Ying R. Yang

493 total citations
12 papers, 451 citations indexed

About

Ying R. Yang is a scholar working on Molecular Biology, Materials Chemistry and Clinical Biochemistry. According to data from OpenAlex, Ying R. Yang has authored 12 papers receiving a total of 451 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 6 papers in Materials Chemistry and 5 papers in Clinical Biochemistry. Recurrent topics in Ying R. Yang's work include Biochemical and Molecular Research (11 papers), Enzyme Structure and Function (6 papers) and Amino Acid Enzymes and Metabolism (5 papers). Ying R. Yang is often cited by papers focused on Biochemical and Molecular Research (11 papers), Enzyme Structure and Function (6 papers) and Amino Acid Enzymes and Metabolism (5 papers). Ying R. Yang collaborates with scholars based in United States and Canada. Ying R. Yang's co-authors include H. K. Schachman, Marc W. Kirschner, Johanna Syvänen, Algirdas Vėlyvis, Lewis E. Kay, I. R. Gibbons, Lei Wu, C. David Pauza, Marc Navre and Michael J. Karels and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Ying R. Yang

12 papers receiving 405 citations

Peers

Ying R. Yang

BIOCH

Hubert G. Britton United Kingdom

Styliani C. Pastra-Landis United States

Kenneth E. Moon Australia

C.M. Anderson United States

Christiane Portemer France

Bernd Hennig Germany

Alisa A. Garaeva Netherlands

Helmut Schneider Germany

Rosa Uy United States

Norihiko Fujii Japan

Hubert G. Britton United Kingdom

Ying R. Yang

345 ×1.1

167 ×0.9

90 ×0.5

153 ×1.4

BIOCH

145 ×1.4

Citations per year, relative to Ying R. Yang Ying R. Yang (= 1×) peers Hubert G. Britton

Countries citing papers authored by Ying R. Yang

Since Specialization

Citations

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

Fields of papers citing papers by Ying R. Yang

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ying R. Yang

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

All Works

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12 of 12 papers shown

Vėlyvis, Algirdas, Ying R. Yang, H. K. Schachman, & Lewis E. Kay. (2007). A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase. Proceedings of the National Academy of Sciences. 104(21). 8815–8820. 76 indexed citations

Beernink, Peter T., et al.. (2001). Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function. Protein Science. 10(3). 528–537. 18 indexed citations

Yang, Ying R. & H. K. Schachman. (1996). A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains. Biophysical Chemistry. 59(3). 289–297. 6 indexed citations

Yang, Ying R. & H. K. Schachman. (1993). Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.. Proceedings of the National Academy of Sciences. 90(24). 11980–11984. 36 indexed citations

Eisenstein, Edward, et al.. (1992). Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits.. Journal of Biological Chemistry. 267(31). 22148–22155. 13 indexed citations

Schachman, H. K., C. David Pauza, Marc Navre, et al.. (1984). Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation.. Proceedings of the National Academy of Sciences. 81(1). 115–119. 65 indexed citations

Hensley, Preston, Ying R. Yang, & H. K. Schachman. (1981). On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase. Journal of Molecular Biology. 152(1). 131–152. 26 indexed citations

Yang, Ying R., Marc W. Kirschner, & H. K. Schachman. (1978). [5] Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits. Methods in enzymology on CD-ROM/Methods in enzymology. 51. 35–41. 65 indexed citations

Subramani, Suresh, et al.. (1977). Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamoylase. Proceedings of the National Academy of Sciences. 74(9). 3777–3781. 28 indexed citations

10.

Gibbons, I. R., Ying R. Yang, & H. K. Schachman. (1974). Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide Chains. Proceedings of the National Academy of Sciences. 71(11). 4452–4456. 33 indexed citations

11.

Yang, Ying R., Johanna Syvänen, G M Nagel, & H. K. Schachman. (1974). Aspartate Transcarbamoylase Molecules Lacking One Regulatory Subunit. Proceedings of the National Academy of Sciences. 71(3). 918–922. 44 indexed citations

12.

Syvänen, Johanna, Ying R. Yang, & Marc W. Kirschner. (1973). Preparation of 125I-Catalytic Subunit of Aspartate Transcarbamylase and Its Use in Studies of the Regulatory Subunit. Journal of Biological Chemistry. 248(11). 3762–3768. 41 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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