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Su, Ming-Yuan
Associate Professor
sumy@sustech.edu.cn

SELF-INTRODUCTION:

Dr. Su, Ming-Yuan is currently an Associate Professor and doctoral supervisor in the School of Medicine. She received her phD degree from National Taiwan University in 2015 and did her postdoc training in UC Berkeley and Lawrence Berkeley National Laboratory during 2016-2021. Dr. Su joined the School of Medicine, SUSTech as an Assistant Professor since May 2021. She has published papers on Nature, Molecular Cell, Nature Communication and Autophagy etc.  Su lab aims to integrate the structural biology, biochemistry, molecular biology and mass spectrometry to understand the regulation mechanism of lysosomal signalling, and how the position and biogenesis of lysosomes are controlled as well as the relevant diseases.


EDUCATION:

2012-08- 2015-08   Ph.D,  Institute of Biochemical Sciences, National Taiwan University

2010-08- 2012-07   M.S.,  Institute of Biochemical Sciences, National Taiwan University

2005-08- 2009-07   B.S.,   Department of Chemistry, National Taiwan University

 

WOKRING EXPERIENCE:

2022-06-present  School of Medicine, Southern University of Science and Technology(SUSTech), Associate Professor

2021-05-2022-05  School of Medicine, Southern University of Science and Technology(SUSTech), Assistant Professor

2016-08-2021-03  University of California, Berkeley/Lawrence Berkeley National Laboratory, Postdoc

2015-09-2016-07  Academia Sinica, Distinguished Postdoctoral Scholar

                     

HONORS AND AWARDS:

2019-2021 AFTD Basic Science Postdoctoral Fellowship

2016 Distinguished Postdoctoral Scholar, Academia Sinica

2012-2014 Postgraduate Scholarship, Macau Government- Comiss?o Técnica de Atribui??o de Bolsas para Estudos Pós-Graduados

2011, 2013 Outstanding Overseas Student Scholarship, National Taiwan University

2012 Dean’s Award, College of Life Sciences, National Taiwan University

2005-2009 College Scholarship, Macau Government- Direc??o dos Servi?os de Educa??o e Juventude

 

Research:

We combine biochemistry, cell biology, structural mass spectrometry, and structural biology to study the structure and mechanisms of protein machineries in lysosomal biology and protein homeostasis

 

PUBLICATIONS:

After 2021:

8. Su M-Y*,#, Teng F*, Wang S*, Mai X, Zeng H, Li J, Song X, Wang X and Stjepanovic G. Cryo-EM structures of amino acid sensors bound to the human GATOR2 complex. Cell Reports. 2025. https://doi.org/10.1016/j.celrep.2025.116088. (*equal contribution)

7. Zhang J*, Chen C*, Chen X*, Liao K, Li F, Song X, Liu C, Su M-Y, Sun H, Hou T, Tan C, Fang L#, Rao H#. Linker-free PROTACs efficiently induce the degradation of oncoproteins. Nat Commun. 2025 May 23;16(1):4794. (*equal contribution)

6. Wang Y, Liu M, Wang S, Mai X, Wang X, Teng F, Lyn T, Su M-Y#, Stjepanovic G#.  Mechanism of D-type cyclin recognition by the AMBRA1 E3 ligase receptor. Sci Adv. 2025 May 23;11(21):eadu8708.

5. Zhang J, Chen X, Chen C, Li F, Song X, Liu C, Liao K, Su M-Y, Tan CSH, Fang L, Rao H. Distinct Amino Acid-Based PROTACs Target Oncogenic Kinases for Degradation in Non-Small Cell Lung Cancer (NSCLC). J Med Chem. 2024, 67(16):13666-13680.

4. Mai X, Wang Y, Wang X, Liu M, Teng F, Liu Z, Su M-Y#, Stjepanovic G#. Structural basis for membrane remodelling by the AP5:SPG11-SPG15 complex. Nature Structural & Molecular Biology. 2025. 10.1038/s41594-025-01500-0

3. Teng F*, Wang Y*, Liu M,  Tian S, Stjepanovic G#, Su M-Y#. 2023. Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme. Structure 31, 1431-1440 e1435. (*equal contribution)

2. Liu M, Wang Y, Teng F, Wang X, Mai X, Su M-Y#, Stjepanovic G#. 2023. Structural basis for substrate recruitment by AMBRA1 E3 ligase receptor. Nat Commun. 2023 Nov 22;14(1):7631.

1. Su M-Y, Fromm SA, Remis J, Toso DB, Hurley JH. 2021. Structural basis for the ARF GAP activity and specificity of the C9orf72 complex. Nature Communications 12(1):3786.


Before 2021:

1. Su M-Y, Fromm SA, Zoncu R, Hurley JH. 2020. Structure of the C9orf72 Arf GAP complex haploinsufficient in ALS and FTD. Nature 585(7824):251-255.

2. Turco E*, Witt M*, Abert C*, Bock-Bierbaum T*, Su M-Y*, Trapannone R, Sztacho M, Danieli A, Shi X, Zaffagnini G, GamperA, Schuschnig M, Fracchiolla D, Bernklau D, Romanov J, Hartl M, Hurley JH, Daumke O, Martens S. 2019. FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates. Mol Cell 74:330-346.e11. (*equal contribution)

3. Turco E, Witt M, Abert C, Bock-Bierbaum T, Su M-Y, Trapannone R, Sztacho M, Danieli A, Shi X, Zaffagnini G, Gamper A, Schuschnig M, Fracchiolla D, Bernklau D, Romanov J, Hartl M, Hurley JH, Daumke O, Martens S. 2019. How RB1CC1/FIP200 claws its way to autophagic engulfment of SQSTM1/p62-ubiquitin condensates. Autophagy 15:1475–1477.

4. Su M-Y, Morris KL, Kim DJ, Fu Y, Lawrence R, Stjepanovic G, Zoncu R, Hurley JH. 2017. Hybrid Structure of the RagA/CRagulator mTORC1 Activation Complex. Mol Cell 68:835-846.e3.

5. Su M-Y, Som N, Wu C-Y, Su S-C, Kuo Y-T, Ke L-C, Ho M-R, Tzeng S-R, Teng C-H, Mengin-Lecreulx D, Reddy M, Chang C-I. 2017. Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc. Nat Commun 8:1516.

6. Lin C-C, Su S-C, Su M-Y, Liang P-H, Feng C-C, Wu S-H, Chang C-I. 2016. Structural Insights into the Allosteric Operation of the Lon AAA+ Protease. Structure 24:667–675.

7. Su M-Y, Peng W-H, Ho M-R, Su S-C, Chang Y-C, Chen G-C, Chang C-I. 2015. Structure of yeast Ape1 and its role in autophagic vesicle formation. Autophagy 11:1580–1593.

8. Chao S-W, Su M-Y, Chiou L-C, Chen L-C, Chang C-I, Huang W-J. 2015. Total Synthesis of Hispidulin and the Structural Basis for Its Inhibition of Proto-oncogene Kinase Pim-1. J Nat Prod 78:1969–1976. 

9. Su M-Y, Chang C-I, Chang C-F. 2013. 1H, 13C and 15N resonance assignments of the pyrin domain from human PYNOD. Biomol NMR Assign 7:141–143.

10. Su M-Y, Kuo C-I, Chang C-F, Chang C-I. 2013. Three-dimensional structure of human NLRP10/PYNOD pyrin domain reveals a homotypic interaction site distinct from its mouse homologue. PLoS ONE 8:e67843.



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