Results 101 to 110 of about 17,002 (210)

Eradication [PDF]

Science, 1980
openaire   +2 more sources

The cytosolic fate of ricin A chain in target cells [PDF]

Ricin is a heterodimeric, toxic plant protein. It is able to deliver its catalytic A chain (RTA) into the cytosol of target cells. RTA crosses the endoplasmic reticulum (ER) membrane into the cytosol, masquerading as a substrate of ER-associated ...
Hart, Philip John
core  

SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex

Nature Communications
The SEL1L-HRD1 protein complex represents the most conserved branch of endoplasmic reticulum (ER)-associated degradation (ERAD). Despite recent advances in both mouse models and humans, in vivo evidence for the importance of SEL1L in the ERAD complex ...
Liangguang Leo Lin, Huilun Helen Wang, Brent Pederson, Xiaoqiong Wei, Mauricio Torres, You Lu, Zexin Jason Li, Xiaodan Liu, Hancheng Mao, Hui Wang, Linyao Elina Zhou, Zhen Zhao, Shengyi Sun, Ling Qi   +13 more
doaj   +1 more source

Finding the will and the way of ERAD substrate retrotranslocation

, 2012
ER-associated degradation (ERAD) is a mechanism by which numerous ER-localized proteins are targeted for cytosolic degradation by the ubiquitin-proteasome system.
Sommer, T., Hampton, R.Y.
core   +1 more source

AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and Polyubiquitination of NKCC2

Cells
Inactivating mutations of kidney Na-K-2Cl cotransporter NKCC2 lead to antenatal Bartter syndrome (BS) type 1, a life-threatening salt-losing tubulopathy.
Nadia Frachon, Sylvie Demaretz, Elie Seaayfan, Lydia Chelbi, Dalal Bakhos-Douaihy, Kamel Laghmani   +5 more
doaj   +1 more source

Unconventional roles of nonlipidated LC3 in ERAD tuning and coronavirus infection

Secretory and membrane proteins attain their native structure in the endoplasmic reticulum (ER). Folding-defective polypeptides are selected for degradation by processes collectively defined as ER-associated degradation (ERAD). Enhanced ERAD activity may
Bernasconi, Riccardo, Noack, Julia, Molinari, Maurizio   +2 more
core   +1 more source

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates [PDF]

, 2019
Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting out terminally misfolded polypeptides for ER-associated degradation (ERAD).
Bernasconi, Riccardo, Galli, Carmela, Calanca, Verena, Nakajima, Toshihiro, Molinari, Maurizio   +4 more
core  

Hypomorphic variants of SEL1L-HRD1 ER-associated degradation are associated with neurodevelopmental disorders

The Journal of Clinical Investigation
Recent studies using cell type–specific knockout mouse models have improved our understanding of the pathophysiological relevance of suppressor of lin-12-like–HMG-CoA reductase degradation 1 (SEL1L-HRD1) endoplasmic reticulum–associated (ER-associated ...
Huilun H. Wang, Liangguang L. Lin, Zexin J. Li, Xiaoqiong Wei, Omar Askander, Gerarda Cappuccio, Mais O. Hashem, Laurence Hubert, Arnold Munnich, Mashael Alqahtani, Qi Pang, Margit Burmeister, You Lu, Karine Poirier, Claude Besmond, Shengyi Sun, Nicola Brunetti-Pierri, Fowzan S. Alkuraya, Ling Qi   +18 more
doaj   +1 more source

Sec61p is required for ERAD-L: Genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY

, 2008
Misfolded proteins in the endoplasmic reticulum (ER) are exported to the cytosol for degradation by the proteasome in a process known as ER-associated degradation (ERAD). CPY* is a well characterized ERAD substrate whose degradation is dependent upon the
Willer, Martin, Forte, G. M A, Stirling, Colin J.   +2 more
core   +1 more source

Hypomorphic human SEL1L and HRD1 variants uncouple multilayered ER-associated degradation machinery

The Journal of Clinical Investigation
The suppressor of lin-12-like–HMG-CoA reductase degradation 1 (SEL1L-HRD1) complex of the endoplasmic reticulum–associated degradation (ERAD) machinery is a key cellular proteostasis pathway.
Katharine Umphred-Wilson, Stanley Adoro
doaj   +1 more source