Zhihe Kuang

483 total citations
18 papers, 393 citations indexed

About

Zhihe Kuang is a scholar working on Molecular Biology, Immunology and Physiology. According to data from OpenAlex, Zhihe Kuang has authored 18 papers receiving a total of 393 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 5 papers in Immunology and 4 papers in Physiology. Recurrent topics in Zhihe Kuang's work include Receptor Mechanisms and Signaling (4 papers), Glycosylation and Glycoproteins Research (3 papers) and interferon and immune responses (3 papers). Zhihe Kuang is often cited by papers focused on Receptor Mechanisms and Signaling (4 papers), Glycosylation and Glycoproteins Research (3 papers) and interferon and immune responses (3 papers). Zhihe Kuang collaborates with scholars based in Australia, China and India. Zhihe Kuang's co-authors include Raymond S. Norton, Shenggen Yao, Andrew Low, Sandra E. Nicholson, Rowena S. Lewis, Seth L. Masters, Tracy A. Willson, Tatiana B. Kolesnik, Leon A. Bach and Briony E. Forbes and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Experimental Medicine and The Journal of Cell Biology.

In The Last Decade

Zhihe Kuang

17 papers receiving 389 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Zhihe Kuang Australia 10 298 79 50 49 41 18 393
Renata de Freitas Saito Brazil 14 314 1.1× 76 1.0× 14 0.3× 79 1.6× 23 0.6× 26 485
Eva C. Keilhauer Germany 8 499 1.7× 33 0.4× 17 0.3× 30 0.6× 33 0.8× 9 623
Valérie Le Fourn Switzerland 14 399 1.3× 65 0.8× 58 1.2× 10 0.2× 49 1.2× 18 564
Davin R. Jensen United States 15 294 1.0× 73 0.9× 15 0.3× 25 0.5× 10 0.2× 24 508
Emmanuel Ruffet France 11 237 0.8× 60 0.8× 51 1.0× 19 0.4× 10 0.2× 12 383
Michael Trinh United States 7 148 0.5× 33 0.4× 12 0.2× 23 0.5× 77 1.9× 9 311
Morris A. Kostiuk Canada 12 329 1.1× 16 0.2× 24 0.5× 65 1.3× 43 1.0× 16 546
José Canales Spain 12 221 0.7× 73 0.9× 14 0.3× 12 0.2× 15 0.4× 39 395
Marie‐Estelle Losfeld United States 12 388 1.3× 147 1.9× 14 0.3× 23 0.5× 49 1.2× 16 469
Michael Brent United States 6 283 0.9× 59 0.7× 7 0.1× 26 0.5× 48 1.2× 6 458

Countries citing papers authored by Zhihe Kuang

Since Specialization
Citations

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

Fields of papers citing papers by Zhihe Kuang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Zhihe Kuang

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

All Works

18 of 18 papers shown
1.
Luo, Yanhong, Weiwei Hu, Jinjin Yang, et al.. (2024). Subtle Structural Differences Affect the Inhibitory Potency of RGD-Containing Cyclic Peptide Inhibitors Targeting SPSB Proteins. International Journal of Molecular Sciences. 25(12). 6764–6764.
2.
Yang, Jinjin, et al.. (2023). Crystal structure of the 3-ketodihydrosphingosine reductase TSC10 from Cryptococcus neoformans. Biochemical and Biophysical Research Communications. 670. 73–78. 1 indexed citations
3.
You, Tingting, Yanhong Luo, Huan Wei, et al.. (2021). Structural basis for the regulation of inducible nitric oxide synthase by the SPRY domain-containing SOCS box protein SPSB2, an E3 ubiquitin ligase. Nitric Oxide. 113-114. 1–6. 5 indexed citations
4.
Kuang, Zhihe, et al.. (2020). Crystal structure of the SPRY domain-containing protein 7 reveals unique structural features. Biochemical and Biophysical Research Communications. 531(3). 350–356. 5 indexed citations
5.
Luo, Yanhong, et al.. (2019). Crystal structure of the SPRY domain of human SPSB2 in the apo state. Acta Crystallographica Section F Structural Biology Communications. 75(6). 412–418. 3 indexed citations
6.
Wei, Huan, et al.. (2019). Backbone 1H, 13C, and 15N resonance assignments of the PRY-SPRY domain of RNF135. Biomolecular NMR Assignments. 13(2). 299–304. 4 indexed citations
7.
You, Tingting, Yuhui Wang, Huan Wei, et al.. (2017). Crystal structure of SPSB2 in complex with a rational designed RGD-containing cyclic peptide inhibitor of SPSB2-iNOS interaction. Biochemical and Biophysical Research Communications. 489(3). 346–352. 14 indexed citations
8.
Liu, Xiaoyun, et al.. (2016). Rational design for the stability improvement of Armillariella tabescens β-mannanase MAN47 based on N-glycosylation modification. Enzyme and Microbial Technology. 97. 82–89. 16 indexed citations
9.
Kuang, Zhihe, Minmin Zhang, Kallol Gupta, et al.. (2013). Mammalian Neuronal Sodium Channel Blocker μ-Conotoxin BuIIIB Has a Structured N-Terminus That Influences Potency. ACS Chemical Biology. 8(6). 1344–1351. 21 indexed citations
10.
Safavi‐Hemami, Helena, Zhihe Kuang, Nicholas A. Williamson, et al.. (2011). Embryonic Toxin Expression in the Cone Snail Conus victoriae. Journal of Biological Chemistry. 286(25). 22546–22557. 25 indexed citations
11.
Lewis, Rowena S., Tatiana B. Kolesnik, Zhihe Kuang, et al.. (2011). TLR Regulation of SPSB1 Controls Inducible Nitric Oxide Synthase Induction. The Journal of Immunology. 187(7). 3798–3805. 51 indexed citations
12.
Kuang, Zhihe, Rowena S. Lewis, Joan Curtis, et al.. (2010). The SPRY domain–containing SOCS box protein SPSB2 targets iNOS for proteasomal degradation. The Journal of Cell Biology. 190(1). 129–141. 77 indexed citations
13.
Filippakopoulos, P., Andrew Low, Timothy Sharpe, et al.. (2010). Structural Basis for Par-4 Recognition by the SPRY Domain- and SOCS Box-Containing Proteins SPSB1, SPSB2, and SPSB4. Journal of Molecular Biology. 401(3). 389–402. 56 indexed citations
14.
Kuang, Zhihe, Rowena S. Lewis, Joan Curtis, et al.. (2010). The SPRY domain–containing SOCS box protein SPSB2 targets iNOS for proteasomal degradation. The Journal of Experimental Medicine. 207(8). i22–i22. 2 indexed citations
15.
Kuang, Zhihe, Shenggen Yao, Yibin Xu, et al.. (2009). SPRY Domain-Containing SOCS Box Protein 2: Crystal Structure and Residues Critical for Protein Binding. Journal of Molecular Biology. 386(3). 662–674. 40 indexed citations
16.
Kuang, Zhihe, Shenggen Yao, Kerrie A. McNeil, et al.. (2008). Insulin-like growth factor-I (IGF-I): Solution properties and NMR chemical shift assignments near physiological pH. Growth Hormone & IGF Research. 19(3). 226–231. 3 indexed citations
17.
Kuang, Zhihe, Shenggen Yao, Kerrie A. McNeil, et al.. (2007). Cooperativity of the N- and C-Terminal Domains of Insulin-like Growth Factor (IGF) Binding Protein 2 in IGF Binding. Biochemistry. 46(48). 13720–13732. 21 indexed citations
18.
Kuang, Zhihe, Shenggen Yao, David W. Keizer, et al.. (2006). Structure, Dynamics and Heparin Binding of the C-terminal Domain of Insulin-like Growth Factor-binding Protein-2 (IGFBP-2). Journal of Molecular Biology. 364(4). 690–704. 49 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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