John M. Whiteley

1.8k total citations
65 papers, 1.4k citations indexed

About

John M. Whiteley is a scholar working on Molecular Biology, Clinical Biochemistry and Cell Biology. According to data from OpenAlex, John M. Whiteley has authored 65 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 20 papers in Clinical Biochemistry and 15 papers in Cell Biology. Recurrent topics in John M. Whiteley's work include Metabolism and Genetic Disorders (20 papers), Biochemical and Molecular Research (15 papers) and Aldose Reductase and Taurine (13 papers). John M. Whiteley is often cited by papers focused on Metabolism and Genetic Disorders (20 papers), Biochemical and Molecular Research (15 papers) and Aldose Reductase and Taurine (13 papers). John M. Whiteley collaborates with scholars based in United States, Canada and Italy. John M. Whiteley's co-authors include Kottayil I. Varughese, James A. Hoch, James Zapf, M. D. Madhusudan, Stephanie Webber, N.-H. Xuong, Barbara C.F. Chu, Matthew M. Skinner, F.M. Huennekens and Nguyen‐Huu Xuong and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Molecular Cell.

In The Last Decade

John M. Whiteley

65 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John M. Whiteley United States	21	961	377	239	177	158	65	1.4k
Giovanna Valentini Italy	22	952 1.0×	254 0.7×	240 1.0×	137 0.8×	65 0.4×	58	1.7k
Stuart M. Arfin United States	25	1.5k 1.6×	376 1.0×	164 0.7×	126 0.7×	55 0.3×	56	1.9k
Faik N. Musayev United States	25	853 0.9×	158 0.4×	338 1.4×	188 1.1×	164 1.0×	64	1.5k
Dale T. Blankenship United States	21	997 1.0×	272 0.7×	98 0.4×	178 1.0×	30 0.2×	26	1.8k
DeWayne Roberts United States	19	1.2k 1.2×	154 0.4×	70 0.3×	61 0.3×	34 0.2×	44	1.7k
Keiichi Hosokawa Japan	21	1.0k 1.1×	320 0.8×	76 0.3×	80 0.5×	44 0.3×	50	1.4k
E. Horjales Mexico	20	752 0.8×	128 0.3×	270 1.1×	212 1.2×	75 0.5×	36	1.2k
Roger F. Sherwood United Kingdom	19	959 1.0×	269 0.7×	105 0.4×	96 0.5×	24 0.2×	38	1.5k
Jean Hickman United States	19	1.0k 1.1×	140 0.4×	118 0.5×	174 1.0×	62 0.4×	25	2.0k
Karsten Theis United States	13	890 0.9×	261 0.7×	136 0.6×	63 0.4×	67 0.4×	20	1.2k

Countries citing papers authored by John M. Whiteley

Since Specialization

Citations

This map shows the geographic impact of John M. Whiteley'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 John M. Whiteley with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites John M. Whiteley more than expected).

Fields of papers citing papers by John M. Whiteley

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John M. Whiteley. 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 John M. Whiteley. The network helps show where John M. Whiteley may publish in the future.

Co-authorship network of co-authors of John M. Whiteley

This figure shows the co-authorship network connecting the top 25 collaborators of John M. Whiteley. A scholar is included among the top collaborators of John M. Whiteley 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 John M. Whiteley. John M. Whiteley 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

Varughese, Kottayil I., M. D. Madhusudan, Xiao Zhen Zhou, John M. Whiteley, & James A. Hoch. (1998). Formation of a Novel Four-Helix Bundle and Molecular Recognition Sites by Dimerization of a Response Regulator Phosphotransferase. Molecular Cell. 2(4). 485–493. 85 indexed citations

Madhusudan, M. D., James Zapf, James A. Hoch, et al.. (1997). A Response Regulatory Protein with the Site of Phosphorylation Blocked by an Arginine Interaction: Crystal Structure of Spo0F from Bacillus subtilis^,. Biochemistry. 36(42). 12739–12745. 40 indexed citations

Leblanc, Éric, et al.. (1997). Pterin and Folate Reduction by theLeishmania tarentolaeH Locus Short-Chain Dehydrogenase/Reductase PTR1. Archives of Biochemistry and Biophysics. 342(2). 197–202. 49 indexed citations

Zhou, Xiao Zhen, John M. Whiteley, J A Hoch, & Kottayil I. Varughese. (1997). Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, spo0B, fromBacillus subtilis. Proteins Structure Function and Bioinformatics. 27(4). 597–600. 12 indexed citations

Zapf, James, et al.. (1996). Phosphoprotein hydrolysis is modulated by amino acid residue 56 in Spo0F apprx P from Bacillus subtilis. The FASEB Journal. 10(6). 1251. 1 indexed citations

Madhusudan, M. D., James Zapf, John M. Whiteley, et al.. (1996). Crystallization and preliminary X-ray analysis of a Y13S mutant of Spo0F fromBacillus subtilis. Acta Crystallographica Section D Biological Crystallography. 52(3). 589–590. 5 indexed citations

Kiefer, Philip M., et al.. (1996). Altered Structural and Mechanistic Properties of Mutant Dihydropteridine Reductases. Journal of Biological Chemistry. 271(7). 3437–3444. 17 indexed citations

Madhusudan, M. D., James Zapf, John M. Whiteley, et al.. (1996). Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis. Structure. 4(6). 679–690. 56 indexed citations

Feher, Victoria A., James Zapf, James A. Hoch, et al.. (1995). ¹H,¹⁵N, and¹³C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of thebacillus subtilisresponse regulator, SpoOF, determined by heteronuclear high-resolution NMR. Protein Science. 4(9). 1801–1814. 29 indexed citations

10.

Varughese, Kottayil I., et al.. (1994). Structural and mechanistic implications of incorporating naturally occurring aberrant mutations of human dihydropteridine reductase into a rat model. International journal of peptide & protein research. 44(3). 278–287. 1 indexed citations

11.

Su, Ying, Matthew M. Skinner, N.-H. Xuong, et al.. (1994). Crystal structure of a monoclinic form of dihydropteridine reductase from rat liver. Acta Crystallographica Section D Biological Crystallography. 50(6). 884–888. 1 indexed citations

12.

Whiteley, John M., et al.. (1993). Dihydropteridine Reductase. Pteridines. 4(4). 159–173. 9 indexed citations

13.

Whiteley, John M., N.-H. Xuong, & Kottayil I. Varughese. (1993). Is Dihydropteridine Reductase an Anomalous Dihydrofolate Reductase, a Flavin-Like Enzyme, or a Short-Chain Dehydrogenase?. Advances in experimental medicine and biology. 338. 115–121. 9 indexed citations

14.

Priest, David G., et al.. (1991). A sensitive radioenzymatic assay for (S)-5-formyltetrahydrofolate. Analytical Biochemistry. 196(2). 284–289. 8 indexed citations

15.

Galivan, John, Myung S. Rhee, David G. Priest, et al.. (1991). The Effect of Methotrexate on the Folate Coenzyme Pools in Human Hepatoma Cells in Culture. Advances in experimental medicine and biology. 309A. 75–78. 1 indexed citations

16.

Matthews, David A., Kottayil I. Varughese, Matthew M. Skinner, et al.. (1991). Role of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase. Archives of Biochemistry and Biophysics. 287(1). 234–239. 8 indexed citations

17.

Webber, Stephanie, John Hural, & John M. Whiteley. (1988). The estimation of dihydropteridine reductase in human blood cells. Clinica Chimica Acta. 173(2). 117–126. 2 indexed citations

18.

Chu, Barbara C.F. & John M. Whiteley. (1980). The Interaction of Carrier-Bound Methotrexate with L1210 Cells. Molecular Pharmacology. 17(3). 382–387. 18 indexed citations

19.

Chu, Barbara C.F. & John M. Whiteley. (1977). High Molecular Weight Derivatives of Methotrexate as Chemotherapeutic Agents. Molecular Pharmacology. 13(1). 80–88. 45 indexed citations

20.

Whiteley, John M., et al.. (1969). Synthesis and properties of 2-amino-4-hydroxy-5,6-dimethyl-5,6,7,8-tetrahydropteridine and the 5,7-dimethyl isomer. Archives of Biochemistry and Biophysics. 133(2). 436–441. 14 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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