Osamu Nureki

ORCID: 0000-0003-1813-7008
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About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • Enzyme Structure and Function
  • CRISPR and Genetic Engineering
  • Photoreceptor and optogenetics research
  • Receptor Mechanisms and Signaling
  • Bacterial Genetics and Biotechnology
  • Mass Spectrometry Techniques and Applications
  • RNA Research and Splicing
  • Amino Acid Enzymes and Metabolism
  • Advanced biosensing and bioanalysis techniques
  • Genomics and Phylogenetic Studies
  • Nitric Oxide and Endothelin Effects
  • Neuroscience and Neuropharmacology Research
  • Sphingolipid Metabolism and Signaling
  • Lipid Membrane Structure and Behavior
  • Ion channel regulation and function
  • Biochemical and Molecular Research
  • Photosynthetic Processes and Mechanisms
  • DNA and Nucleic Acid Chemistry
  • Magnesium in Health and Disease
  • Protein Structure and Dynamics
  • Plant Micronutrient Interactions and Effects
  • RNA regulation and disease
  • Neural dynamics and brain function

The University of Tokyo
2016-2025

Juntendo University
2024

Tokyo University of Science
2010-2023

Max Planck Institute of Biophysics
2021

ORCID
2021

RIKEN
2001-2017

Japan Agency for Medical Research and Development
2016

RIKEN Advanced Science Institute
2013-2015

Tokyo Institute of Technology
2004-2014

RIKEN Center for Sustainable Resource Science
2014

The RNA-guided endonuclease Cas9 cleaves its target DNA and is a powerful genome-editing tool. However, the widely used Streptococcus pyogenes enzyme (SpCas9) requires an NGG protospacer adjacent motif (PAM) for recognition, thereby restricting targetable genomic loci. Here, we report rationally engineered SpCas9 variant (SpCas9-NG) that can recognize relaxed NG PAMs. crystal structure revealed loss of base-specific interaction with third nucleobase compensated by newly introduced...

10.1126/science.aas9129 article EN Science 2018-08-30

Snapshots of bacteriorhodopsin Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out cell against transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallography at an x-ray free electron laser provide 13 structural snapshots conformational changes occur in nanoseconds milliseconds after photoactivation. These begin active site, propagate toward extracellular side protein, and mediate internal protonation...

10.1126/science.aah3497 article EN Science 2016-12-22

Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments multicellular organisms and regulate the permeation of ions through intercellular space. Claudins major constituents tight form strands mediate function as paracellular barriers. We report structure mammalian claudin-15 at a resolution 2.4 angstroms. The reveals characteristic β-sheet fold comprising two extracellular segments, which is anchored to transmembrane four-helix bundle by...

10.1126/science.1248571 article EN Science 2014-04-17

A cap-specific m 6 writer N ,2′- O -dimethyladenosine (m Am) is present at the transcription start nucleotide of capped mRNAs in vertebrates. Akichika et al. quantified abundance this modification transcriptome and identified protein, adenosine methyltransferase (CAPAM), needed for modification. CAPAM contains a unique structure that recognizes -methyladenosine A) as substrate. The protein interacts with RNA polymerase II, suggesting occurs cotranscriptionally. Am promotes translation...

10.1126/science.aav0080 article EN Science 2018-11-23
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