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Author Details

Tadashi Makio
University of Alberta
1998
17
12
Nevan J Krogan (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
34001511Nodosome Inhibition as a Novel Broad-Spectrum Antiviral Strategy against Arboviruses, Enteroviruses, and SARS-CoV-2.Antimicrob Agents Chemother2021
33547084Nsp1 protein of SARS-CoV-2 disrupts the mRNA export machinery to inhibit host gene expression.Sci Adv2021
33097660SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling.Proc Natl Acad Sci U S A2020
32051285Passive diffusion through nuclear pore complexes regulates levels of the yeast SAGA and SLIK coactivator complexes.J Cell Sci2020
24165935Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex.J Cell Biol2013
21173275Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.Proc Natl Acad Sci U S A2011
19414608The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly.J Cell Biol2009
18754794Identification and characterization of a Jem1p ortholog of Candida albicans: dissection of Jem1p functions in karyogamy and protein quality control in Saccharomyces cerevisiae.Genes Cells2008
12493774Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion.J Biol Chem2003
12614617Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy.J Mol Biol2003
12742022The allosteric transition of GroEL induced by metal fluoride-ADP complexes.J Mol Biol2003
23345759Chaperonin-affected folding of globular proteins.J Biol Phys2002
11563916Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin.J Mol Biol2001
11342042Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.Biochim Biophys Acta2001
10673379Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.Biochem Biophys Res Commun2000
10512721Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.J Mol Biol1999
9533891Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL.J Mol Biol1998
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Collaborators

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Vanderbilt University School of Medicine
Co-authored papers 1
Icahn School of Medicine at Mount Sinai
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Sanford Burnham Prebys Medical Discovery Institute
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Quantitative Biosciences Institute (QBI) Coronavirus Research Group (QCRG)
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Icahn School of Medicine at Mount Sinai
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