William S. Allison

2.7k total citations
69 papers, 2.3k citations indexed

About

William S. Allison is a scholar working on Molecular Biology, Clinical Biochemistry and Spectroscopy. According to data from OpenAlex, William S. Allison has authored 69 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 63 papers in Molecular Biology, 10 papers in Clinical Biochemistry and 9 papers in Spectroscopy. Recurrent topics in William S. Allison's work include ATP Synthase and ATPases Research (43 papers), Mitochondrial Function and Pathology (30 papers) and Biochemical and Molecular Research (16 papers). William S. Allison is often cited by papers focused on ATP Synthase and ATPases Research (43 papers), Mitochondrial Function and Pathology (30 papers) and Biochemical and Molecular Research (16 papers). William S. Allison collaborates with scholars based in United States, Japan and France. William S. Allison's co-authors include Nathan O. Kaplan, Lita V. Benitez, Chao Dou, Masasuke Yoshida, Jean‐Michel Jault, Kwan-sa You, Lawrence I. Grossman, Lyle J. Arnold, Tadashi Matsui and Seung R. Paik and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Accounts of Chemical Research.

In The Last Decade

William S. Allison

69 papers receiving 2.1k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
William S. Allison United States	25	1.8k	297	285	243	221	69	2.3k
Bruce M. Anderson United States	25	1.1k 0.6×	273 0.9×	295 1.0×	132 0.5×	221 1.0×	83	1.7k
C.L. Borders United States	26	1.5k 0.8×	319 1.1×	171 0.6×	179 0.7×	220 1.0×	58	2.3k
Jean‐François Biellmann France	23	969 0.5×	367 1.2×	177 0.6×	254 1.0×	435 2.0×	93	1.7k
R. Heiner Schirmer Germany	20	2.1k 1.2×	673 2.3×	372 1.3×	289 1.2×	296 1.3×	28	2.9k
Robert Simoni United States	28	2.5k 1.4×	408 1.4×	447 1.6×	197 0.8×	254 1.1×	209	3.4k
Paul M. Horowitz United States	28	1.5k 0.8×	531 1.8×	421 1.5×	137 0.6×	151 0.7×	114	2.3k
Herman Schreuder Germany	32	1.7k 0.9×	527 1.8×	384 1.3×	149 0.6×	337 1.5×	81	3.1k
Dennis Piszkiewicz United States	21	783 0.4×	350 1.2×	348 1.2×	299 1.2×	306 1.4×	45	1.5k
Eberhard Hofmann Germany	21	1.6k 0.9×	371 1.2×	173 0.6×	186 0.8×	123 0.6×	138	2.4k
J. Paul G. Malthouse Ireland	22	1.2k 0.7×	263 0.9×	145 0.5×	161 0.7×	372 1.7×	100	2.0k

Countries citing papers authored by William S. Allison

Since Specialization

Citations

This map shows the geographic impact of William S. Allison's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by William S. Allison with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites William S. Allison more than expected).

Fields of papers citing papers by William S. Allison

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by William S. Allison. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by William S. Allison. The network helps show where William S. Allison may publish in the future.

Co-authorship network of co-authors of William S. Allison

This figure shows the co-authorship network connecting the top 25 collaborators of William S. Allison. A scholar is included among the top collaborators of William S. Allison based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with William S. Allison. William S. Allison is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Allison, William S. & Immo E. Scheffler. (2009). Mitochondrial electron transport complexes and reactive oxygen species. Academic Press eBooks. 1 indexed citations

Dong, Ken C., et al.. (2002). 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. Journal of Biological Chemistry. 277(11). 9540–9547. 6 indexed citations

Allison, William S., et al.. (2000). Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for Nucleotides. Journal of Biological Chemistry. 275(14). 10057–10063. 20 indexed citations

Allison, William S., et al.. (2000). Inhibitory Mg-ADP—Fluoroaluminate Complexes Bound to Catalytic Sites of F1-ATPases: Are They Ground-State or Transition-State Analogs?. Journal of Bioenergetics and Biomembranes. 32(5). 531–538. 11 indexed citations

Dou, Chao, et al.. (1999). 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. Journal of Biological Chemistry. 274(44). 31366–31372. 11 indexed citations

Grodsky, Neil B. & William S. Allison. (1999). 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(3). 285–294. 2 indexed citations

Allison, William S., et al.. (1997). Photoinactivation of the F1-ATPase from Spinach Chloroplasts by Dequalinium Is Accompanied by Derivatization of Methionine β183. Journal of Biological Chemistry. 272(51). 32294–32300. 7 indexed citations

Jault, Jean‐Michel, Chao Dou, Neil B. Grodsky, et al.. (1996). 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. Journal of Biological Chemistry. 271(46). 28818–28824. 55 indexed citations

Allison, William S., Jean‐Michel Jault, Chao Dou, & Neil B. Grodsky. (1996). 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?. Journal of Bioenergetics and Biomembranes. 28(5). 433–438. 7 indexed citations

10.

Jault, Jean‐Michel, et al.. (1995). 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(50). 16412–16418. 57 indexed citations

11.

Jault, Jean‐Michel, Seung R. Paik, Neil B. Grodsky, & William S. Allison. (1994). 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(50). 14979–14985. 13 indexed citations

12.

Jault, Jean‐Michel & William S. Allison. (1994). 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. FEBS Letters. 347(1). 13–16. 5 indexed citations

13.

Muneyuki, Eiro, et al.. (1994). 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 (BBA) - Bioenergetics. 1188(1-2). 108–116. 5 indexed citations

14.

Zhuo, Shaoqiu, Seung R. Paik, James Register, & William S. Allison. (1993). Photoinactivation of the bovine heart mitochondrial F1-ATPase by [14C]dequalinium crosslinks 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(9). 2219–2227. 18 indexed citations

15.

Odaka, Masafumi, et al.. (1993). In vivo affinity label of a protein expressed in Escherichia coli. FEBS Letters. 336(2). 231–235. 7 indexed citations

16.

Muneyuki, Eiro, et al.. (1991). Heterogeneous hydrolysis of substoichiometric ATP by the F1-ATPase from Escherichia coli. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1058(2). 304–311. 19 indexed citations

17.

Bullough, David A., Eduardo A. Ceccarelli, David Roise, & William S. Allison. (1989). Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 975(3). 377–383. 60 indexed citations

18.

Bullough, David A. & William S. Allison. (1988). 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. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 934(3). 397–400. 6 indexed citations

19.

Bullough, David A., Masasuke Yoshida, & William S. Allison. (1986). 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 °C. Archives of Biochemistry and Biophysics. 244(2). 865–871. 6 indexed citations

20.

Vunakis, Helen Van, et al.. (1963). Immunochemical Studies on the Components of the Pepsinogen System. The Journal of General Physiology. 46(3). 589–604. 33 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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