Merry R. Sherman

2.8k total citations
31 papers, 2.3k citations indexed

About

Merry R. Sherman is a scholar working on Molecular Biology, Genetics and Spectroscopy. According to data from OpenAlex, Merry R. Sherman has authored 31 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 12 papers in Genetics and 7 papers in Spectroscopy. Recurrent topics in Merry R. Sherman's work include Estrogen and related hormone effects (12 papers), Mass Spectrometry Techniques and Applications (5 papers) and Receptor Mechanisms and Signaling (5 papers). Merry R. Sherman is often cited by papers focused on Estrogen and related hormone effects (12 papers), Mass Spectrometry Techniques and Applications (5 papers) and Receptor Mechanisms and Signaling (5 papers). Merry R. Sherman collaborates with scholars based in United States and Spain. Merry R. Sherman's co-authors include Bert W. O’Malley, Mark G.P. Saifer, Lorraine K. Miller, Pierre Corvol, John Stevens, Fernando Pérez-Ruiz, Karl A. Piez, David O. Toft, Yee-Wan Stevens and L. David Williams and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Clinical Endocrinology & Metabolism.

In The Last Decade

Merry R. Sherman

31 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Merry R. Sherman United States 21 1.2k 850 330 206 197 31 2.3k
Yale J. Topper United States 36 2.0k 1.7× 1.5k 1.8× 703 2.1× 36 0.2× 90 0.5× 97 4.1k
W. A. Schroeder United States 40 1.5k 1.3× 366 0.4× 200 0.6× 88 0.4× 62 0.3× 116 5.1k
John C. Voyta United States 18 1.4k 1.2× 140 0.2× 153 0.5× 83 0.4× 96 0.5× 37 2.3k
Leon W. Cunningham United States 33 1.4k 1.2× 143 0.2× 108 0.3× 285 1.4× 121 0.6× 76 2.6k
Nancy Krett United States 35 2.1k 1.8× 652 0.8× 284 0.9× 88 0.4× 95 0.5× 76 3.5k
Terutoshi Kimura Japan 29 2.3k 1.9× 241 0.3× 73 0.2× 69 0.3× 148 0.8× 119 3.4k
Toru Kawakami Japan 30 2.5k 2.2× 340 0.4× 136 0.4× 152 0.7× 131 0.7× 106 3.8k
G A Keller United States 29 4.4k 3.8× 177 0.2× 157 0.5× 154 0.7× 92 0.5× 34 5.6k
Arnold E. Reif United States 21 1.1k 0.9× 181 0.2× 203 0.6× 45 0.2× 436 2.2× 64 2.6k
Evelyn Barrack United States 35 2.2k 1.9× 959 1.1× 933 2.8× 13 0.1× 100 0.5× 60 3.9k

Countries citing papers authored by Merry R. Sherman

Since Specialization
Citations

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

Fields of papers citing papers by Merry R. Sherman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Merry R. Sherman. 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 Merry R. Sherman. The network helps show where Merry R. Sherman may publish in the future.

Co-authorship network of co-authors of Merry R. Sherman

This figure shows the co-authorship network connecting the top 25 collaborators of Merry R. Sherman. A scholar is included among the top collaborators of Merry R. Sherman 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 Merry R. Sherman. Merry R. Sherman 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.
Saifer, Mark G.P., et al.. (2013). Selectivity of binding of PEGs and PEG-like oligomers to anti-PEG antibodies induced by methoxyPEG-proteins. Molecular Immunology. 57(2). 236–246. 88 indexed citations
2.
Sherman, Merry R., Mark G.P. Saifer, & Fernando Pérez-Ruiz. (2007). PEG-uricase in the management of treatment-resistant gout and hyperuricemia. Advanced Drug Delivery Reviews. 60(1). 59–68. 218 indexed citations
3.
Kelly, Susan J., Marielle Delnomdedieu, Michael I. Oliverio, et al.. (2001). Diabetes Insipidus in Uricase-Deficient Mice: A Model for Evaluating Therapy with Poly(Ethylene Glycol)-Modified Uricase. Journal of the American Society of Nephrology. 12(5). 1001–1009. 68 indexed citations
4.
Saifer, Mark G.P., et al.. (1997). Improved conjugation of cytokines using high molecular weight poly(ethylene glycol): PEG-GM-CSF as a prototype. 38(1). 576–577. 3 indexed citations
5.
Smith, Richard, Frank M. Balis, Kenneth Ott, et al.. (1995). Pharmacokinetics and tolerability of ventricularly administered superoxide dismutase in monkeys and preliminary clinical observations in familial ALS. Journal of the Neurological Sciences. 129. 13–18. 10 indexed citations
6.
Sherman, Merry R. & John Stevens. (1984). Structure of Mammalian Steroid Receptors: Evolving Concepts and Methodological Developments. Annual Review of Physiology. 46(1). 83–105. 158 indexed citations
7.
8.
Schlechte, Janet & Merry R. Sherman. (1982). Decreased Glucocorticoid Receptor Binding in Adrenal Insufficiency*. The Journal of Clinical Endocrinology & Metabolism. 54(1). 145–149. 18 indexed citations
9.
Miller, Lorraine K., et al.. (1981). Human Breast Tumor Estrogen Receptor: Effects of Molybdate and Electrophoretic Analyses*. Endocrinology. 108(4). 1369–1378. 85 indexed citations
10.
Niu, En-Mei, et al.. (1981). Structural similarity of molybdate-stabilized steroid receptors in human breast tumors, uteri and leukocytes. Journal of Steroid Biochemistry. 15. 1–10. 59 indexed citations
11.
Lee, Henry J., et al.. (1981). Binding of glucocorticoid 21-OIC acids and esters to molybdate-stabilized hepatic receptors. Journal of Steroid Biochemistry. 14(12). 1325–1335. 32 indexed citations
12.
Sherman, Merry R., et al.. (1980). Estrogen Receptor Cleavage and Plasminogen Activation by Enzymes in Human Breast Tumor Cytosol*. Endocrinology. 106(6). 1715–1727. 102 indexed citations
13.
Sherman, Merry R.. (1979). Allosteric and Competitive Steroid-Receptor Interactions. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 12. 123–133. 10 indexed citations
14.
Bullock, Leslie P., C. Wayne Bardin, & Merry R. Sherman. (1978). Androgenic, Antiandrogenic, and Synandrogenic Actions of Progestins: Role of Steric and Allosteric Interactions with Androgen Receptors*. Endocrinology. 103(5). 1768–1782. 88 indexed citations
15.
Sherman, Merry R. & Lorraine K. Miller. (1976). Fractionation of Diverse Steroid-Binding Proteins: Basic and Clinical Applications. PubMed. 4. 51–67. 2 indexed citations
16.
Miller, Lorraine K., et al.. (1975). Steroid-receptor quantitation and characterization by electrophoresis in highly crosslinked polyacrylamide gels. Biochemistry. 14(20). 4433–4443. 59 indexed citations
17.
Sherman, Merry R.. (1975). [18] Physical-chemical analysis of steroid hormone receptors. Methods in enzymology on CD-ROM/Methods in enzymology. 36. 211–234. 71 indexed citations
18.
Sherman, Merry R., et al.. (1974). Progesterone Receptors of Chick Oviduct. Journal of Biological Chemistry. 249(17). 5351–5363. 76 indexed citations
19.
O’Malley, Bert W., David O. Toft, & Merry R. Sherman. (1971). Progesterone-binding Components of Chick Oviduct. Journal of Biological Chemistry. 246(4). 1117–1122. 121 indexed citations
20.
Piez, Karl A. & Merry R. Sherman. (1970). Equilibrium and kinetic studies of the helix-coil transition in α1-CB2, a small peptide from collagen. Biochemistry. 9(21). 4134–4140. 47 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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