Xiangshi Tan

1.3k total citations
70 papers, 1.0k citations indexed

About

Xiangshi Tan is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Xiangshi Tan has authored 70 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 34 papers in Cell Biology and 18 papers in Physiology. Recurrent topics in Xiangshi Tan's work include Hemoglobin structure and function (34 papers), Porphyrin Metabolism and Disorders (18 papers) and Heme Oxygenase-1 and Carbon Monoxide (11 papers). Xiangshi Tan is often cited by papers focused on Hemoglobin structure and function (34 papers), Porphyrin Metabolism and Disorders (18 papers) and Heme Oxygenase-1 and Carbon Monoxide (11 papers). Xiangshi Tan collaborates with scholars based in China, United States and United Kingdom. Xiangshi Tan's co-authors include Ying‐Wu Lin, Ge‐Bo Wen, Shu‐Qin Gao, Zhong‐Xian Huang, Paul A. Lindahl, Tianlei Ying, Hong Yuan, Zhonghua Wang, Qiming Xu and Bo He and has published in prestigious journals such as Journal of the American Chemical Society, PLoS ONE and Biochemistry.

In The Last Decade

Xiangshi Tan

70 papers receiving 1.0k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Xiangshi Tan 604 328 146 142 137 70 1.0k
Michael R. Gunther 525 0.9× 267 0.8× 395 2.7× 115 0.8× 18 0.1× 27 1.4k
D. Moira Glerum 2.2k 3.6× 110 0.3× 229 1.6× 84 0.6× 90 0.7× 53 2.9k
Günter Fred Fuhrmann 1.1k 1.8× 154 0.5× 219 1.5× 90 0.6× 27 0.2× 74 1.6k
Olivier M. Lardinois 384 0.6× 165 0.5× 137 0.9× 64 0.5× 13 0.1× 25 803
Lijuan Liu 473 0.8× 77 0.2× 84 0.6× 35 0.2× 113 0.8× 47 1.4k
Sumita Chakraborty 654 1.1× 80 0.2× 130 0.9× 63 0.4× 16 0.1× 33 1.1k
T. Arakawa 1.1k 1.7× 143 0.4× 99 0.7× 34 0.2× 37 0.3× 53 1.6k
Jolanda Van der Zee 433 0.7× 115 0.4× 202 1.4× 44 0.3× 10 0.1× 36 1.2k
Anna Maria Santoro 437 0.7× 105 0.3× 217 1.5× 50 0.4× 11 0.1× 45 1.1k
Carl Bernofsky 573 0.9× 81 0.2× 112 0.8× 27 0.2× 34 0.2× 45 1.1k

Countries citing papers authored by Xiangshi Tan

Since Specialization
Citations

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

Fields of papers citing papers by Xiangshi Tan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Xiangshi Tan. 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 Xiangshi Tan. The network helps show where Xiangshi Tan may publish in the future.

Co-authorship network of co-authors of Xiangshi Tan

This figure shows the co-authorship network connecting the top 25 collaborators of Xiangshi Tan. A scholar is included among the top collaborators of Xiangshi Tan 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 Xiangshi Tan. Xiangshi Tan 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.
Guo, Pengfei, et al.. (2024). Site-specific incorporation of 19F-nuclei at protein C-terminus to probe allosteric conformational transitions of metalloproteins. Communications Biology. 7(1). 1613–1613. 1 indexed citations
2.
Mi, Pengbing, et al.. (2023). Lewis Acid‐Assisted Molybdenum(VI) Complexes with S, N‐bidentate Ligands to Reduce Nitrate. European Journal of Inorganic Chemistry. 26(9). 2 indexed citations
3.
Yuan, Hong, Huamin Wang, Lijuan Sun, et al.. (2023). Regulating the Heme Active Site by Covalent Modifications: Two Case Studies of Myoglobin. ChemBioChem. 25(3). e202300678–e202300678. 3 indexed citations
4.
Dai, Wei, Hong Yuan, Xiaojuan Wang, et al.. (2023). Self-oxidation of cysteine to sulfinic acid in an engineered T67C myoglobin: structure and reactivity. RSC Chemical Biology. 4(5). 330–333. 1 indexed citations
5.
Li, Yanyan, Lu Yu, Aokun Liu, et al.. (2023). Effects of naturally occurring S47F/A mutations on the structure and function of human cytochrome c. Journal of Inorganic Biochemistry. 246. 112296–112296. 1 indexed citations
6.
Gao, Shu‐Qin, Hong Yuan, Xichun Liu, et al.. (2022). The X‐ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand‐binding sites. Proteins Structure Function and Bioinformatics. 90(5). 1152–1158. 7 indexed citations
7.
Lü, Xing, Hao Cheng, Qiming Xu, & Xiangshi Tan. (2021). Encapsulation of STING Agonist cGAMP with Folic Acid-Conjugated Liposomes Significantly Enhances Antitumor Pharmacodynamic Effect. Cancer Biotherapy and Radiopharmaceuticals. 38(8). 543–557. 8 indexed citations
8.
Yang, Xiang, Yuejuan Zhang, Ying Ge, et al.. (2020). Kinetic, Thermodynamic, and Crystallographic Studies of 2-Triazolylthioacetamides as Verona Integron-Encoded Metallo-β-Lactamase 2 (VIM-2) Inhibitor. Biomolecules. 10(1). 72–72. 6 indexed citations
9.
10.
Xu, Qiming, Wei Xu, Hao Cheng, Hong Yuan, & Xiangshi Tan. (2019). Efficacy and mechanism of cGAMP to suppress Alzheimer’s disease by elevating TREM2. Brain Behavior and Immunity. 81. 495–508. 57 indexed citations
11.
Cheng, Huimin, Xiaojuan Wang, Jiakun Xu, et al.. (2018). Formation of Cys-heme cross-link in K42C myoglobin under reductive conditions with molecular oxygen. Journal of Inorganic Biochemistry. 182. 141–149. 12 indexed citations
12.
Liao, Fei, Hong Yuan, Ke‐Jie Du, et al.. (2016). Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin. Molecular BioSystems. 12(10). 3139–3145. 6 indexed citations
13.
Wang, Hongyan, Fangfang Zhong, Jie Pan, et al.. (2012). Structural and functional insights into the heme-binding domain of the human soluble guanylate cyclase α2 subunit and heterodimeric α2β1. JBIC Journal of Biological Inorganic Chemistry. 17(5). 719–730. 4 indexed citations
14.
Luo, Ying, Wěi Li, Cuiqing Zhu, et al.. (2011). The mechanism for heme to prevent Aβ1–40 aggregation and its cytotoxicity. JBIC Journal of Biological Inorganic Chemistry. 16(5). 809–816. 26 indexed citations
15.
Li, Lianzhi, et al.. (2010). Spectroscopic study on acid-induced unfolding and refolding of apo-neuroglobin. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 75(5). 1600–1604. 10 indexed citations
16.
Zhong, Fangfang, Hongyan Wang, Tianlei Ying, Zhong‐Xian Huang, & Xiangshi Tan. (2010). Efficient expression of human soluble guanylate cyclase in Escherichia coli and its signaling-related interaction with nitric oxide. Amino Acids. 39(2). 399–408. 13 indexed citations
17.
Sun, Lu, Zhonghua Wang, Fengyun Ni, Xiangshi Tan, & Zhong‐Xian Huang. (2009). The Role of Ile476 in the Structural Stability and Substrate Binding of Human Cytochrome P450 2C8. The Protein Journal. 29(1). 32–43. 4 indexed citations
18.
Ying, Tianlei, et al.. (2009). Evolutionary alkaline transition in human cytochrome c. Journal of Bioenergetics and Biomembranes. 41(3). 251–257. 22 indexed citations
19.
Stubna, Audria, et al.. (2006). Mössbauer and EPR Study of Recombinant Acetyl-CoA Synthase from Moorella thermoacetica. Biochemistry. 45(28). 8674–8685. 33 indexed citations
20.
Tan, Xiangshi, Anne Volbeda, Juan C. Fontecilla‐Camps, & Paul A. Lindahl. (2006). Function of the tunnel in acetylcoenzyme A synthase/carbon monoxide dehydrogenase. JBIC Journal of Biological Inorganic Chemistry. 11(3). 371–378. 25 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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