Zobrazeno 1 - 10
of 327
pro vyhledávání: ''
Autor:
Marius K. Lemberg, Kvido Strisovsky
Publikováno v:
Molecular Cell. 81:2507-2519
Protein homeostasis mechanisms are fundamentally important to match cellular needs and to counteract stress conditions. A fundamental challenge is to understand how defective proteins are recognized and extracted from cellular organelles to be degrad
Autor:
Michael L. Skowyra, Tom A. Rapoport
Publikováno v:
Molecular cell. 82(17)
Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases. Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which interacts with a docking complex in the peroxisomal membrane and then returns to t
Autor:
Sven M. Lange, Syed Arif Abdul Rehman, Dmitri I. Svergun, Lee A. Armstrong, Yogesh Kulathu, Yosua Adi Kristariyanto, Axel Knebel, Tobias W. Gräwert
Publikováno v:
'Molecular Cell ', vol: 81, pages: 4176-4190 (2021)
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Summary Of the eight distinct polyubiquitin (polyUb) linkages that can be assembled, the roles of K48-linked polyUb (K48-polyUb) are the most established, with K48-polyUb modified proteins being targeted for degradation. MINDY1 and MINDY2 are members
Publikováno v:
Molecular cell. 82(13)
The NF-κB essential modulator (NEMO) is a regulatory subunit of the IκB kinase (IKK) complex that phosphorylates the NF-κB inhibitors IκBs. NEMO mediates IKK activation by binding to polyubiquitin chains (polyUb). Here, we show that Lys63(K63)-li
Publikováno v:
Molecular cell. 82(1)
Deubiquitinases (DUBs) are specialized proteases that remove ubiquitin from substrates or cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in eukaryotic biology. Dysregulation of DUBs is implicated in sever
Autor:
Linhan Wang, Jiqiang Li, Qingchen Wang, Man-Xi Ge, Jia Ji, Di Liu, Zhiyuan Wang, Yang Cao, Yaoyang Zhang, Zai-Rong Zhang
Publikováno v:
Molecular cell. 82(18)
Membrane protein clients of endoplasmic reticulum (ER)-associated degradation must be retrotranslocated from the ER membrane by the AAA-ATPase p97 for proteasomal degradation. Before direct engagement with p97, client transmembrane domains (TMDs) tha
Autor:
Vishnu Balaji, Leonie Müller, Robin Lorenz, Éva Kevei, William H. Zhang, Ulises Santiago, Jan Gebauer, Ernesto Llamas, David Vilchez, Carlos J. Camacho, Wojciech Pokrzywa, Thorsten Hoppe
Publikováno v:
Molecular cell. 82(17)
The high substrate selectivity of the ubiquitin/proteasome system is mediated by a large group of E3 ubiquitin ligases. The ubiquitin ligase CHIP regulates the degradation of chaperone-controlled and chaperone-independent proteins. To understand how
Autor:
Jia Z. Shen, Zhixin Qiu, Qiulian Wu, Guoxin Zhang, Rebecca Harris, Dahui Sun, Juha Rantala, William D. Barshop, Linjie Zhao, Deguan Lv, Kwang-Ai Won, James Wohlschlegel, Olle Sangfelt, Heike Laman, Jeremy N. Rich, Charles Spruck
Publikováno v:
Mol Cell
A mesenchymal tumor phenotype associates with immunotherapy resistance, although the mechanism is unclear. Here, we identified FBXO7 as a maintenance regulator of mesenchymal and immune evasion phenotypes of cancer cells. FBXO7 bound and stabilized S
Publikováno v:
Molecular cell. 81(11)
Agents that induce DNA damage can cure some cancers. However, the side effects of chemotherapy are severe because of the indiscriminate action of DNA-damaging agents on both healthy and cancerous cells. DNA repair pathway inhibition provides a less t
Autor:
Ivan Ahel, Yan Yan, Baomin Feng, Jun Hyeok Kim, Ping He, Johannes Gregor Matthias Rack, Jyan-Chyun Jang, Ying Wang, Liang Kong, Libo Shan, Chao Zhang, Lahong Xu
Publikováno v:
Molecular cell. 81(22)
Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD+ onto acceptor proteins. Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydr