Gregory K. Farber

1.8k total citations
32 papers, 1.4k citations indexed

About

Gregory K. Farber is a scholar working on Materials Chemistry, Molecular Biology and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Gregory K. Farber has authored 32 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Materials Chemistry, 14 papers in Molecular Biology and 4 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Gregory K. Farber's work include Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (8 papers) and Diet, Metabolism, and Disease (4 papers). Gregory K. Farber is often cited by papers focused on Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (8 papers) and Diet, Metabolism, and Disease (4 papers). Gregory K. Farber collaborates with scholars based in United States and United Kingdom. Gregory K. Farber's co-authors include Gregory A. Petsko, Hemant P. Yennawar, Neela H. Yennawar, Dagmar Ringe, Soojay Banerjee, Ronald E. Viola, Wuxian Shi, Arthur Glasfeld, Karen N. Allen and Arnon Lavie and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Biochemistry.

In The Last Decade

Gregory K. Farber

32 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gregory K. Farber United States 22 995 618 206 134 114 32 1.4k
Ronald E. Viola United States 29 1.7k 1.7× 954 1.5× 187 0.9× 406 3.0× 33 0.3× 112 2.7k
Alessio Peracchi Italy 28 2.0k 2.0× 609 1.0× 55 0.3× 477 3.6× 39 0.3× 63 2.6k
P.D.J. Weitzman United Kingdom 23 1.2k 1.2× 657 1.1× 54 0.3× 277 2.1× 17 0.1× 88 1.7k
Xin Wen China 23 825 0.8× 286 0.5× 50 0.2× 85 0.6× 71 0.6× 90 1.6k
George R. Dubay United States 20 413 0.4× 356 0.6× 67 0.3× 78 0.6× 32 0.3× 29 1.7k
Marián Antalı́k Slovakia 21 1.0k 1.0× 306 0.5× 32 0.2× 42 0.3× 24 0.2× 102 1.7k
Xevi Biarnés Spain 24 1.3k 1.3× 301 0.5× 332 1.6× 26 0.2× 30 0.3× 53 2.0k
Martin J. Kronman United States 23 955 1.0× 414 0.7× 38 0.2× 89 0.7× 36 0.3× 42 1.6k
Martin St. Maurice United States 23 991 1.0× 508 0.8× 34 0.2× 267 2.0× 31 0.3× 49 1.5k
Suman Kundu India 24 1.3k 1.3× 174 0.3× 171 0.8× 31 0.2× 28 0.2× 94 2.1k

Countries citing papers authored by Gregory K. Farber

Since Specialization
Citations

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

Fields of papers citing papers by Gregory K. Farber

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gregory K. Farber. 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 Gregory K. Farber. The network helps show where Gregory K. Farber may publish in the future.

Co-authorship network of co-authors of Gregory K. Farber

This figure shows the co-authorship network connecting the top 25 collaborators of Gregory K. Farber. A scholar is included among the top collaborators of Gregory K. Farber 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 Gregory K. Farber. Gregory K. Farber is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Farber, Gregory K., et al.. (2023). Common measures in mental health: a joint initiative by funders and journals. The Lancet Psychiatry. 10(6). 465–470. 31 indexed citations
2.
Farber, Gregory K., et al.. (2023). A Collaborative Effort to Establish Common Metrics for Use in Mental Health. JAMA Psychiatry. 80(10). 981–981. 10 indexed citations
3.
Yennawar, Neela H., et al.. (2001). The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallographica Section D Biological Crystallography. 57(4). 506–515. 39 indexed citations
4.
Park, Sungdae, Hong Zhang, Dalai Yan, et al.. (2001). A dimeric two‐component receiver domain inhibits the σ54‐dependent ATPase in DctD. The FASEB Journal. 15(7). 1326–1328. 31 indexed citations
5.
Brenchley, Jean E., et al.. (2000). Distributions of structural features contributing to thermostability in mesophilic and thermophilic α/β barrel glycosyl hydrolases. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1543(1). 189–201. 34 indexed citations
6.
Kidd, Richard, P.S. Sears, Dee‐Hua Huang, et al.. (1999). Breaking the low barrier hydrogen bond in a serine protease. Protein Science. 8(2). 410–417. 23 indexed citations
7.
Farber, Gregory K.. (1999). New approaches to rational drug design. Pharmacology & Therapeutics. 84(3). 327–332. 18 indexed citations
8.
Kidd, Richard, et al.. (1998). Crystallization and preliminary X-ray studies of the Rhizobium meliloti DctD two-component receiver domain. Acta Crystallographica Section D Biological Crystallography. 54(6). 1416–1418. 1 indexed citations
9.
Farber, Gregory K.. (1998). Sensing photons. Nature Structural Biology. 5(6). 415–417. 1 indexed citations
10.
Yennawar, Hemant P., et al.. (1997). The effect of denaturants on protein structure. Protein Science. 6(8). 1727–1733. 86 indexed citations
11.
Farber, Gregory K.. (1997). Laue crystallography: Lights! Camera! Action!. Current Biology. 7(6). R352–R354. 5 indexed citations
12.
Stoddard, Barry & Gregory K. Farber. (1995). Direct measurement of reactivity in the protein crystal by steady-state kinetic studies. Structure. 3(10). 991–996. 17 indexed citations
13.
Yennawar, Neela H., Hemant P. Yennawar, & Gregory K. Farber. (1994). X-ray Crystal Structure of .gamma.-Chymotrypsin in Hexane. Biochemistry. 33(23). 7326–7336. 114 indexed citations
14.
Allen, Karen N., Arnon Lavie, Arthur Glasfeld, et al.. (1994). Role of the Divalent Metal Ion in Sugar Binding, Ring Opening, and Isomerization by D-Xylose Isomerase: Replacement of a Catalytic Metal by an Amino Acid. Biochemistry. 33(6). 1488–1494. 64 indexed citations
15.
Allen, Karen N., Arnon Lavie, Gregory K. Farber, et al.. (1994). Isotopic Exchange plus Substrate and Inhibition Kinetics of D-Xylose Isomerase Do Not Support a Proton-Transfer Mechanism. Biochemistry. 33(6). 1481–1487. 55 indexed citations
16.
Stoddard, Barry, Gregory K. Farber, & Roland K. Strong. (1993). The Facts and Fancy of Microgravity Protein Crystallization. Biotechnology and Genetic Engineering Reviews. 11(1). 57–78. 3 indexed citations
17.
Zheng, Ya‐Jun, Kenneth M. Merz, & Gregory K. Farber. (1993). Theoretical examination of the mechanism of aldose–ketose isomerization. Protein Engineering Design and Selection. 6(5). 479–484. 23 indexed citations
18.
Stoddard, Barry, Roland K. Strong, A. S. Arrott, & Gregory K. Farber. (1992). Mir for the crystallographers' money. Nature. 360(6402). 293–294. 14 indexed citations
19.
Farber, Gregory K. & Gregory A. Petsko. (1990). The evolution of α/β barrel enzymes. Trends in Biochemical Sciences. 15(6). 228–234. 329 indexed citations
20.
Farber, Gregory K., Gregory A. Petsko, & Dagmar Ringe. (1987). The 3.0 Å crystal structure of xylose isomerase from Streptomyces olivochromogenes. Protein Engineering Design and Selection. 1(6). 459–466. 43 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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