 423-7. PMID 6217817 DOI: 10.1016/0006-291X(82)91738-7 |
0.406 |
|
| 1981 |
Andrews WW, Allison WS. 1-fluoro-2, 4-dinitrobenzene modifies a tyrosine residue when it inactivates the bovine mitochondrial F(1)-ATPase. Biochemical and Biophysical Research Communications. 99: 813-9. PMID 6454415 DOI: 10.1016/0006-291X(81)91237-7 |
0.431 |
|
| 1981 |
Esch FS, Böhlen P, Otsuka AS, Yoshida M, Allison WS. Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit. The Journal of Biological Chemistry. 256: 9084-9. PMID 6114957 |
0.367 |
|
| 1979 |
Esch FS, Allison WS. On the subunit stoichiometry of the F1-ATPase and the sites in it that react specifically with p-fluorosulfonylbenzoyl-5'-adenosine. The Journal of Biological Chemistry. 254: 10740-6. PMID 159296 |
0.364 |
|
| 1979 |
Esch FS, Allison WS. A three-step procedure for the isolation of peptides derived from adenine nucleotide binding sites of enzymes labeled with p-fluorosulfonyl [14C]benzoyl-5'-adenosine. Analytical Biochemistry. 95: 39-43. PMID 158993 DOI: 10.1016/0003-2697(79)90182-9 |
0.364 |
|
| 1978 |
Lewis RV, Allison WS. The use of photoactivated hetero-bifunctional reagents to cross-link cytochrome c to proteins that bind it by electrostatic interactions. Archives of Biochemistry and Biophysics. 190: 163-73. PMID 213028 DOI: 10.1016/0003-9861(78)90264-3 |
0.317 |
|
| 1978 |
Esch FS, Allison WS. Identification of a tyrosine residue at a nucleotide binding site in the beta subunit of the mitochondrial ATPase with p-fluorosulfonyl[14C]-benzoyl-5'-adenosine. The Journal of Biological Chemistry. 253: 6100-6. PMID 150416 |
0.38 |
|
| 1978 |
You Ks, Arnold LJ, Allison WS, Kaplan NO. Enzyme stereospecificities for nicotinamide nucleotides Trends in Biochemical Sciences. 3: 265-268. DOI: 10.1016/S0968-0004(78)95849-8 |
0.539 |
|
| 1977 |
Lewis RV, Roberts MF, Dennis EA, Allison WS. Photoactivated heterobifunctional cross-linking reagents which demonstrate the aggregation state of phospholipase A2. Biochemistry. 16: 5650-4. PMID 921957 DOI: 10.1021/Bi00644A041 |
0.319 |
|
| 1976 |
Arnold LJ, You K, Allison WS, Kaplan NO. Determination of the hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked oxidoreductases by proton magnetic resonance. Biochemistry. 15: 4844-9. PMID 186097 DOI: 10.1021/Bi00667A014 |
0.555 |
|
| 1975 |
Taylor SS, Allison WS, Kaplan NO. The amino acid sequence of the tryptic peptides isolated from dogfish M4 lactate dehydrogenase. The Journal of Biological Chemistry. 250: 8740-7. PMID 1184589 |
0.529 |
|
| 1975 |
You K-S, Benitez LV, McConachie WA, Allison WS. The conversion of glyceraldehyde-3-phosphate dehydrogenase to an acylphosphatase by trinitroglycerin and inactivation of this activity by azide and ascorbate. Biochimica Et Biophysica Acta. 384: 317-30. PMID 235996 DOI: 10.1016/0005-2744(75)90033-9 |
0.42 |
|
| 1973 |
Allison WS, Swain LC. The inactivation of papain and glyceraldehyde-3-phosphate dehydrogenase by phenyldiimide. Archives of Biochemistry and Biophysics. 155: 405-10. PMID 4735851 DOI: 10.1016/0003-9861(73)90130-6 |
0.392 |
|
| 1973 |
Allison WS, Benitez LV, Johnson CL. The formation of a protein sulfenamide during the inactivation of the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by benzylamine. Biochemical and Biophysical Research Communications. 52: 1403-9. PMID 4717755 DOI: 10.1016/0006-291X(73)90657-8 |
0.413 |
|
| 1973 |
Taylor SS, Oxley SS, Allison WS, Kaplan NO. Aminoacid sequence of dogfish M4 lactate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 70: 1790-3. PMID 4515938 DOI: 10.1073/Pnas.70.6.1790 |
0.586 |
|
| 1973 |
Benitez LV, Allison WS. The mechanism of the diaphorase reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase. Archives of Biochemistry and Biophysics. 159: 89-96. PMID 4361558 DOI: 10.1016/0003-9861(73)90432-3 |
0.384 |
|
| 1973 |
Allison WS, Swain LC, Tracy SM, Benitez LV. The inactivation of lactoperoxidase and the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by phenlyhydrazine and phenyldiimide. Archives of Biochemistry and Biophysics. 155: 400-4. PMID 4350253 DOI: 10.1016/0003-9861(73)90129-X |
0.375 |
|
| 1973 |
Adams MJ, Buehner M, Chandrasekhar K, Ford GC, Hackert ML, Liljas A, Rossmann MG, Smiley IE, Allison WS, Everse J, Kaplan NO, Taylor SS. Structure-function relationships in lactate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 70: 1968-72. PMID 4146647 DOI: 10.1073/Pnas.70.7.1968 |
0.576 |
|
| 1972 |
Allison WS, Benitez LV. An adenosine triphosphate-phosphate exchange catalyzed by a soluble enzyme couple inhibited by uncouplers of oxidative phosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 69: 3004-8. PMID 4507619 DOI: 10.1073/Pnas.69.10.3004 |
0.367 |
|
| 1969 |
Allison WS, Admiraal J, Kaplan NO. The subunits of dogfish M4 lactic dehydrogenase. The Journal of Biological Chemistry. 244: 4743-9. PMID 5808514 |
0.455 |
|
| 1964 |
WILSON AC, KAPLAN NO, LEVINE L, PESCE A, REICHLIN M, ALLISON WS. EVOLUTION OF LACTIC DEHYDROGENASES. Federation Proceedings. 23: 1258-66. PMID 14236134 |
0.543 |
|
| 1964 |
ALLISON WS, KAPLAN NO. EFFECT OF TETRATHIONATE ON THE STABILITY AND IMMUNOLOGICAL PROPERTIES OF MUSCLE TRIOSEPHOSPHATE DEHYDROGENASES. Biochemistry. 3: 1792-800. PMID 14235350 DOI: 10.1021/Bi00899A036 |
0.44 |
|
| 1964 |
ALLISON WS, KAPLAN NO. THE COMPARATIVE ENZYMOLOGY OF TRIOSEPHOSPHATE DEHYDROGENASE. The Journal of Biological Chemistry. 239: 2140-52. PMID 14209940 |
0.485 |
|
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