Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Nobuko Hosokawa"'
Publikováno v:
Cell Structure and Function, Vol 49, Iss 2, Pp 67-81 (2024)
Collagen is the most abundant protein in the extracellular matrix of animals, and 28 types of collagen have been reported in humans. We previously analyzed the endoplasmic reticulum (ER)-to-Golgi transport of fibril-forming type III collagen (Hirata
Externí odkaz:
https://doaj.org/article/833efb147b1945998b4ade18ff398130
Publikováno v:
The FEBS Journal. 288(15):4637-4654
Misfolded proteins in the endoplasmic reticulum (ER) are degraded by ER-associated degradation (ERAD). In mammalian cells, the HRD1-SEL1L membrane ubiquitin ligase complex plays a central role in this process. However, SEL1L is inherently unstable, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0f962cdf41aa5d60c250fa33d52a6dc
http://hdl.handle.net/2433/267989
http://hdl.handle.net/2433/267989
Publikováno v:
Cell Structure and Function. 45:107-119
Collagen is the most abundant protein in animal tissues and is critical for their proper organization. Nascent procollagens in the endoplasmic reticulum (ER) are considered too large to be loaded into coat protein complex II (COPII) vesicles, which h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c914cd58fdfa431575b52d8e3fd307aa
https://doi.org/10.1247/csf.20025
https://doi.org/10.1247/csf.20025
Publikováno v:
Molecular biology of the cell. 33(3)
Collagen is the major protein component of the extracellular matrix. Synthesis of procollagens starts in the endoplasmic reticulum (ER), and three α chains form a rigid triple helix 300-400 nm in length. It remains unclear how such a large cargo is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1756993fcb09eb223176159c847e02f7
https://pubmed.ncbi.nlm.nih.gov/35044867
https://pubmed.ncbi.nlm.nih.gov/35044867
Publikováno v:
J Biol Chem
Molecular chaperones facilitate protein folding by associating with nascent polypeptides, thereby preventing protein misfolding and aggregation. Endoplasmic reticulum (ER) chaperone BiP, the sole HSP70 chaperone in the ER, is regulated by HSP40 chape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a8b050ee1fc062165b838799a4cb62
https://doi.org/10.1074/jbc.ra119.009603
https://doi.org/10.1074/jbc.ra119.009603
Autor:
Nobuko, Hosokawa
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2132
Quality control of newly synthesized glycoproteins is tightly regulated by sugar processing of N-glycans and by recognition of specific glycan structures by lectins in the endoplasmic reticulum (ER). Mannose trimming and its recognition determine the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::234ae5751570d3a2eb0d279f55b09c99
https://pubmed.ncbi.nlm.nih.gov/32306323
https://pubmed.ncbi.nlm.nih.gov/32306323
Autor:
Nobuko Hosokawa
Publikováno v:
Methods in Molecular Biology ISBN: 9781071604298
Quality control of newly synthesized glycoproteins is tightly regulated by sugar processing of N-glycans and by recognition of specific glycan structures by lectins in the endoplasmic reticulum (ER). Mannose trimming and its recognition determine the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09a4ffcd46c1d71d482720ed17ee678a
https://doi.org/10.1007/978-1-0716-0430-4_15
https://doi.org/10.1007/978-1-0716-0430-4_15
Publikováno v:
Journal of Biological Chemistry. 293:10663-10674
Protein folding in the cell is regulated by several quality-control mechanisms. Correct folding of glycoproteins in the endoplasmic reticulum (ER) is tightly monitored by the recognition of glycan signals by lectins in the ER-associated degradation (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ce81024ad9bd1b92a120c85e0b498ab
https://doi.org/10.1074/jbc.ra118.003129
https://doi.org/10.1074/jbc.ra118.003129
Publikováno v:
Genes to Cells. 22:684-698
The folding of newly synthesized proteins in the endoplasmic reticulum (ER) is assisted by ER-resident chaperone proteins. BiP (immunoglobulin heavy-chain-binding protein), a member of the HSP70 family, plays a central role in protein quality control
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16c10c154b9e852ba6cb2ca8ed1e64e0
https://doi.org/10.1111/gtc.12506
https://doi.org/10.1111/gtc.12506
Autor:
Ikuo Wada, Nobuko Hosokawa
Publikováno v:
FEBS Journal. 283:157-172
Misfolded proteins in the endoplasmic reticulum (ER) are transported to the cytoplasm for degradation by the ubiquitin-proteasome system, a process otherwise known as ER-associated degradation (ERAD). Mammalian HRD1, an integral membrane ubiquitin li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36240704b6888ec22d2655a8714bd5df
https://doi.org/10.1111/febs.13564
https://doi.org/10.1111/febs.13564