Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Jack Rohrer"'
Autor:
Takuma Kozono, Hiroyuki Sato, Wataru Okumura, Chifuyu Jogano, Miwa Tamura-Nakano, Yuki I. Kawamura, Jack Rohrer, Takashi Tonozuka, Atsushi Nishikawa
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-17 (2021)
Abstract Jaw1/LRMP is a type II integral membrane protein that is localized at the endoplasmic reticulum (ER) and outer nuclear membrane. We previously reported that a function of Jaw1 is to maintain the nuclear shape as a KASH protein via its carbox
Externí odkaz:
https://doaj.org/article/9b0bbb77d4e84230962f6a8b257e98b9
Autor:
Wataru Okumura, Kazuko Tadahira, Takuma Kozono, Miwa Tamura-Nakano, Hiroyuki Sato, Hitomi Matsui, Taeko Dohi, Jack Rohrer, Takashi Tonozuka, Atsushi Nishikawa
Publikováno v:
The Journal of Biochemistry. 173:383-392
Jaw1/LRMP is a membrane protein that is localized to the endoplasmic reticulum and outer nuclear membrane. Previously, we revealed that Jaw1 functions to maintain nuclear shape by interacting with microtubules as a Klarsicht/ANC-1/Syne/homology (KASH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2fee8e8fa4d87b7ec99d9c629ef04967
https://doi.org/10.1093/jb/mvad004
https://doi.org/10.1093/jb/mvad004
Autor:
Besmira Sabani, Michael Brand, Ina Albert, Joelle Inderbitzin, Fritz Eichenseher, Mathias Schmelcher, Jack Rohrer, Rainer Riedl, Steffi Lehmann
Publikováno v:
Nanomedicine: Nanotechnology, Biology and Medicine. 47:102607
Extracellular vesicles (EVs), nanovesicles released by cells to effectively exchange biological information, are gaining interest as drug delivery system. Yet, analogously to liposomes, they show short blood circulation times and accumulation in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88ac526fafebb2ba74fccbdc3a12007f
https://doi.org/10.1016/j.nano.2022.102607
https://doi.org/10.1016/j.nano.2022.102607
Autor:
Atsushi Nishikawa, Wataru Okumura, Chifuyu Jogano, Jack Rohrer, Hiroyuki Sato, Yuki I. Kawamura, Takuma Kozono, Miwa Tamura-Nakano, Takashi Tonozuka
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-17 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-17 (2021)
Jaw1/LRMP is a type II integral membrane protein that is localized at the endoplasmic reticulum (ER) and outer nuclear membrane. We previously reported that a function of Jaw1 is to maintain the nuclear shape as a KASH protein via its carboxyl termin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b908002329cf553e55034b27174936ce
A treasure trove of intracellular cancer drug targets remains hidden behind cell membranes. However, engineered pathogen-derived toxins such as Shiga toxins can deliver small or macromolecular drugs to specific intracellular organelles. After binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47774e4431b458762dae428e992a52ec
https://hdl.handle.net/11475/11523
https://hdl.handle.net/11475/11523
Autor:
Romain Péanne, Jack Rohrer, Sandrine Duvet, Gert Matthijs, François Foulquier, Anne-Marie Mir, Dominique Legrand
Erworben im Rahmen der Schweizer Nationallizenzen (http://www.nationallizenzen.ch)
Initially described by Jaeken et al. in 1980, congenital disorders of glycosylation (CDG) is a rapidly expanding group of human multisystemic disorders. To date,
Initially described by Jaeken et al. in 1980, congenital disorders of glycosylation (CDG) is a rapidly expanding group of human multisystemic disorders. To date,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbe938d5b560c73094c397d85fb8296d
http://doc.rero.ch/record/293081/files/cwq176.pdf
http://doc.rero.ch/record/293081/files/cwq176.pdf
Autor:
Hans J. Geuze, Kai Huang, Beat E. Schaub, Prashant Nair, Jack Rohrer, Xiang Chen, Janice Griffith, Robert F. Murphy
Publikováno v:
Journal of Cell Science. 118:2949-2956
The human mannose 6-phosphate uncovering enzyme participates in the uncovering of the mannose 6-phosphate recognition tag on lysosomal enzymes, a process that facilitates recognition of those enzymes by mannose 6-phosphate receptors to ensure deliver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1131ca635d29468024989c2f07cba7d3
https://doi.org/10.1242/jcs.02434
https://doi.org/10.1242/jcs.02434
Publikováno v:
Journal of Biological Chemistry. 279:41012-41017
The alternatively spliced messenger RNA of the human cysteine peptidase cathepsin B missing exons 2 and 3 encodes a truncated form of the enzyme lacking the signal peptide and part of the inhibitory propeptide. This deletion results in a new N-termin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::087ad4ba8308fbadcbef50c209a48d9c
https://doi.org/10.1074/jbc.m405333200
https://doi.org/10.1074/jbc.m405333200
Publikováno v:
Journal of Biological Chemistry. 279:23542-23549
Lysosomal biogenesis depends on proper transport of lysosomal enzymes by the cation-dependent mannose 6-phosphate receptor (CD-MPR) from the trans-Golgi network (TGN) to endosomes. Trafficking of the CDMPR is mediated by sorting signals in its cytopl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf28d85a4641eff96a46c300e6bb2647
https://doi.org/10.1074/jbc.m313525200
https://doi.org/10.1074/jbc.m313525200
Publikováno v:
Journal of Biological Chemistry. 278:24753-24758
Intracellular cycling of the cation-dependent mannose 6-phosphate receptor (CD-MPR) between different compartments is directed by signals localized in its cytoplasmic tail. A di-aromatic motif (Phe18-Trp19 with Trp19 as the key residue) in its cytopl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cea371648d7375b3a58b0148928068f
https://doi.org/10.1074/jbc.m300174200
https://doi.org/10.1074/jbc.m300174200