Results 1 to 10 of about 37,506 (169)

Remodeling the proteostasis network to rescue glucocerebrosidase variants by inhibiting ER-associated degradation and enhancing ER folding. [PDF]

PLoS ONE, 2013
Gaucher's disease (GD) is characterized by loss of lysosomal glucocerebrosidase (GC) activity. Mutations in the gene encoding GC destabilize the protein's native folding leading to ER-associated degradation (ERAD) of the misfolded enzyme.
Fan Wang, Laura Segatori
doaj   +6 more sources

The role of ER-associated degradation and ER-phagy in health and disease [PDF]

Signal Transduction and Targeted Therapy
The endoplasmic reticulum (ER) is a major cellular organelle for the synthesis and folding of secretory and transmembrane proteins, whose proper function underpins organellar homeostasis, proper tissue function, and organismal physiology. Protein quality
Young Joo Jeon, Ze’ev A. Ronai
doaj   +2 more sources

A small molecule VDAC ligand inhibits ERAD and induces selective cancer cell death via disruption of calcium homeostasis [PDF]

Nature Communications
Endoplasmic reticulum-associated degradation (ERAD) is a critical protein quality control mechanism that also regulates lipid metabolism and calcium homeostasis.
Wenjing Yan, Daniel C. Talley, Antara Syam, Carina Danchik, Yongwang Zhong, Xianzheng Zhang, Xiaoying Liu, Bolormaa Baljinnyam, Stephen C. Kales, Matthew G. Cyr, Yuhong Fang, Alexey V. Zakharov, Xin Hu, Taylor Niehoff, Tuan Xu, Yanyan Qu, Allison Yang, Valentine V. Courouble, Qin Yao, Anton Simeonov, Ruili Huang, Tatiana K. Rostovtseva, Sergey M. Bezrukov, Christopher A. LeClair, Josephine M. Egan, Hua Wang, Dingyin Tao, Ganesha Rai, Mark J. Henderson, Shengyun Fang   +29 more
doaj   +2 more sources

Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex [PDF]

Nature Communications
The SEL1L-HRD1 complex represents the most conserved branch of endoplasmic reticulum (ER)-associated degradation (ERAD), a critical quality-control pathway that clears misfolded ER proteins.
Liangguang Leo Lin, Emir Maldosevic, Linyao Elina Zhou, Ahmad Jomaa, Ling Qi   +4 more
doaj   +2 more sources

Regulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin [PDF]

Cells, 2014
Quality control of protein folding inside the endoplasmic reticulum (ER) includes chaperone-mediated assistance in folding and the selective targeting of terminally misfolded species to a pathway called ER-associated protein degradation, or simply ERAD ...
Leticia Lemus, Veit Goder
doaj   +4 more sources

Oligosaccharyltransferase Is Involved in Targeting to ER-Associated Degradation [PDF]

Cells
Most membrane and secretory proteins undergo N-glycosylation, catalyzed by oligosaccharyltransferase (OST), a membrane-bound complex in the endoplasmic reticulum (ER).
Marina Shenkman, Navit Ogen-Shtern, Chaitanya Patel, Haddas Saad, Bella Groisman, Metsada Pasmanik-Chor, Sonya M. Schermann, Roman Körner, Gerardo Z. Lederkremer   +8 more
doaj   +2 more sources

Malaria eradication [PDF]

The Lancet, 2020
Kennedy, J, McCoy, D
  +18 more sources

Characterization of endoplasmic reticulum-associated degradation in the human fungal pathogen Candida albicans [PDF]

PeerJ, 2023
Background Candida albicans is the most prevalent human fungal pathogen. In immunocompromised individuals, C. albicans can cause serious systemic disease, and patients infected with drug-resistant isolates have few treatment options.
Ellen M. Doss, Joshua M. Moore, Bryce H. Harman, Emma H. Doud, Eric M. Rubenstein, Douglas A. Bernstein   +5 more
doaj   +2 more sources

Sugar coating autophagy: exploring the links between the inhibition of NGLY1 (N-glycanase 1) and autophagy induction

Autophagy Reports, 2023
The cytosolic enzyme NGLY1 (N-glycanase 1) is a central mediator of glycoprotein catabolism. The enzyme acts to cleave N-linked glycans from modified substrate asparagine residues prior to degradation of misfolded proteins by the proteasome, playing a ...
Holger B. R. Kramer, Sarah Ann Allman
doaj   +1 more source

Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. [PDF]

PLoS ONE, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Jessica R Blount, Aaron A Burr, Amanda Denuc, Gemma Marfany, Sokol V Todi   +4 more
doaj   +1 more source