eLife, 2017 Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation.
Marta Carroni +10 more
doaj +1 more source
Transcriptional Response to Acute Thermal Exposure in Juvenile Chinook Salmon Determined by RNAseq. [PDF]
, 2015 Thermal exposure is a serious and growing challenge facing fish species worldwide. Chinook salmon (Oncorhynchus tshawytscha) living in the southern portion of their native range are particularly likely to encounter warmer water due to a confluence of ...
Baerwald, Melinda R +6 more
core
Frontiers in Neuroscience, 2018 Background: Most neurodegenerative diseases are sporadic and develop with age. Degenerative neural tissues often contain intra- and extracellular protein aggregates, suggesting that the proteostasis network that combats protein misfolding could be ...
Hisayo Jin, Mari Komita, Tomohiko Aoe
doaj +1 more source
Altered Function of the DnaJ Family Cochaperone DNJ-17 Modulates Locomotor Circuit Activity in a Caenorhabditis elegans Seizure Model. [PDF]
, 2016 The highly conserved cochaperone DnaJ/Hsp40 family proteins are known to interact with molecular chaperone Hsp70, and can regulate many cellular processes including protein folding, translocation, and degradation.
Jin, Yishi, Takayanagi-Kiya, Seika
core +2 more sources
Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads [PDF]
, 2017 Allosteric compounds that stimulate Hsp90 adenosine triphosphatase (ATPase) activity were rationally designed, showing anticancer potencies in the low micromolar to nanomolar range.
Agard, Da +10 more
core +1 more source
The Endoplasmic Reticulum Glucosyltransferase Recognizes Nearly Native Glycoprotein Folding Intermediates [PDF]
, 2004 The UDP-Glc:glycoprotein glucosyltransferase (GT), a key player in the endoplasmic reticulum (ER) quality control of glycoprotein folding, only glucosylates glycoproteins displaying non-native conformations.
Caramelo, Julio Javier +3 more
core +1 more source
Chaperone driven polymer translocation through Nanopore: spatial distribution and binding energy
, 2016 Chaperones are binding proteins which work as a driving force to bias the biopolymer translocation by binding to it near the pore and preventing its backsliding. Chaperones may have different spatial distribution. Recently we show the importance of their
Abdolvahab, Rouhollah Haji
core +1 more source
Environmental stress responses in Lactococcus lactis [PDF]
, 1999 Bacteria can encounter a variety of physical conditions during their life. Bacterial cells are able to survive these (often adverse) conditions by the induction of specific or general protection mechanisms. The lactic acid bacterium Lactococcus lactis is
Kok, Jan, +2 more
core +3 more sources
Regulation of podocyte survival and endoplasmic reticulum stress by fatty acids and its modification by Stearoyl-CoA desaturases and cyclic AMP [PDF]
, 2011 Podocyte apoptosis is a hallmark in the development and progression of diabetic nephropathy (DN). Several factors of the diabetic milieu are known to induce podocyte apoptosis. Currently, the role of free fatty acids (FFAs) for podocytopathy and podocyte
Sieber, Jonas
core +1 more source
Ricin trafficking in plant and mammalian cells [PDF]
, 2011 Ricin is a heterodimeric plant protein that is potently toxic to mammalian and many other eukaryotic cells. It is synthesized and stored in the endosperm cells of maturing Ricinus communis seeds (castor beans).
Lord, Mike, Spooner, Robert A.
core +2 more sources