James G. Robertson

2.6k total citations
26 papers, 865 citations indexed

About

James G. Robertson is a scholar working on Molecular Biology, Endocrinology, Diabetes and Metabolism and Materials Chemistry. According to data from OpenAlex, James G. Robertson has authored 26 papers receiving a total of 865 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 6 papers in Endocrinology, Diabetes and Metabolism and 6 papers in Materials Chemistry. Recurrent topics in James G. Robertson's work include Biochemical and Molecular Research (8 papers), Enzyme Structure and Function (6 papers) and Peptidase Inhibition and Analysis (5 papers). James G. Robertson is often cited by papers focused on Biochemical and Molecular Research (8 papers), Enzyme Structure and Function (6 papers) and Peptidase Inhibition and Analysis (5 papers). James G. Robertson collaborates with scholars based in United States, Germany and Australia. James G. Robertson's co-authors include Joseph J. Villafranca, Hsu‐Tso Ho, Paul Falk, Ann W. Walsh, Joanne J. Bronson, P. F. MISCO, Stanley V. D’Andrea, David Stock, Yaxiong Sun and William E. Harte and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

James G. Robertson

26 papers receiving 841 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James G. Robertson United States 15 465 292 97 81 73 26 865
Li Du China 17 483 1.0× 113 0.4× 139 1.4× 109 1.3× 164 2.2× 33 968
Christoph Rosenbohm Denmark 13 888 1.9× 234 0.8× 41 0.4× 36 0.4× 37 0.5× 18 1.3k
Anuraag Shrivastav Canada 17 569 1.2× 300 1.0× 69 0.7× 46 0.6× 35 0.5× 48 1.1k
Virginia L. Rath United States 16 871 1.9× 239 0.8× 124 1.3× 72 0.9× 14 0.2× 23 1.2k
Seung Seo Lee United Kingdom 17 791 1.7× 519 1.8× 112 1.2× 37 0.5× 101 1.4× 32 1.2k
Timothy L. Foley United States 17 591 1.3× 233 0.8× 41 0.4× 24 0.3× 40 0.5× 27 807
Francesco Merlino Italy 21 508 1.1× 88 0.3× 46 0.5× 72 0.9× 42 0.6× 54 909
Subhasis Banerjee India 18 391 0.8× 301 1.0× 44 0.5× 35 0.4× 26 0.4× 63 1.0k
Fangyi Zhu United States 19 436 0.9× 317 1.1× 25 0.3× 46 0.6× 41 0.6× 42 1.0k
Jun Sakakibara Japan 20 644 1.4× 215 0.7× 31 0.3× 29 0.4× 48 0.7× 45 1.8k

Countries citing papers authored by James G. Robertson

Since Specialization
Citations

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

Fields of papers citing papers by James G. Robertson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James G. Robertson. 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 James G. Robertson. The network helps show where James G. Robertson may publish in the future.

Co-authorship network of co-authors of James G. Robertson

This figure shows the co-authorship network connecting the top 25 collaborators of James G. Robertson. A scholar is included among the top collaborators of James G. Robertson 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 James G. Robertson. James G. Robertson 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.
Zhao, Guohua, Chet Kwon, Aiying Wang, et al.. (2013). Substituted piperidinyl glycinyl 2-cyano-4,5-methano pyrrolidines as potent and stable dipeptidyl peptidase IV inhibitors. Bioorganic & Medicinal Chemistry Letters. 23(6). 1622–1625. 11 indexed citations
2.
Ellsworth, Bruce A., Wei Meng, Manorama M. Patel, et al.. (2008). Aglycone exploration of C-arylglucoside inhibitors of renal sodium-dependent glucose transporter SGLT2. Bioorganic & Medicinal Chemistry Letters. 18(17). 4770–4773. 43 indexed citations
3.
Robertson, James G.. (2007). Enzymes as a special class of therapeutic target: clinical drugs and modes of action. Current Opinion in Structural Biology. 17(6). 674–679. 54 indexed citations
4.
Robertson, James G.. (2005). Mechanistic Basis of Enzyme-Targeted Drugs. Biochemistry. 44(15). 5561–5571. 179 indexed citations
5.
Magnin, David R., Prakash C. Taunk, James G. Robertson, et al.. (2005). Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1. Bioorganic & Medicinal Chemistry Letters. 16(6). 1731–1734. 3 indexed citations
6.
Zhao, Guohua, Prakash C. Taunk, David R. Magnin, et al.. (2005). Diprolyl nitriles as potent dipeptidyl peptidase IV inhibitors. Bioorganic & Medicinal Chemistry Letters. 15(18). 3992–3995. 19 indexed citations
7.
Wang, Aiying, et al.. (2003). Application of robotics to steady state enzyme kinetics: analysis of tight-binding inhibitors of dipeptidyl peptidase IV. Analytical Biochemistry. 321(2). 157–166. 6 indexed citations
8.
Bronson, Joanne J., Stanley V. D’Andrea, Milind Deshpande, et al.. (2000). 4-Thiazolidinones: novel inhibitors of the bacterial enzyme murB. Bioorganic & Medicinal Chemistry Letters. 10(8). 715–717. 201 indexed citations
9.
Robertson, James G., et al.. (1997). Growth hormone but not insulin‐like growth factor‐I improves wound strength in pigs. Wound Repair and Regeneration. 5(2). 168–174. 10 indexed citations
10.
Constantine, Keith L., Luciano Mueller, Valentina Goldfarb, et al.. (1997). Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes. Journal of Molecular Biology. 267(5). 1223–1246. 46 indexed citations
11.
Robertson, James G., et al.. (1996). Insulin-like growth factor I (IGF-I) and IGF-Binding proteins in rat wound fluid.. Endocrinology. 137(7). 2774–2781. 11 indexed citations
12.
Sheriff, S., Herbert E. Klei, John S. Sack, et al.. (1996). Crystallization and preliminary crystallographic analysis ofE. coliuridine 5'-diphospho-N-acetylenolpyruvylglucosamine reductase in two new crystal forms. Acta Crystallographica Section D Biological Crystallography. 52(3). 586–588. 1 indexed citations
13.
Fairman, Robert, et al.. (1995). Physical characterizations of E coli UDP-N-acetylmuramateL-alanine ligase. The FASEB Journal. 9(6). 1243. 1 indexed citations
14.
Yanchunas, Joseph, et al.. (1995). Steady-State Kinetic Mechanism of Escherichia coli UDP-N-Acetylenolpyruvylglucosamine Reductase. Biochemistry. 34(16). 5390–5402. 33 indexed citations
15.
Robertson, James G., Joseph Yanchunas, & Joseph J. Villafranca. (1995). Dimerization of Native and C-Terminally Proteolyzed p56lck Tyrosine Kinase. Archives of Biochemistry and Biophysics. 317(1). 259–266. 1 indexed citations
16.
Robertson, James G.. (1995). Determination of Subunit Dissociation Constants in Native and Inactivated CTP Synthetase by Sedimentation Equilibrium. Biochemistry. 34(22). 7533–7541. 33 indexed citations
17.
Robertson, James G., Gregory W. Adams, Katalin F. Medzihradszky, Alma L. Burlingame, & Joseph J. Villafranca. (1994). Complete Assignment of Disulfide Bonds in Bovine Dopamine .beta.-Hydroxylase. Biochemistry. 33(38). 11563–11575. 24 indexed citations
18.
Robertson, James G. & Joseph J. Villafranca. (1993). Characterization of metal ion activation and inhibition of CTP synthetase. Biochemistry. 32(14). 3769–3777. 21 indexed citations
19.
Robertson, James G., Louis J. Sparvero, & Joseph J. Villafranca. (1992). Inactivation and covalent modification of CTP synthetase by thiourea dioxide. Protein Science. 1(10). 1298–1307. 9 indexed citations
20.
Diamond, Alan M., S.D. Gorham, David J. Etherington, James G. Robertson, & Nicholas Light. (1991). The Effect of Modification on the Susceptibility of Collagen to Proteolysis: I. Chemical Modification of Amino Acid Side Chains. Matrix. 11(5). 321–329. 22 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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