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Nova · Professor Researcher · re-ranking top 20…

Ji Liu

· Associate Professor Term; Director for Resident Research, Ophthalmology

Yale University · Ophthalmology, Visual Science

Active 1989–2024

h-index60
Citations14.9k
Papers358132 last 5y
Funding$17.0M3 active
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About

Ji Liu, MD, MS, is an Associate Professor of Ophthalmology & Visual Science at Yale University, where he also serves as the Director for Resident Research in Ophthalmology. He joined Yale Eye Center as an Assistant Professor in July 2013 and has a distinguished background in ophthalmology, with extensive training and research experience. Dr. Liu completed his medical degree at Hunan Medical University and earned his MS from Xiangya School of Medicine. He completed his internship at Brookdale University Hospital and Medical Center, followed by a research fellowship and associate position at the University of Pennsylvania School of Medicine. His ophthalmology residency was completed at George Washington University, where he was appointed Chief Resident and received an Interdisciplinary Research Fund award. After a year as a Clinical Glaucoma Fellow at Yale Eye Center, he joined Yale's faculty full-time. Dr. Liu's clinical expertise includes performing complex lens, iris, and glaucoma surgeries. He has contributed to the introduction of multiple novel glaucoma surgeries, including I-stent, I-track, and Xen Gel Stent, at Yale-New Haven Hospital. His dedication to patient care has helped many restore vision or prevent glaucoma progression. Recognized as Connecticut Magazine's Top Doctor in 2022, Dr. Liu is also passionate about medical education, working closely with students, residents, and fellows. His research interests encompass the medical and surgical management of glaucoma, ophthalmic laser procedures, cataract surgery, intraocular lens implants, complex anterior segment surgeries, and medical education. He has authored over fifty scientific publications, including papers and book chapters, and has been invited to present at regional, national, and international conferences.

Research topics

  • Biology
  • Biophysics
  • Biochemistry
  • Chemistry
  • Computer Science
  • Physics
  • Cell biology
  • Genetics
  • Stereochemistry
  • Microbiology
  • Crystallography

Selected publications

  • The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation

    Proceedings of the National Academy of Sciences · 2022 · 45 citations

    • Biophysics
    • Crystallography
    • Chemistry

    flagellar motor in a position that colocalizes with the stator. Cryogenic electron tomography reconstructions of the intact motor in whole wild-type cells and cells lacking FliL revealed that the periplasmic domain of FliL (FliL-C) forms 18 circumferentially positioned rings integrated with the 18 MotAB units. FliL-C formed partial rings in the crystal, and the crystal structure-based full ring model was consistent with the shape of the rings observed in situ. Our data suggest that each FliL ring is coaxially sandwiched between the MotA ring and the dimeric periplasmic MotB moiety of the stator unit and that the central hole of the FliL ring has density that is consistent with the plug/linker region of MotB in its extended, active conformation. Significant structural similarities were found between FliL-C and stomatin/prohibitin/flotillin/HflK/C domains of scaffolding proteins, suggesting that FliL acts as a scaffold. The binding energy released upon association of FliL with the stator units could be used to power the release of the plug helices. The finding that isolated FliL-C forms stable partial rings provides an insight into the putative mechanism by which the FliL rings assemble around the stator units.

  • Interconnecting solvent quality, transcription, and chromosome folding in Escherichia coli

    Cell · 2021 · 105 citations

    • Biology
    • Biophysics
    • Cell biology
  • c-di-GMP modulates type IV MSHA pilus retraction and surface attachment in Vibrio cholerae

    Nature Communications · 2020 · 102 citations

    • Biophysics
    • Chemistry
    • Microbiology

    Biofilm formation by Vibrio cholerae facilitates environmental persistence, and hyperinfectivity within the host. Biofilm formation is regulated by 3',5'-cyclic diguanylate (c-di-GMP) and requires production of the type IV mannose-sensitive hemagglutinin (MSHA) pilus. Here, we show that the MSHA pilus is a dynamic extendable and retractable system, and its activity is directly controlled by c-di-GMP. The interaction between c-di-GMP and the ATPase MshE promotes pilus extension, whereas low levels of c-di-GMP correlate with enhanced retraction. Loss of retraction facilitated by the ATPase PilT increases near-surface roaming motility, and impairs initial surface attachment. However, prolonged retraction upon surface attachment results in reduced MSHA-mediated surface anchoring and increased levels of detachment. Our results indicate that c-di-GMP directly controls MshE activity, thus regulating MSHA pilus extension and retraction dynamics, and modulating V. cholerae surface attachment and colonization.

  • Molecular mechanism for rotational switching of the bacterial flagellar motor

    Nature Structural & Molecular Biology · 2020 · 136 citations

    Senior authorCorresponding
    • Computer Science
    • Biophysics
    • Chemistry

Recent grants

Frequent coauthors

  • Yunjie Chang

    Zhejiang University

    40 shared
  • Kenneth A. Taylor

    Florida State University

    39 shared
  • Md A. Motaleb

    Vidyasagar University

    33 shared
  • James K Stoops

    The University of Texas Health Science Center at Houston

    25 shared
  • Chunhao Li

    Virginia Commonwealth University

    24 shared
  • Xiaowei Zhao

    Helix (United States)

    21 shared
  • Shiwei Zhu

    21 shared
  • Bo Hu

    21 shared

Labs

Education

  • M.D., not specified

    not specified

  • M.S., not specified

    not specified

Awards & honors

  • 2004 Annual Research Award

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