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Molecular Biology

D-Index
65
Citations
19267
World Ranking
1654
National Ranking
38

Overview

Jianping Ding is affiliated with the Chinese Academy of Sciences in China and has a notable body of research focused on molecular biology, biochemistry, genetics, and cancer research. Their work spans several interrelated subfields, including molecular biology, cancer research, biochemistry, materials chemistry, and clinical biochemistry.

Their research addresses key topics such as cancer, hypoxia, and metabolism; enzyme structure and function; metabolism and genetic disorders; epigenetics and DNA methylation; RNA modifications and cancer; mitochondrial function and pathology; and amino acid enzymes and metabolism.

Ding has published extensively in various scientific journals and frequently contributes to the following venues:

  • Nature Communications
  • Structure
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Journal of Biological Chemistry
  • Nature Cancer

Their recent notable papers include:

  • "Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2," 2022, Nature Microbiology
  • "Protein-metabolite interactomics of carbohydrate metabolism reveal regulation of lactate dehydrogenase," 2023, Science
  • "Aldolase B suppresses hepatocellular carcinogenesis by inhibiting G6PD and pentose phosphate pathways," 2020, Nature Cancer
  • "HBO1 is a versatile histone acyltransferase critical for promoter histone acylations," 2021, Nucleic Acids Research
  • "Structural basis for self-cleavage prevention by tag:anti-tag pairing complementarity in type VI Cas13 CRISPR systems," 2021, Molecular Cell

Ding has collaborated frequently with several coauthors, highlighting ongoing research partnerships within their scientific community. Some of the most frequent collaborators are:

  • Tianlong Zhang
  • Pengkai Sun
  • Xingchen Chen
  • Tengfei Ma
  • Chunyan Yi

Their scholarly focus integrates biochemical pathways and molecular mechanisms underlying cancer and metabolic diseases, with a particular emphasis on enzyme function and regulatory processes at the molecular level. The intersection of metabolism and genetic disorders appears prominently in their work.

This profile outlines Jianping Ding's contribution to contemporary molecular biology and biochemistry through a combination of experimental insights and collaborative research published in high-impact scientific journals.

Best Publications

  • Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA

    Yu-Fei He;Bin-Zhong Li;Zheng Li;Peng Liu

  • Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA

    A Jacobo-Molina;J Ding;R G Nanni;A D Clark

  • Glioma-Derived Mutations in IDH1 Dominantly Inhibit IDH1 Catalytic Activity and Induce HIF-1α

    Shimin Zhao;Yan Lin;Wei Xu;Wenqing Jiang

  • Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance

    Chris Tantillo;Jianping Ding;Alfredo Jacobo-Molina;Raymond G. Nanni

  • Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA.

    Stefan G. Sarafianos;Kalyan Das;Chris Tantillo;Arthur D. Clark

  • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity

    Xiang Xu;Jingyue Zhao;Zhen Xu;Baozhen Peng

  • Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors

    Jianping Ding;Kalyan Das;Henri Moereels;Luc Koymans

  • Structure of unliganded HIV-1 reverse transcriptase at 2.7 A resolution: implications of conformational changes for polymerization and inhibition mechanisms.

    Y. Hsiou;J. Ding;K. Das;A. D. Clark

  • Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with β-branched amino acids

    Stefan G. Sarafianos;Kalyan Das;Arthur D. Clark;Jianping Ding

  • Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 A resolution.

    Jianping Ding;Kalyan Das;Yu Hsiou;Stefan G Sarafianos

  • Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant.

    Kalyan Das;Jianping Ding;Yu Hsiou;Arthur D. Clark

  • Structure of HIV-1 reverse transcriptase in a complex with the non-nucleoside inhibitor α-APA R 95845 at 2.8 å resolution

    J Ding;K Das;C Tantillo;W Zhang

  • Chromatin targeting of de novo DNA methyltransferases by the PWWP domain

    Ying-Zi Ge;Min-Tie Pu;Humaira Gowher;Hai-Ping Wu

  • Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design

    Xiang Xu;Yunqing Liu;Susan Weiss;Eddy Arnold

  • INSIGHTS INTO DNA POLYMERIZATION MECHANISMS FROM STRUCTURE AND FUNCTION ANALYSIS OF HIV-1 REVERSE TRANSCRIPTASE

    Premal H. Patel;Alfredo Jacobo-Molina;Jianping Ding;Chris Tantillo

  • The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance.

    Yu Hsiou;Jianping Ding;Jianping Ding;Kalyan Das;Arthur D Clark

  • Structure of HIV-1 reverse transcriptase/DNA complex at 7 Å resolution showing active site locations

    Edward Arnold;Alfredo Jacobo-Molina;Raymond G. Nanni;Roger L. Williams

  • Sensitivity of wild-type human immunodeficiency virus type 1 reverse transcriptase to dideoxynucleotides depends on template length; the sensitivity of drug-resistant mutants does not

    Paul L. Boyer;Chris Tantillo;Alfredo Jacobo-Molina;Raymond G. Nanni

  • Structural and molecular interactions of CCR5 inhibitors with CCR5.

    Kenji Maeda;Kenji Maeda;Debananda Das;Hiromi Ogata-Aoki;Hirotomo Nakata

  • Structures of HIV-1 RT-DNA complexes before and after incorporation of the anti-AIDS drug tenofovir.

    Steve Tuske;Steve Tuske;Stefan G Sarafianos;Stefan G Sarafianos;Arthur D Clark;Arthur D Clark;Jianping Ding;Jianping Ding;Jianping Ding

Frequent Co-Authors

Hualiang Jiang
Hualiang Jiang Chinese Academy of Sciences
Stephen Hughes
Stephen Hughes National Cancer Institute
Xu Shen
Xu Shen Nanjing University of Chinese Medicine
Eddy Arnold
Eddy Arnold Rutgers, The State University of New Jersey
Kalyan Das
Kalyan Das Rega Institute for Medical Research
Guoliang Xu
Guoliang Xu Fudan University
Yajun Guo
Yajun Guo Second Military Medical University
Stefan G. Sarafianos
Stefan G. Sarafianos University of Missouri
Guoping Zhao
Guoping Zhao Chinese Academy of Sciences
Kaixian Chen
Kaixian Chen Chinese Academy of Sciences

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