Huilin Li

ORCID: 0000-0001-8085-8928
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About
Contact & Profiles
Research Areas
  • DNA Repair Mechanisms
  • Bacterial Genetics and Biotechnology
  • Ubiquitin and proteasome pathways
  • RNA and protein synthesis mechanisms
  • DNA and Nucleic Acid Chemistry
  • Genomics and Chromatin Dynamics
  • Enzyme Structure and Function
  • Biochemical and Molecular Research
  • Photosynthetic Processes and Mechanisms
  • Glycosylation and Glycoproteins Research
  • RNA modifications and cancer
  • Epigenetics and DNA Methylation
  • Endoplasmic Reticulum Stress and Disease
  • Peptidase Inhibition and Analysis
  • Advanced biosensing and bioanalysis techniques
  • Ion channel regulation and function
  • Protein Structure and Dynamics
  • CRISPR and Genetic Engineering
  • ATP Synthase and ATPases Research
  • Microtubule and mitosis dynamics
  • Cellular transport and secretion
  • X-ray Diffraction in Crystallography
  • Bacteriophages and microbial interactions
  • Escherichia coli research studies
  • Cardiac electrophysiology and arrhythmias

Van Andel Institute
2016-2025

Northwest A&F University
2008-2025

Shanghai Pudong New Area Gongli Hospital
2025

Shenyang Agricultural University
2025

Second Military Medical University
2005-2025

Institute of Agricultural Resources and Regional Planning
2025

Chinese Academy of Agricultural Sciences
2025

Beijing Technology and Business University
2024-2025

Nanjing Forestry University
2023-2024

Zhongnan Hospital of Wuhan University
2022-2024

During pre-replication complex (pre-RC) formation, origin recognition (ORC), Cdc6, and Cdt1 cooperatively load the 6-subunit mini chromosome maintenance (MCM2-7) onto DNA. Loading of MCM2-7 is a prerequisite for DNA licensing that restricts replication to once per cell cycle. S phase functions as part replicative helicase but within pre-RC inactive. The organization helicases before after loading has been studied in bacteria viruses not eukaryotes major importance understanding mechanism...

10.1073/pnas.0911500106 article EN Proceedings of the National Academy of Sciences 2009-11-13

The structure of epothilone A, bound to alpha,beta-tubulin in zinc-stabilized sheets, was determined by a combination electron crystallography at 2.89 angstrom resolution and nuclear magnetic resonance-based conformational analysis. complex explains both the broad-based structure-activity relationship known mutational resistance profile. Comparison with Taxol shows that longstanding expectation common pharmacophore is not met, because each ligand exploits tubulin-binding pocket unique...

10.1126/science.1099190 article EN Science 2004-08-05

Controlled colloid bonding using DNA Colloidal particles can act as analogs of atoms for studying crystallization and packing behavior, but they don't naturally bond together the way do. Short strands are one versatile to link colloidal (see Perspective by Tao). Kim et al. designed a series gold colloids with ligands that reversibly bound or released neighboring via opened closed hairpin loops. Liu devised set pack into origami structures. Inside each structure were cage nanoparticle. These...

10.1126/science.aad2080 article EN Science 2016-02-05

Significance All cellular life forms use a ring-shaped hexameric helicase during DNA replication. CMG (Cdc45, Mcm2–7, GINS) is the eukaryotic replicative helicase. contains Mcm2–7 that harbors motors. known to bind many other proteins, including leading and lagging polymerase primase. Thus, threading of through at replication fork determines orientation associated polymerases fork, an important structural feature with consequences may direct future experimentation. This report uses cryo-EM...

10.1073/pnas.1620500114 article EN Proceedings of the National Academy of Sciences 2017-01-17

The pathology of Huntington's disease is characterized by neuronal degeneration and inclusions containing N-terminal fragments mutant huntingtin (htt). To study htt aggregation, we examined purified in vitro, finding globular protofibrillar intermediates participating the genesis mature fibrils. These were high β-structure. Furthermore, Congo Red, a dye that stains amyloid fibrils, prevented assembly into but not formation protofibrils. Other proteins capable forming ordered aggregates, such...

10.1074/jbc.m205809200 article EN cc-by Journal of Biological Chemistry 2002-10-01

Amyloid fibrils associated with Alzheimer's disease and a wide range of other neurodegenerative diseases have cross β-sheet structure, where main chain hydrogen bonding occurs between β-strands in the direction fibril axis. The surface has pronounced ridges grooves when individual parallel orientation amino acids are in-register one another. Here we show that Aβ amyloid fibrils, Met35 packs against Gly33 C-terminus Aβ40 Gly37 Aβ42. These packing interactions suggest protofilament subunits...

10.1021/bi052485f article EN Biochemistry 2006-04-07
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