Rong Li

Last updated
Rong Li
RongLi.png
Born
Rong Li

1967 (age 56–57)
Beijing
NationalityAmerican
Alma mater Yale University (B.S., M.S.)
University of California, San Francisco (Ph.D.)
University of California, Berkeley (postdoctoral fellowship)
Known for Cell biology
Cellular asymmetry
Cell dynamics
Aneuploidy
Cell morphology
Eukaryotic cells
Oogenesis
Cell migration
Awards Bloomberg Distinguished Professorships (2015)
William Neaves Award (2010-2012)
Hoechst Marion Roussel Award (now the Aventis Award) (1999-2001)
Scientific career
Fields Cell biology
Evolutionary biology
Chemical engineering
Biomolecular engineering
Institutions Johns Hopkins University Stowers Institute for Medical Research
Doctoral advisor Andrew W Murray
Website cellbio.jhmi.edu/people/faculty/rong-li-phd

Rong Li is the Director of Mechanobiology Institute, a Singapore Research Center of Excellence, at the National University of Singapore. She is a Distinguished Professor [1] at the National University of Singapore's Department of Biological Sciences and Bloomberg Distinguished Professor [2] of Cell Biology and Chemical & Biomolecular Engineering at the Johns Hopkins School of Medicine and Whiting School of Engineering. She previously served as Director of Center for Cell Dynamics in the Johns Hopkins School of Medicine’s Institute for Basic Biomedical Sciences. [3] [4] She is a leader in understanding cellular asymmetry, division and evolution, and specifically, in how eukaryotic cells establish their distinct morphology and organization in order to carry out their specialized functions.

Contents

Biography

Rong Li was born in Beijing, China in 1967. She was the first high school graduate from the People's Republic of China admitted to Yale University. [3] She went on to graduate in four years from Yale University Summa Cum Laude and with Distinction in Major with a combined B.S. and M.S. in Biophysics & Biochemistry. She then earned a Ph.D. in Cell Biology through the Herbert W. Boyer Program in Biological Sciences (PIBS) at the University of California, San Francisco, and subsequently completed a postdoctoral fellowship at the University of California, Berkeley in Molecular Cell Biology. [5] In 1994, she accepted an assistant professorship in cell biology at Harvard University, rising to the associate level in 2000. From 2005 to 2015, she was an Investigator at the Stowers Institute for Medical Research and an affiliated Professor in the Department of Molecular and Integrative Physiology at the University of Kansas School of Medicine.

In July 2015, Li was named a Bloomberg Distinguished Professor at Johns Hopkins University for her accomplishments as an interdisciplinary researcher and excellence in teaching. [6] [7] The Bloomberg Distinguished Professorship program was established in 2013 by a gift from Michael Bloomberg. [8] [9] Li holds appointments in the Johns Hopkins School of Medicine’s Department of Cell Biology and the Whiting School of Engineering’s Department of Chemical and Biomolecular Engineering. [10] [11] In 2019, Rong Li was recruited by National University of Singapore to serve as Director of the Mechanobiology Institute.

In 2019, Li won the Sandra K. Masur Senior Leadership Award from The American Society for Cell Biology (ASCB). [12] This award recognizes individuals for scientific achievements and a record of active leadership in mentoring women and individuals from underrepresented groups in their scientific careers. [13] In 2024, she was elected as the ASCB president of Year 2026. [14]

Research

Rong Li is an accomplished investigator in the area of cell dynamics – the interrogation of biological function at the highest possible resolution in space and time. [15] Li's research has entailed integrative approaches, encompassing biochemistry, genetics, quantitative imaging and fluorescence spectroscopy, mathematical modeling, quantitative genomics and proteomics. [16]

To understand the pathways that control cell motility, [17] tissue morphogenesis, [18] and neuronal development, Li monitors both physical and biochemical reactions that overlap spatially and change rapidly, but occur only locally within a complex environment. [16] Her broad goal is to understand how eukaryotic cells establish their distinct morphology and organization in order to carry out their specialized functions with applications in development and cancer. [19] [20] [21] Specifically, how eukaryotic cells generate pattern through self-organization with or without environmental cues, accomplish division or motility through coordinated structural rearrangements and force production, [22] and, when challenged with stress and roadblocks, evolve innovative solutions to main vitality and functionality. [23] A key part of her research is exploring how the ability to evolve is built into cellular systems and how that ability gives rise to a cell's properties. Li has published several seminal papers on the impact of aneuploidy on cellular fitness, gene expression, stress adaptation, and genome instability. As aneuploidy and chromosome instability are hallmarks of cancer, her results on how aneuploidy fuels the evolution of cellular adaptation and drug resistance have direct relevance to the understanding of cancer evolution and disease progression. Li has also studied the molecular mechanisms that lead to oocyte maturation, [24] [25] which can contribute to “advances in the treatment of infertility and the field of regenerative medicine.” [26]

Her early work with Andrew Murray at Harvard University provided the first insight into the genetic basis of the spindle assembly checkpoint. [27] [28] The paper documenting this work is one of the Nature Milestones in Cell Division. [29] Li has subsequently made a number of significant discoveries in the area of mitotic exit control [30] and cytokinesis. [31] [32] She is recognized as a leader in the study of cell polarity in the context of morphogenesis and asymmetric cell division, and has been at the forefront of using mathematical and biophysical approaches to understand cell polarity as a self-organizing, dynamical system. [33] [34] This advancement of quantitative and predictive understanding of cellular behavior relates to health, to learning and to human individuality, especially her research on topics such as cell polarity, asymmetric cell division, polycystic kidney disease, and adaptive evolution. [35]

Li was one of the first to demonstrate the critical in vivo role for the Arp2/3 complex and WASP family proteins in the control of actin filament assembly, and to show through in vitro biochemistry that the Arp2/3 complex is an actin nucleator activated by WASP family members. [36] In collaboration with Drs. Dorit Hanein, Niels Volkmann and Thomas D. Pollard, her laboratory helped determine the three-dimensional structure of the Arp2/3 complex in actin branch junctions. [37] Li's recent work has revealed insights into the in vivo function of Arp2/3-nucleated dendritic actin network in mammalian asymmetric cell division and cell motility. [38]

Li is one of the pioneers using state-of-the-art microscopy technologies to study aging and protein homeostasis (proteostasis), and uncovered some fundamental aspects of protein aggregation in cells. Her laboratory discovered endoplasmic reticulum (ER) and mitochondria-based retention of protein aggregates during aggregate formation and cell division [39] and mitochondrial import of aggregation-prone proteins. [40] Her lab also discovered that (TDP-43) protein aggregation directly occurs at ER-exit sites to impair ER-to-Golgi transport. [41]

Publications

Li has more than 140 publications, 18,000 citations in Google Scholar and an h-index of 72, [42] with many of her papers appearing in top journals such as Cell , Nature , Science , Nature Cell Biology , Molecular Biology of the Cell , Journal of Cell Biology and the Proceedings of the National Academy of Sciences of the United States of America .

Books and book chapters

source: [16]

Highly cited articles

source: [43]

See also

Related Research Articles

<span class="mw-page-title-main">Cytoskeleton</span> Network of filamentous proteins that forms the internal framework of cells

The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components: microfilaments, intermediate filaments, and microtubules, and these are all capable of rapid growth or disassembly depending on the cell's requirements.

<span class="mw-page-title-main">Microfilament</span> Filament in the cytoplasm of eukaryotic cells

Microfilaments, also called actin filaments, are protein filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton. They are primarily composed of polymers of actin, but are modified by and interact with numerous other proteins in the cell. Microfilaments are usually about 7 nm in diameter and made up of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement, cell motility, changes in cell shape, endocytosis and exocytosis, cell contractility, and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors. Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement.

<span class="mw-page-title-main">Actin</span> Family of proteins

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

<span class="mw-page-title-main">Wiskott–Aldrich syndrome protein</span> Mammalian protein found in humans

The Wiskott–Aldrich syndrome protein (WASp) is a 502-amino acid protein expressed in cells of the hematopoietic system that in humans is encoded by the WAS gene. In the inactive state, WASp exists in an autoinhibited conformation with sequences near its C-terminus binding to a region near its N-terminus. Its activation is dependent upon CDC42 and PIP2 acting to disrupt this interaction, causing the WASp protein to 'open'. This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex. Activated Arp2/3 nucleates new F-actin.

<span class="mw-page-title-main">Podosome</span>

Podosomes are conical, actin-rich structures found on the outer surface of the plasma membrane of animal cells. Their size ranges from approximately 0.5 μm to 2.0 μm in diameter. While usually situated on the periphery of the cellular membrane, these unique structures display a polarized pattern of distribution in migrating cells, situating at the front border between the lamellipodium and lamellum. Their primary purpose is connected to cellular motility and invasion; therefore, they serve as both sites of attachment and degradation along the extracellular matrix. Many different specialized cells exhibit these dynamic structures such as invasive cancer cells, osteoclasts, vascular smooth muscle cells, endothelial cells, and certain immune cells like macrophages and dendritic cells.

Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants. Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another, or in the cell cortex as a barrier to the diffusion of membrane-bound proteins.

The Rho family of GTPases is a family of small signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions.

<span class="mw-page-title-main">ACTR3</span> Mammalian protein found in Homo sapiens

Actin-related protein 3 is a protein that in humans is encoded by the ACTR3 gene.

<span class="mw-page-title-main">ACTR2</span> Mammalian protein found in Homo sapiens

Actin-related protein 2 is a protein that in humans is encoded by the ACTR2 gene.

<span class="mw-page-title-main">WASL (gene)</span> Mammalian protein found in Homo sapiens

Neural Wiskott–Aldrich syndrome protein is a protein that in humans is encoded by the WASL gene.

<span class="mw-page-title-main">WIPF1</span> Protein-coding gene in the species Homo sapiens

WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.

<span class="mw-page-title-main">ARPC1B</span> Mammalian protein found in Homo sapiens

Actin-related protein 2/3 complex subunit 1B is a protein that in humans is encoded by the ARPC1B gene.

<span class="mw-page-title-main">ANLN</span> Mammalian protein found in Homo sapiens

Anillin is a conserved protein implicated in cytoskeletal dynamics during cellularization and cytokinesis. The ANLN gene in humans and the scraps gene in Drosophila encode Anillin. In 1989, anillin was first isolated in embryos of Drosophila melanogaster. It was identified as an F-actin binding protein. Six years later, the anillin gene was cloned from cDNA originating from a Drosophila ovary. Staining with anti-anillin antibody showed the anillin localizes to the nucleus during interphase and to the contractile ring during cytokinesis. These observations agree with further research that found anillin in high concentrations near the cleavage furrow coinciding with RhoA, a key regulator of contractile ring formation.

Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis. Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to humans.

<span class="mw-page-title-main">Cell polarity</span> Polar morphology of a cell, a specific orientation of the cell structure

Cell polarity refers to spatial differences in shape, structure, and function within a cell. Almost all cell types exhibit some form of polarity, which enables them to carry out specialized functions. Classical examples of polarized cells are described below, including epithelial cells with apical-basal polarity, neurons in which signals propagate in one direction from dendrites to axons, and migrating cells. Furthermore, cell polarity is important during many types of asymmetric cell division to set up functional asymmetries between daughter cells.

<span class="mw-page-title-main">Actin assembly-inducing protein</span>

The Actin assembly-inducing protein (ActA) is a protein encoded and used by Listeria monocytogenes to propel itself through a mammalian host cell. ActA is a bacterial surface protein comprising a membrane-spanning region. In a mammalian cell, the bacterial ActA interacts with the Arp2/3 complex and actin monomers to induce actin polymerization on the bacterial surface generating an actin comet tail. The gene encoding ActA is named actA or prtB.

Actin remodeling is the biochemical process that allows for the dynamic alterations of cellular organization. The remodeling of actin filaments occurs in a cyclic pattern on cell surfaces and exists as a fundamental aspect to cellular life. During the remodeling process, actin monomers polymerize in response to signaling cascades that stem from environmental cues. The cell's signaling pathways cause actin to affect intracellular organization of the cytoskeleton and often consequently, the cell membrane. Again triggered by environmental conditions, actin filaments break back down into monomers and the cycle is completed. Actin-binding proteins (ABPs) aid in the transformation of actin filaments throughout the actin remodeling process. These proteins account for the diverse structure and changes in shape of Eukaryotic cells. Despite its complexity, actin remodeling may result in complete cytoskeletal reorganization in under a minute.

<span class="mw-page-title-main">Arp2/3 complex</span> Macromolecular complex

Arp2/3 complex is a seven-subunit protein complex that plays a major role in the regulation of the actin cytoskeleton. It is a major component of the actin cytoskeleton and is found in most actin cytoskeleton-containing eukaryotic cells. Two of its subunits, the Actin-Related Proteins ARP2 and ARP3, closely resemble the structure of monomeric actin and serve as nucleation sites for new actin filaments. The complex binds to the sides of existing ("mother") filaments and initiates growth of a new ("daughter") filament at a distinctive 70-degree angle from the mother. Branched actin networks are created as a result of this nucleation of new filaments. The regulation of rearrangements of the actin cytoskeleton is important for processes like cell locomotion, phagocytosis, and intracellular motility of lipid vesicles.

Susanne Marie Rafelski is an American biochemist. Rafelski studied biochemistry at the University of Arizona with David Galbraith. She obtained her PhD in 2005 from Stanford University, under supervision of Julie Theriot.

<span class="mw-page-title-main">David G. Drubin</span> American biologist, academic, and researcher

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References

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  2. ↑ "Bloomberg Distinguished Professorships".
  3. 1 2 Brooks, Kelly "Four new Bloomberg Distinguished Professors named at Johns Hopkins ", JHU Hub, Baltimore, 08 July 2015. Retrieved on 11 August 2015.
  4. ↑ "Center for Cell Dynamics Director" . Retrieved 2015-09-29.
  5. ↑ "Rong Li Biographical Sketch" (PDF). Retrieved 2015-08-12.
  6. ↑ "Michael R. Bloomberg commits $350 million to Johns Hopkins for transformational academic initiative". 2013-01-26.
  7. ↑ Anderson, Nick. "Bloomberg pledges $350 million to Johns Hopkins University", The Washington Post, Washington, D.C., 23 January 2013. Retrieved on 12 March 2015.
  8. ↑ Barbaro, Michael. "$1.1 Billion in Thanks From Bloomberg to Johns Hopkins", The New York Times , New York, 26 January 2013. Retrieved on 1 March 2015.
  9. ↑ "Michael R. Bloomberg Commits $350 Million to Johns Hopkins for Transformational Academic Initiative 2013".
  10. ↑ "Department of Chemical and Biomolecular Engineering Faculty Page: Rong Li" . Retrieved 2015-09-29.
  11. ↑ Brooks, Kelly. "Four new Bloomberg Distinguished Professors named at Johns Hopkins", The Hub, Baltimore, 8 July 2015. Retrieved on 11 July 2015.
  12. ↑ Sun, Gordon. "Rong Li wins the 2019 Sandra K Masur Senior Leadership Award from ASCB | Rong Li Lab" . Retrieved 2021-10-26.
  13. ↑ "Sandra K. Masur Senior Leadership Award". ASCB. Retrieved 2021-10-26.
  14. ↑ "Rong Li Elected 2026 ASCB President".
  15. ↑ Senior, Kathryn (1 April 2010). "Spotlight: An interview with Rong Li". Development. 137 (7): 1015–1016. doi: 10.1242/dev.050138 . PMID   20215341.
  16. 1 2 3 "Li CV" (PDF). Retrieved 2015-09-30.
  17. ↑ Winter, Dirk; Podtelejnikov, Alexandre; Mann, Matthias; Li, Rong (1 July 1997). "The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches". Current Biology. 7 (7): 519–529. Bibcode:1997CBio....7..519W. doi: 10.1016/S0960-9822(06)00223-5 . PMID   9210376. S2CID   52837402.
  18. ↑ Slaughter, Brian; Das, Arupratan; Schwartz, Joel; Rubinstein, Boris; Li, Rong (15 December 2009). "Dual Modes of Cdc42 Recycling Fine-Tune Polarized Morphogenesis". Developmental Cell. 17 (6): 823–835. doi:10.1016/j.devcel.2009.10.022. PMC   2805562 . PMID   20059952.
  19. ↑ Pavelka, Norman; Rancati, Giulia; Li, Rong (1 December 2010). "Dr Jekyll and Mr Hyde: role of aneuploidy in cellular adaptation and cancer". Current Opinion in Cell Biology. 22 (6): 809–815. doi:10.1016/j.ceb.2010.06.003. PMC   2974767 . PMID   20655187.
  20. ↑ Potopova, Tamara; Zhu, Jin; Li, Rong (1 December 2013). "Aneuploidy and chromosomal instability: a vicious cycle driving cellular evolution and cancer genome chaos". Cancer and Metastasis Reviews. 32 (3): 377–389. doi:10.1007/s10555-013-9436-6. PMC   3825812 . PMID   23709119.
  21. ↑ Ye, J; Chu, T; Li, Rong; Niu, Y; Xia, J; Shao, M; Han, B (1 August 2015). "Pol ζ polymorphisms are associated with platinum based chemotherapy response and side effects among non-small cell lung cancer patients". Neoplasma. 62 (5): 833–839. doi: 10.4149/neo_2015_101 . PMID   26278154.
  22. ↑ Lippincott, John; Li, Rong (26 January 1998). "Sequential Assembly of Myosin II, an IQGAP-like Protein, and Filamentous Actin to a Ring Structure Involved in Budding Yeast Cytokinesis". Journal of Cell Biology . 140 (2): 355–366. doi:10.1083/jcb.140.2.355. PMC   2132585 . PMID   9442111.
  23. ↑ "Cell Bio Faculty Webpage" . Retrieved 2015-08-16.
  24. ↑ Yi, Kexi; Li, Rong (1 October 2012). "Actin cytoskeleton in cell polarity and asymmetric division during mouse oocyte maturation". Cytoskeleton . 69 (10): 727–737. doi: 10.1002/cm.21048 . PMID   22753278.
  25. ↑ Yi, Kexi; Rubinstein, Boris; Unruh, Jay; Guo, Fengli; Slaughter, Brian; Li, Rong (25 September 2013). "Sequential actin-based pushing forces drive meiosis I chromosome migration and symmetry breaking in oocytes". Journal of Cell Biology . 200 (5): 567–576. doi:10.1083/jcb.201211068. PMC   3587830 . PMID   23439682.
  26. ↑ "Unraveling the mysteries of the oocyte" (PDF). Retrieved 2015-08-12.
  27. ↑ Li, Rong; Murray, Andrew W. (1991). "Feedback control of mitosis in budding yeast". Cell. 66 (3): 519–31. doi:10.1016/0092-8674(81)90015-5. PMID   1651172. S2CID   11306198.
  28. ↑ Li, Rong (27 April 1999). "Bifurcation of the mitotic checkpoint pathway in budding yeast". PNAS . 96 (9): 4989–4994. Bibcode:1999PNAS...96.4989L. doi: 10.1073/pnas.96.9.4989 . PMC   21804 . PMID   10220406.
  29. ↑ Nature Publishing Group (December 2001). "Milestones in Cell Division: Milestone 18". Nature Reviews Molecular Cell Biology. Nature Publishing Group: 1–2. doi:10.1038/nrm.2018.41 . Retrieved 2015-09-30.
  30. ↑ Bosl, William; Li, Rong (6 May 2005). "Mitotic-Exit Control as an Evolved Complex System". Cell . 121 (3): 325–333. doi: 10.1016/j.cell.2005.04.006 . PMID   15882616. S2CID   18553706.
  31. ↑ VerPlank, Lynn; Li, Rong (1 May 2005). "Cell Cycle-regulated Trafficking of Chs2 Controls Actomyosin Ring Stability during Cytokinesis". Molecular Biology of the Cell . 16 (5): 2529–2543. doi:10.1091/mbc.E04-12-1090. PMC   1087255 . PMID   15772160.
  32. ↑ Li, Rong (1 December 2007). "Cytokinesis in development and disease: variations on a common theme". Cellular and Molecular Life Sciences . 64 (23): 3044–3058. doi:10.1007/s00018-007-7285-6. PMC   11136365 . PMID   17882379. S2CID   8118193.
  33. ↑ Li, Rong; Bowerman, Bruce (22 March 2010). Symmetry Breaking in Biology. Vol. 2. Cold Spring Harbor Laboratory Press. pp. a003475. doi:10.1101/cshperspect.a003475. ISBN   978-0879698898. PMC   2829966 . PMID   20300216.{{cite book}}: |journal= ignored (help)
  34. ↑ Stowers Institute for Medical Research (13 December 2007). "Rong Li Lab reports protein interactions of MAP kinase signaling pathway". EurekaAlert!. American Association for the Advancement of Science . Retrieved 2015-09-29.
  35. ↑ "Cell Biology Faculty Profile: Rong Li, Ph.D." Retrieved 2015-08-12.
  36. ↑ Egile C, Rouiller I, Xu XP, Volkmann N, Li R, Hanein D (November 2005). "Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions". PLOS Biol. 3 (11): e383. doi: 10.1371/journal.pbio.0030383 . PMC   1278936 . PMID   16262445. Open Access logo PLoS transparent.svg
  37. ↑ Volkmann, Niels; Page, Christopher; Li, Rong; Hanein, Dorit (1 June 2014). "Three-dimensional reconstructions of actin filaments capped by Arp2/3 complex". European Journal of Cell Biology . 93 (5–6): 179–183. doi:10.1016/j.ejcb.2014.01.003. PMC   4110117 . PMID   24552843.
  38. ↑ Suraneni, Praveen; Fogelson, Ben; Rubinstein, Boris; Noguera, Philippe; Volkmann, Niels; Hanein, Dorit; Mogilner, Alex; Li, Rong (1 March 2015). "A mechanism of leading-edge protrusion in the absence of Arp2/3 complex". Molecular Biology of the Cell . 26 (5): 901–912. doi:10.1091/mbc.E14-07-1250. PMC   4342026 . PMID   25568333.
  39. ↑ Zhou, et al. (2014). "Organelle-based aggregation and retention of damaged proteins in asymmetrically dividing cells". Cell. 159 (3): 530–542. doi:10.1016/j.cell.2014.09.026. PMC   6726438 . PMID   25417105.
  40. ↑ Ruan, et al. (2017). "Cytosolic proteostasis through importing of misfolded proteins into mitochondria". Nature. 543 (7645): 443–446. Bibcode:2017Natur.543..443R. doi:10.1038/nature21695. PMC   5793917 . PMID   28241148.
  41. ↑ Wu, et al. (2024). "TDP43 aggregation at ER-exit sites impairs ER-to-Golgi transport". bioRxiv.
  42. ↑ "Rong Li, PhD". scholar.google.com. Retrieved 2021-05-19.
  43. ↑ Google Scholar "Author: Rong Li, PhD", Google Scholar , 12 August 2015. Retrieved on 12 August 2015.
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