Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Takuo Osawa"'
Publikováno v:
JACS Au, Vol 4, Iss 4, Pp 1323-1333 (2024)
Externí odkaz:
https://doaj.org/article/e8b9c6f97c014e32a6daf0c6fb0dfbc4
Autor:
Takuo Osawa, Nobuo N. Noda
Publikováno v:
Protein Science : A Publication of the Protein Society
The degradation of cytoplasmic components via autophagy is crucial for intracellular homeostasis. In the process of autophagy, a newly synthesized isolation membrane (IM) is developed to sequester degradation targets and eventually the IM seals, form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59ca592f5c97521e48f83c6d28043f3f
https://doi.org/10.1002/pro.3623
https://doi.org/10.1002/pro.3623
Publikováno v:
Chemistry and Physics of Lipids. 218:1-9
Autophagy is an intracellular degradation system conserved among eukaryotes that mediates the degradation of various biomolecules and organelles. During autophagy, a double membrane-bound organelle termed an autophagosome is synthesized de novo and d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::258aac1bbb90fecf5888d3ec4a0664d3
https://doi.org/10.1016/j.chemphyslip.2018.11.001
https://doi.org/10.1016/j.chemphyslip.2018.11.001
Publikováno v:
Cold Spring Harbor Perspectives in Biology. :a041254
Autophagy is an intracellular degradation system involving de novo generation of autophagosomes, which function as a transporting vesicle of cytoplasmic components to lysosomes for degradation. Isolation membranes (IMs) or phagophores, the precursor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6640b2af2d76ce00bde446b0a1abd891
https://doi.org/10.1101/cshperspect.a041254
https://doi.org/10.1101/cshperspect.a041254
Publikováno v:
Genes to cells : devoted to molecularcellular mechanismsREFERENCES. 25(1)
Atg2 is one of the essential factors for autophagy. Recent advance of structural and biochemical study on yeast Atg2 proposed that Atg2 tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum and mediates direct lipid transfer (L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8907c09687a2c6f4e1374335f0b1d09e
https://pubmed.ncbi.nlm.nih.gov/31721365
https://pubmed.ncbi.nlm.nih.gov/31721365
Publikováno v:
FEBS Letters. 589:2327-2333
Transglycosylation (TG) activity of a family GH18 chitinase from the cycad, Cycas revoluta, (CrChiA) was modulated by removing or introducing a tryptophan side chain. The removal from subsite +3 through mutation of Trp168 to alanine suppressed TG act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5204b51eeb764310c05a2d7954c9dec4
https://doi.org/10.1016/j.febslet.2015.07.018
https://doi.org/10.1016/j.febslet.2015.07.018
Publikováno v:
Molecular Cell. 58:418-430
In prokaryotes, Clustered regularly interspaced short palindromic repeat (CRISPR)-derived RNAs (crRNAs), together with CRISPR-associated (Cas) proteins, capture and degrade invading genetic materials. In the type III-B CRISPR-Cas system, six Cas prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8c9be6376ea1203a4c198b947e72c28
https://doi.org/10.1016/j.molcel.2015.03.018
https://doi.org/10.1016/j.molcel.2015.03.018
Autor:
Takuo Osawa, Tomoyuki Numata
Publikováno v:
Nihon Kessho Gakkaishi. 57:317-323
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5d5a86295cba5c49a7e523a43c7f753
https://doi.org/10.5940/jcrsj.57.317
https://doi.org/10.5940/jcrsj.57.317
Publikováno v:
Journal of Molecular Biology. 425:3811-3823
Clustered, regularly interspaced, short palindromic repeat (CRISPR) loci found in prokaryotes are transcribed to produce CRISPR RNAs (crRNAs) that, together with CRISPR-associated (Cas) proteins, target and degrade invading genetic materials. Cmr pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06a2e5bd7f3eae91277b649efd04c9ec
https://doi.org/10.1016/j.jmb.2013.03.042
https://doi.org/10.1016/j.jmb.2013.03.042
Autor:
Yoko Okazaki, Takuo Osawa, Hideko Inanaga, Tomoyuki Numata, Tamo Fukamizo, Kaori Kondo, Tatsuya Fukuda, Takayuki Ohnuma, Shoko Shinya
Publikováno v:
The FEBS Journal. 279:3639-3651
The substrate-binding mode of a 26-kDa GH19 chitinase from rye, Secale cereale, seeds (RSC-c) was investigated by crystallography, site-directed mutagenesis and NMR spectroscopy. The crystal structure of RSC-c in a complex with an N-acetylglucosamine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d0403e26127f2766094caea08fdc2fb
https://doi.org/10.1111/j.1742-4658.2012.08723.x
https://doi.org/10.1111/j.1742-4658.2012.08723.x