Zobrazeno 1 - 10
of 129
pro vyhledávání: '"Golgi organization"'
Akademický článek
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Autor:
Hieda, M., Matsumoto, T., Isobe, M., Kurono, S., Yuka, K., Kametaka, S., Wang, J. Y., Chi, Y. H., Kameda, K., Kimura, Hiroshi, Matsuura, N., Matsuura, S.
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Scientific Reports
Scientific Reports
The morphology of the Golgi complex is influenced by the cellular context, which strictly correlates with nuclear functions; however, the mechanism underlying this association remains elusive. The inner nuclear membrane SUN proteins, SUN1 and SUN2, h
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 4 (2016)
Unexpectedly, members of the Rab VI subfamily exhibit considerable variation in their effects on Golgi organization and trafficking. By fluorescence microscopy, neither depletion nor overexpression of the GDP-locked form of Rab6a/a’, the first tran
Externí odkaz:
https://doaj.org/article/7c063619ce2443f7b63a98eeffd60ac3
Publikováno v:
Trends in Molecular Medicine. 26:380-393
Centrosome cohesion, the joining of the two centrosomes of a cell, is increasingly appreciated as a major regulator of cell functions such as Golgi organization and cilia positioning. One major element of centrosome cohesion is the centrosome linker
Autor:
Philipp W. N. Schmid, Matthias Mörgelin, Jan M. Gebauer, Sinan Oecal, Ulrich Baumann, Johannes Buchner, Elena Theres Abraham
Publikováno v:
The Journal of Biological Chemistry
'Journal of Biological Chemistry ', vol: 297, pages: 101169-1-101169-13 (2021)
'Journal of Biological Chemistry ', vol: 297, pages: 101169-1-101169-13 (2021)
Collagens play important roles in development and homeostasis in most higher organisms. In order to function, collagens require the specific chaperone HSP47 for proper folding and secretion. HSP47 is known to bind to the collagen triple-helix but the
Autor:
Yishi Shen, Shucun Qin, Bingxiang Wang, Yongfang Zhao, Lei Zhai, Boyan Liu, Xiaole Chang, Adekunle Alabi, Shijun Deng, Maggie Wang, Hong-mei Gu, Da-Wei Zhang, Xiao-dan Xia, Guiqing Wang, Sijie Xing
Publikováno v:
Journal of Lipid Research
Journal of Lipid Research, Vol 62, Iss, Pp 100091-(2021)
Journal of Lipid Research, Vol 62, Iss, Pp 100091-(2021)
Plasma LDL is produced from catabolism of VLDL and cleared from circulation mainly via the hepatic LDL receptor (LDLR). Proprotein convertase subtilisin/kexin type 9 (PCSK9) promotes LDLR degradation, increasing plasma LDL-C levels. Circulating PCSK9
Publikováno v:
Journal of Molecular Cell Biology
Hsp90 is an abundant and special molecular chaperone considered to be the regulator of many transcription factors and signaling kinases. Its high abundance is indicative of its involvement in some more fundamental processes. In this study, we provide
Autor:
Kota Saito, Miharu Maeda
Publikováno v:
The Journal of Biochemistry. 166:115-119
Proteins synthesized within the endoplasmic reticulum (ER) are exported from ER exit sites via coat protein complex II (COPII)-coated vesicles. Although the mechanisms of COPII-vesicle formation at the ER exit sites are highly conserved among species
Autor:
Christopher R. Neal, Judith Mantell, Janine McCaughey, Alex Paterson, David J. Stephens, Kate J. Heesom, Nicola L. Stevenson
Complex machinery is required to drive secretory cargo export from the endoplasmic reticulum, an essential process in eukaryotic cells. In vertebrates, the Mia3 gene encodes two major forms of Transport ANd Golgi Organization Protein 1 (TANGO1S and T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::37794b4b51d48eb287582852d8e3ef86
https://doi.org/10.1101/2021.02.24.432632
https://doi.org/10.1101/2021.02.24.432632
Autor:
Matsui, Yuto
0048
甲第22832号
医博第4671号
新制||医||1047(附属図書館)
学位規則第4条第1項該当
Doctor of Medical Science
Kyoto University
DFAM
甲第22832号
医博第4671号
新制||医||1047(附属図書館)
学位規則第4条第1項該当
Doctor of Medical Science
Kyoto University
DFAM
Externí odkaz:
http://hdl.handle.net/2433/259728