M
Ming Lei
Researcher at University of Michigan
Publications - 74
Citations - 10371
Ming Lei is an academic researcher from University of Michigan. The author has contributed to research in topics: Telomere & Telomere-binding protein. The author has an hindex of 37, co-authored 66 publications receiving 9513 citations. Previous affiliations of Ming Lei include Chinese Academy of Sciences & University of Pittsburgh.
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Journal ArticleDOI
A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression
Kevin C. Wang,Yul W. Yang,Bo Liu,Amartya Sanyal,Ryan Corces-Zimmerman,Yong Chen,Bryan R. Lajoie,Angeline Protacio,Ryan A. Flynn,Rajnish A. Gupta,Joanna Wysocka,Ming Lei,Job Dekker,Jill A. Helms,Howard Y. Chang +14 more
TL;DR: OTTIP RNA binds the adaptor protein WDR5 directly and targets WDR 5/MLL complexes across HOXA, driving histone H3 lysine 4 trimethylation and gene transcription.
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A hierarchy of timescales in protein dynamics is linked to enzyme catalysis.
Katherine A. Henzler-Wildman,Ming Lei,Vu Hong Thai,S. Jordan Kerns,Martin Karplus,Dorothee Kern +5 more
TL;DR: It is shown that pico- to nano-second timescale atomic fluctuations in hinge regions of adenylate kinase facilitate the large-scale, slower lid motions that produce a catalytically competent state.
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Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
TL;DR: Four additional c-Src structures in which this segment adopts an ordered but inhibitory conformation are reported, in which the ordered activation loop forms an alpha helix that stabilizes the inactive conformation of the kinase domain, blocks the peptide substrate-binding site, and prevents Tyr-416 phosphorylation.
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The POT1-TPP1 telomere complex is a telomerase processivity factor
TL;DR: The crystal structure of a domain of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the β-subunit of the telomere end-binding protein of a ciliated protozoan, suggesting that TPP1 is the missing β- subunit of human POT1 protein.
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Structure of PAK1 in an Autoinhibited Conformation Reveals a Multistage Activation Switch
Ming Lei,Wange Lu,Wuyi Meng,Maria Carla Parrini,Michael J. Eck,Bruce J. Mayer,Stephen C. Harrison +6 more
TL;DR: The p21-activated kinases, stimulated by binding with GTP-liganded forms of Cdc42 or Rac, modulate cytoskeletal actin assembly and activate MAP-kinase pathways and a related switch has been seen in the Wiskott-Aldrich syndrome protein (WASP).