W. Allison

发表

THE COMPARATIVE ENZYMOLOGY OF TRIOSEPHOSPHATE DEHYDROGENASE.

N. Kaplan, W. Allison, 1964, The Journal of biological chemistry.

Photoinactivation of the F1-ATPase from Spinach Chloroplasts by Dequalinium Is Accompanied by Derivatization of Methionine β183*

W. Allison, H. Ren, 1997, The Journal of Biological Chemistry.

Inhibition and inactivation of the F1 adenosinetriphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide.

J. Jault, W. Allison, S. Paik, 1994, Biochemistry.

The amino acid sequence of the tryptic peptides isolated from dogfish M4 lactate dehydrogenase.

S. Taylor, N. Kaplan, W. Allison, 1975, The Journal of biological chemistry.

The TF1-ATPase and ATPase activities of assembled α3β3γ, α3β3γδ, and α3β3γε complexes are stimulated by low and inhibited by high concentrations of rhodamine 6G whereas the dye only inhibits the α3β3, and α3β3δ complexes

Masasuke Yoshida, Y. Kagawa, K. Yokoyama, 1993, Journal of Bioenergetics and Biomembranes.

Inhibition and photoinactivation of the bovine heart mitochondrial F1-ATPase by the cytotoxic agent, dequalinium.

W. Allison, S. Zhuo, 1988, Biochemical and biophysical research communications.

Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan.

W. Allison, J. Verburg, S. Zhuo, 1989, Archives of biochemistry and biophysics.

Determination of the hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked oxidoreductases by proton magnetic resonance.

N. Kaplan, W. Allison, L. J. Arnold, 1976, Biochemistry.

The inactivation of papain and glyceraldehyde-3-phosphate dehydrogenase by phenyldiimide.

W. Allison, L. Swain, 1973, Archives of biochemistry and biophysics.

The use of photoactivated hetero-bifunctional reagents to cross-link cytochrome c to proteins that bind it by electrostatic interactions.

R. Lewis, W. Allison, 1978, Archives of biochemistry and biophysics.

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.

M. Yoshida, W. Allison, P. Böhlen, 1981, The Journal of biological chemistry.

Inhibitory Mg-ADP—Fluoroaluminate Complexes Bound to Catalytic Sites of F1-ATPases: Are They Ground-State or Transition-State Analogs?

W. Allison, H. Ren, C. Dou, 2000, Journal of bioenergetics and biomembranes.

Does the γ subunit move to an abortive position for ATP hydrolysis when the F1·ADP·Mg complex isomerizes to the inactive F1*·ADP·Mg complex?

N. Grodsky, W. Allison, C. Dou, 1996, Journal of bioenergetics and biomembranes.

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.

N. Grodsky, J. Jault, W. Allison, 1994, Biochemistry.

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.

E. Muneyuki, M. Yoshida, T. Hisabori, 1994, Biochimica et biophysica acta.

Tyrosine alpha 244 is derivatized when the bovine heart mitochondrial F1-ATPase is inactivated with 5'-p-fluorosulfonylbenzoylethenoadenosine.

W. Allison, J. Verburg, 1990, The Journal of biological chemistry.

The formation of a protein sulfenamide during the inactivation of the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by benzylamine.

C. L. Johnson, W. Allison, L. Benitez, 1973, Biochemical and biophysical research communications.

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.

W. Allison, H. Ren, 2000, The Journal of biological chemistry.

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.

W. Allison, S. Zhuo, D. Bullough, 1991, Biochimica et biophysica acta.

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.

M. Yoshida, W. Allison, J. Verburg, 1986, Archives of biochemistry and biophysics.

Identification of essential residues in the F1-ATPases by chemical modification.

W. Allison, D. Bullough, W. W. Andrews, 1986, Methods in enzymology.

1-fluoro-2, 4-dinitrobenzene modifies a tyrosine residue when it inactivates the bovine mitochondrial F(1)-ATPase.

W. Allison, W. W. Andrews, 1981, Biochemical and biophysical research communications.

On the subunit stoichiometry of the F1-ATPase and the sites in it that react specifically with p-fluorosulfonylbenzoyl-5'-adenosine.

W. Allison, F. Esch, 1979, The Journal of biological chemistry.

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.

P. A. Fortes, W. Allison, C. Dou, 1998, Biochemistry.

Enzyme stereospecificities for nicotinamide nucleotides

N. Kaplan, W. Allison, L. J. Arnold, 1978 .

In vivo affinity label of a protein expressed in Escherichia coli

M. Yoshida, W. Allison, M. Odaka, 1993, FEBS letters.

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.

W. Allison, F. Hill, P. Laikind, 1985, Archives of biochemistry and biophysics.

The varied responses of different F1-ATPases to chlorpromazine.

M. Yoshida, W. Allison, D. Bullough, 1985, Archives of biochemistry and biophysics.

The mechanism of inactivation of glyceraldehyde 3-phosphate dehydrogenase by tetrathionate, o-iodosobenzoate, and iodine monochloride.

W. Allison, D. Parker, 1969, The Journal of biological chemistry.

The adenine pocket of a single catalytic site is derivatized when the bovine heart mitochondrial F1-ATPase is photoinactivated with 4-amino-1-octylquinaldinium

N. Grodsky, W. Allison, 1999, Cell Biochemistry and Biophysics.

The reaction of formaldehyde with nucleotides and T2 bacteriophage DNA.

L. Grossman, W. Allison, S. Levine, 1961, Journal of molecular biology.

Studies on the hydrogen-transfer reactions catalyzed by pyridine nucleotide linked dehydrogenases.

W. Allison, H. B. White, M. Connors, 1971, Biochemistry.

The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins.

W. Allison, L. Benitez, 1974, The Journal of biological chemistry.

A procedure for the synthesis of p-fluorosulfonyl[14C]-benzoyl-5'-adenosine with [14C] in the benzoyl moiety.

W. Allison, F. Esch, 1978, Analytical biochemistry.

Formation and reactions of sulfenic acids in proteins

W. Allison, 1976 .

The conversion of glyceraldehyde-3-phosphate dehydrogenase to an acylphosphatase by trinitroglycerin and inactivation of this activity by azide and ascorbate.

W. Allison, L. Benitez, You K-S, 1975, Biochimica et biophysica acta.

Structure-function relationships in lactate dehydrogenase.

S. Taylor, N. Kaplan, M. Rossmann, 1973, Proceedings of the National Academy of Sciences of the United States of America.

EVOLUTION OF LACTIC DEHYDROGENASES.

N. Kaplan, A. Wilson, M. Reichlin, 1964, Federation proceedings.

The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover*

Masasuke Yoshida, N. Grodsky, J. Jault, 1996, The Journal of Biological Chemistry.

ADP tethered to tyrosine‐β345 at the catalytic site of the bovine heart F1‐ATPase is converted to tethered AMP by Mg2+‐dependent hydrolysis when the enzyme is photoinactivated with 2‐N3‐ADP

J. Jault, W. Allison, 1994, FEBS letters.

Aminoacid sequence of dogfish M4 lactate dehydrogenase.

S. Taylor, N. Kaplan, W. Allison, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Identification of an essential glutamic acid residue in the beta subunit of the adenosine triphosphatase from the thermophilic bacterium PS3.

M. Yoshida, J. Poser, W. Allison, 1981, The Journal of biological chemistry.

STRUCTURE AND EVOLUTION OF TRIOSE PHOSPHATE AND LACTATE DEHYDROGENASES *

W. Allison, 1968, Annals of the New York Academy of Sciences.

The activation and inactivation of the acyl phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase.

W. Allison, M. J. Connors, 1970, Archives of biochemistry and biophysics.

Antipeptide antibodies to the carboxy terminal and the DCCD binding region of the human mitochondrial ATP synthase beta-subunit.

S. Marzuki, W. Allison, A. Noer, 1992, Biochimica et biophysica acta.

Photoactivated heterobifunctional cross-linking reagents which demonstrate the aggregation state of phospholipase A2.

E. Dennis, M. Roberts, R. Lewis, 1977, Biochemistry.

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.

W. Allison, F. Esch, 1978, The Journal of biological chemistry.

Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides.

E. Ceccarelli, W. Allison, D. Roise, 1989, Biochimica et biophysica acta.

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.

W. Allison, F. Hill, W. W. Andrews, 1984, The Journal of biological chemistry.

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.

W S Allison, W. Allison, F. Hill, 1984, The Journal of biological chemistry.

On the mechanism of inhibition of the bovine heart F1-ATPase by local anesthetics.

W. Allison, P. Laikind, T. M. Goldenberg, 1982, Biochemical and biophysical research communications.

Functional sites in F1-ATPases: Location and interactions

S. Zhuo, J. Jault, W. Allison, 1992, Journal of bioenergetics and biomembranes.

The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide.

M. Yoshida, M. Futai, W. Allison, 1982, The Journal of biological chemistry.

The Fluorescence Spectrum of the Introduced Tryptophans in the α3(βF155W)3γ 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*

W. Allison, H. Ren, K. Dong, 2002, The Journal of Biological Chemistry.

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.

W. Allison, D. Bullough, 1986, The Journal of biological chemistry.

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.

M. Yoshida, W. Allison, F. Hill, 1984, Biochemical and biophysical research communications.

Inactivation of the F1-ATPase from the thermophilic bacterium PS3 by 5′-p-fluorosulfonylbenzoylinosine at 65° C is accompanied by modification of β-tyrosine-364

W. Allison, D. Bullough, 1988 .

The short, swift time of gods on earth : the Hohokam chronicles

William Willard, W. Allison, D. Bahr, 1994 .

Three copies of the beta subunit must be modified to achieve complete inactivation of the bovine mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyladenosine.

W. Allison, D. Bullough, 1986, The Journal of biological chemistry.

Evidence for functional heterogeneity among the catalytic sites of the bovine heart mitochondrial F1-ATPase.

W S Allison, M. Yoshida, W. Allison, 1987, The Journal of biological chemistry.

On what makes the gamma subunit spin during ATP hydrolysis by F(1).

W S Allison, W. Allison, H. Ren, 2000, Biochimica et biophysica acta.

Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for Nucleotides*

W. Allison, H. Ren, 2000, The Journal of Biological Chemistry.

Oxidation of the α3(βD311C/R333C)3γ Subcomplex of the Thermophilic Bacillus PS3 F1-ATPase Indicates That Only Two β Subunits Can Exist in the Closed Conformation Simultaneously*

W. Allison, H. Ren, C. Dou, 1999, The Journal of Biological Chemistry.

Catalytic Activity of the α3β3γ Complex of F1-ATPase without Noncatalytic Nucleotide Binding Site*

Masasuke Yoshida, E. Muneyuki, W. Allison, 1997, The Journal of Biological Chemistry.

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.

W. Allison, S. Paik, S. Zhuo, 1993, Biochemistry.

[43] Glyceraldehyde 3-phosphate dehydrogenase—crystalline

W. Allison, 1966 .

Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic bacterium, PS3.

M. Yoshida, W. Allison, 1986, The Journal of biological chemistry.

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.

A. di Pietro, G. Divita, J. Jault, 1993, The Journal of biological chemistry.

Immunochemical Studies on the Components of the Pepsinogen System

W. Allison, L. Levine, H. van Vunakis, 1963, The Journal of general physiology.

EFFECT OF TETRATHIONATE ON THE STABILITY AND IMMUNOLOGICAL PROPERTIES OF MUSCLE TRIOSEPHOSPHATE DEHYDROGENASES.

N. Kaplan, W. Allison, 1964, Biochemistry.

Inhibition of an oligomycin-sensitive ATPase by cationic dyes, some of which are atypical uncouplers of intact mitochondria.

W. Allison, M. Mai, 1983, Archives of biochemistry and biophysics.

Heterogeneous hydrolysis of substoichiometric ATP by the F1-ATPase from Escherichia coli.

E. Muneyuki, M. Yoshida, W. Allison, 1991, Biochimica et biophysica acta.

F1-ATPase: A Molecular Motor That Hydrolyzes ATP with Sequential Opening and Closing of Catalytic Sites Coupled to Rotation of Its γ Subunit

W. Allison, 1998 .

γM23K, γm232K, and γl77K single substitutions in the TF1-ATPase lower ATPase activity by disrupting a cluster of hydrophobic side chains

S. Bandyopadhyay, W. Allison, 2004 .

Proton-translocating ATPase and lysosomal cystine transport.

A. Jonas, W. Allison, P. Laikind, 1983, The Journal of biological chemistry.

Evidence for direct hydrogen transfer during glyceraldehyde-3-phosphate dehydrogenase catalysis.

W. Allison, D. Parker, M. J. Connors, 1969, Biochemical and biophysical research communications.

The subunits of dogfish M4 lactic dehydrogenase.

N. Kaplan, W. Allison, J. Admiraal, 1969, The Journal of biological chemistry.

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.

E. Mileykovskaya, W. Allison, S. S. Kormer, 1992, Biochimica et biophysica acta.

Probing the Specificity of Nucleotide-Binding to the F1-ATPase from Thermophilic Bacillus Ps3 and Its Isolated α and β Subunits with 2-N3-(β,γ-32P-)ATP

Masasuke Yoshida, J. Jault, W. Allison, 1994 .

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.

M. Yoshida, W. Allison, D. Bullough, 1986, Archives of biochemistry and biophysics.

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.

S. Bandyopadhyay, W. Allison, H. Ren, 2002, Biochemistry.

Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase.

J. Jault, W. Allison, 1993, The Journal of biological chemistry.

An adenosine triphosphate-phosphate exchange catalyzed by a soluble enzyme couple inhibited by uncouplers of oxidative phosphorylation.

W. Allison, L. Benitez, 1972, Proceedings of the National Academy of Sciences of the United States of America.