Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Richard N Sifers"'
Autor:
Jennifer L Mamrosh, Jae Man Lee, Martin Wagner, Peter J Stambrook, Richard J Whitby, Richard N Sifers, San-Pin Wu, Ming-Jer Tsai, Francesco J DeMayo, David D Moore
Publikováno v:
eLife, Vol 4 (2015)
Externí odkaz:
https://doaj.org/article/7cb0c66bbfc04c7ea1650a865d96bc55
Autor:
Jennifer L Mamrosh, Jae Man Lee, Martin Wagner, Peter J Stambrook, Richard J Whitby, Richard N Sifers, San-Pin Wu, Ming-Jer Tsai, Francesco J DeMayo, David D Moore
Publikováno v:
eLife, Vol 3 (2014)
Chronic endoplasmic reticulum (ER) stress results in toxicity that contributes to multiple human disorders. We report a stress resolution pathway initiated by the nuclear receptor LRH-1 that is independent of known unfolded protein response (UPR) pat
Externí odkaz:
https://doaj.org/article/1cc3ba7a8d1b4fd08d92d37e45f4bf72
Autor:
Shujuan Pan, Xiaoyun Cheng, Hongan Chen, Patricia D Castro, Michael M Ittmann, Anne W Hutson, Susan K Zapata, Richard N Sifers
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e72829 (2013)
The MAN1B1 gene product, designated ER alpha-1, 2-mannosidase (ERManI), is an enzyme localized in the Golgi complex of mammalian cells. By functioning as a "gate keeper" to prevent the inappropriate secretion of misfolded glycoproteins, it plays a cr
Externí odkaz:
https://doaj.org/article/a1557f0822c64ef49fa2258e8a8336eb
Autor:
Richard N. Sifers
Publikováno v:
Cell Chemical Biology. 30:1-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b40b569ad43107786393666568615741
https://doi.org/10.1016/j.chembiol.2022.12.008
https://doi.org/10.1016/j.chembiol.2022.12.008
Autor:
Richard N. Sifers, Carolyn J. Adamski, Antrix Jain, Kaifang Pang, J. Lloyd Holder, Sung Yun Jung, Huda Y. Zoghbi, Zhandong Liu, Li Wang, Vitaliy V. Bondar, Evelyn Craigen, John R. Collette, Kihoon Han
Publikováno v:
Molecular psychiatry
Neurons are sensitive to changes in the dosage of many genes, especially those regulating synaptic functions. Haploinsufficiency of SHANK3 causes Phelan-McDermid syndrome and autism, whereas duplication of the same gene leads to SHANK3 duplication sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66f297bd3958c8de78c2b31cd2a33eae
https://doi.org/10.1038/s41380-018-0325-9
https://doi.org/10.1038/s41380-018-0325-9
Publikováno v:
Proc Natl Acad Sci U S A
The failure of polypeptides to achieve conformational maturation following biosynthesis can result in the formation of protein aggregates capable of disrupting essential cellular functions. In the secretory pathway, misfolded asparagine (N)-linked gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4466a4b3788d9ee7c45b94d517b96e56
https://pubmed.ncbi.nlm.nih.gov/32958677
https://pubmed.ncbi.nlm.nih.gov/32958677
Autor:
Marco Sardiello, Rui Chen, Alberto di Ronza, John R. Collette, Aiden Eblimit, Jaiprakash Sharma, Dany Roman, Sung Yun Jung, Richard N. Sifers, Randy Schekman, Lakshya Bajaj, Rituraj Pal, Pengcheng Zheng
Lysosomal enzymes are synthesized in the endoplasmic reticulum (ER) and transferred to the Golgi complex by interaction with the Batten disease protein CLN8. Here we investigated the relationship of this pathway with CLN6, an ER-associated protein of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e27a285efc053b8bea8f283b8e78db39
Autor:
Alberto di Ronza, Pengcheng Zhang, Lakshya Bajaj, Dany Roman, Rituraj Pal, Sung Yun Jung, Jill M. Weimer, Jaiprakash Sharma, Rui Chen, Marco Sardiello, Richard N. Sifers, Randy Schekman, John R. Collette, Aiden Eblimit, Clarissa D. Booth, Kevin T. Chang
Publikováno v:
J Clin Invest
Lysosomal enzymes are synthesized in the endoplasmic reticulum (ER) and transferred to the Golgi complex by interaction with the Batten disease protein CLN8 (ceroid lipofuscinosis, neuronal, 8). Here we investigated the relationship of this pathway w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32a639bfd77e1431c8bb7489b13e2117
https://pubmed.ncbi.nlm.nih.gov/32597833
https://pubmed.ncbi.nlm.nih.gov/32597833
Autor:
Parisa Lotfi, Laura Segatori, Carolyn J. Adamski, Jaiprakash Sharma, Alessandro Simonati, Filippo M. Santorelli, Richard N. Sifers, Maria Chiara Meschini, Marco Sardiello, Lakshya Bajaj, Lauren Popp, Hon Chiu Eastwood Leung, Deepthi Sanagasetti, Kevin T. Chang, John R. Collette, Alberto di Ronza, Michela Palmieri, Abdallah Amawi
Publikováno v:
Nature cell biology
Organelle biogenesis requires proper transport of proteins from their site of synthesis to their target subcellular compartment1–3. Lysosomal enzymes are synthesized in the endoplasmic reticulum (ER) and traffic through the Golgi complex before bei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86c6019468a7a2da83604d9c3a9dfa8e
https://pubmed.ncbi.nlm.nih.gov/30397316
https://pubmed.ncbi.nlm.nih.gov/30397316
Publikováno v:
Molecular Biology of the Cell
Endoplasmic reticulum (ER) α-1, 2-mannosidase and γ-COP contribute to a Golgi-based quality control module that facilitates the retrieval of captured ER-associated protein degradation substrates back to the ER.
Endoplasmic reticulum (ER) α-1,
Endoplasmic reticulum (ER) α-1,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c5af0c809e46dad68f5f28221e0d272
https://doi.org/10.1091/mbc.e12-12-0886
https://doi.org/10.1091/mbc.e12-12-0886