Lin Jiang

8.0k total citations · 4 hit papers
52 papers, 5.6k citations indexed

About

Lin Jiang is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Lin Jiang has authored 52 papers receiving a total of 5.6k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 19 papers in Physiology and 7 papers in Materials Chemistry. Recurrent topics in Lin Jiang's work include Alzheimer's disease research and treatments (19 papers), Protein Structure and Dynamics (17 papers) and Enzyme Structure and Function (7 papers). Lin Jiang is often cited by papers focused on Alzheimer's disease research and treatments (19 papers), Protein Structure and Dynamics (17 papers) and Enzyme Structure and Function (7 papers). Lin Jiang collaborates with scholars based in United States, China and Switzerland. Lin Jiang's co-authors include David Baker, David Eisenberg, Eric A. Althoff, Alexandre Zanghellini, Daniela Röthlisberger, Jasmine L. Gallaher, K. N. Houk, Jamie L. Betker, M.R. Sawaya and Andrew M. Wollacott and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Lin Jiang

50 papers receiving 5.5k citations

Hit Papers

Kemp elimination catalysts by computational enzyme design 2008 2026 2014 2020 2008 2008 2018 2011 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lin Jiang United States 30 4.0k 1.5k 991 621 462 52 5.6k
Janet R. Kumita United Kingdom 37 3.0k 0.7× 1.6k 1.0× 879 0.9× 660 1.1× 495 1.1× 90 4.8k
Per Hammarström Sweden 45 4.5k 1.1× 3.2k 2.1× 1.1k 1.1× 397 0.6× 697 1.5× 145 7.2k
Thomas C. T. Michaels United Kingdom 36 3.1k 0.8× 2.7k 1.7× 636 0.6× 696 1.1× 1.1k 2.4× 95 5.1k
Monica Bucciantini Italy 31 3.7k 0.9× 2.5k 1.6× 611 0.6× 443 0.7× 451 1.0× 87 5.6k
Gianluigi Veglia United States 47 4.9k 1.2× 705 0.5× 1.4k 1.4× 487 0.8× 211 0.5× 216 7.6k
Leonid Breydo United States 30 3.0k 0.7× 2.1k 1.4× 378 0.4× 702 1.1× 395 0.9× 74 4.8k
Annalisa Relini Italy 36 2.7k 0.7× 1.9k 1.2× 357 0.4× 391 0.6× 411 0.9× 109 4.0k
Evan T. Powers United States 52 7.2k 1.8× 2.5k 1.6× 850 0.9× 517 0.8× 588 1.3× 108 9.9k
Christopher A. Waudby United Kingdom 26 2.9k 0.7× 1.3k 0.9× 679 0.7× 443 0.7× 718 1.6× 64 4.2k
Georg Meisl United Kingdom 38 3.4k 0.9× 3.6k 2.3× 521 0.5× 1.1k 1.8× 1.2k 2.5× 104 5.9k

Countries citing papers authored by Lin Jiang

Since Specialization
Citations

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

Fields of papers citing papers by Lin Jiang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lin Jiang

This figure shows the co-authorship network connecting the top 25 collaborators of Lin Jiang. A scholar is included among the top collaborators of Lin Jiang 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 Lin Jiang. Lin Jiang 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
2.
Gong, Shuai, Lin Jiang, Hao Cheng, et al.. (2021). Effects of CRH and ACTH exposure during in vitro maturation on competence of pig and mouse oocytes. Theriogenology. 173. 211–220. 3 indexed citations
3.
Boyer, David R., Binsen Li, Chuanqi Sun, et al.. (2020). The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure. Proceedings of the National Academy of Sciences. 117(7). 3592–3602. 137 indexed citations
4.
Shin, Woo Shik, Jing Di, Qin Cao, et al.. (2019). Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation. Alzheimer s Research & Therapy. 11(1). 86–86. 76 indexed citations
5.
Lu, Jinxia, Qin Cao, Chuchu Wang, et al.. (2019). Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation. Frontiers in Molecular Neuroscience. 12. 54–54. 61 indexed citations
6.
Hayden, Eric Y., Woo Shik Shin, Suman Dutta, et al.. (2019). Ischemic axonal injury up-regulates MARK4 in cortical neurons and primes tau phosphorylation and aggregation. Acta Neuropathologica Communications. 7(1). 135–135. 24 indexed citations
7.
Li, Binsen, P. Ge, Kevin A. Murray, et al.. (2018). Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel. Nature Communications. 9(1). 3609–3609. 470 indexed citations breakdown →
8.
Krotee, Pascal, José A. Rodríguez, M.R. Sawaya, et al.. (2017). Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity. eLife. 6. 89 indexed citations
9.
Rodríguez, José A., Lin Jiang, & David Eisenberg. (2017). Toward the Atomic Structure of PrPSc. Cold Spring Harbor Perspectives in Biology. 9(9). a031336–a031336. 19 indexed citations
10.
Kurt, Timothy D., Patricia Aguilar‐Calvo, Lin Jiang, et al.. (2017). Asparagine and glutamine ladders promote cross-species prion conversion. Journal of Biological Chemistry. 292(46). 19076–19086. 22 indexed citations
11.
Krotee, Pascal, Sarah L. Griner, M.R. Sawaya, et al.. (2017). Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors. Journal of Biological Chemistry. 293(8). 2888–2902. 50 indexed citations
12.
Gu, Lei, Joyce Tran, Lin Jiang, & Zhefeng Guo. (2016). A new structural model of Alzheimer’s Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling. Journal of Structural Biology. 194(1). 61–67. 46 indexed citations
13.
James, Aaron W., Jia Shen, Xinli Zhang, et al.. (2015). NELL-1 in the treatment of osteoporotic bone loss. Nature Communications. 6(1). 7362–7362. 96 indexed citations
14.
Lai, Yen‐Ting, Lin Jiang, Wuyang Chen, & Todd O. Yeates. (2015). On the predictability of the orientation of protein domains joined by a spanning alpha-helical linker. Protein Engineering Design and Selection. 28(11). 491–500. 25 indexed citations
15.
Hayden, Eric Y., Ghiam Yamin, Benson Chen, et al.. (2015). Inhibiting amyloid β‐protein assembly: Size–activity relationships among grape seed‐derived polyphenols. Journal of Neurochemistry. 135(2). 416–430. 30 indexed citations
16.
Saelices, Lorena, Lisa M. Johnson, M.R. Sawaya, et al.. (2015). Uncovering the Mechanism of Aggregation of Human Transthyretin. Journal of Biological Chemistry. 290(48). 28932–28943. 119 indexed citations
17.
Kurt, Timothy D., Lin Jiang, Cyrus Bett, David Eisenberg, & Christina J. Sigurdson. (2014). A Proposed Mechanism for the Promotion of Prion Conversion Involving a Strictly Conserved Tyrosine Residue in the β2-α2 Loop of PrPC. Journal of Biological Chemistry. 289(15). 10660–10667. 33 indexed citations
18.
Althoff, Eric A., Ling Wang, Lin Jiang, et al.. (2012). Robust design and optimization of retroaldol enzymes. Protein Science. 21(5). 717–726. 137 indexed citations
19.
Landau, Meytal, M.R. Sawaya, Kym F. Faull, et al.. (2011). Towards a Pharmacophore for Amyloid. PLoS Biology. 9(6). e1001080–e1001080. 168 indexed citations
20.
Jiang, Lin, et al.. (2005). An artificial aspartic proteinase system. Bioorganic & Medicinal Chemistry. 13(11). 3673–3680. 15 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026