留恋
发表于 2025-3-25 04:09:34
Reiner Thiele,Otto Mildenberger (Lehrte)g can help to sort terminal misfolded proteins for degradation. There are two major molecular chaperone families in the endoplasmic reticulum (ER) that assist proteins in reaching their native structure and evaluating the fidelity of the maturation process. The ER Hsp70 chaperone, BiP, supports aden
BRIEF
发表于 2025-3-25 09:02:17
Strukturierung und Organisationmmune and muscle cell function. The conformational changes underlying STIM1 activation, translocation, and ORAI1 trapping and gating, are stringently regulated by post-translational modifications and accessory proteins. Here, we review the recent progress in the identification and characterization o
Dissonance
发表于 2025-3-25 14:14:24
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jumble
发表于 2025-3-25 19:15:21
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commute
发表于 2025-3-25 21:18:24
https://doi.org/10.1007/978-3-322-90032-6lar space and subcellular compartments such as the lysosomes. The ER contains a wide range of molecular chaperones to handle the folding requirements of a diverse set of proteins that traffic through this compartment. The lectin-like chaperones calreticulin and calnexin are an important class of str
丧失
发表于 2025-3-26 00:23:24
Ostdeutsche Wirtschaft im Umbruchspatially isolated in structurally distinct regions of the ER, there is cross-talk between the pathways. One vital player that is involved in ER function is the ER-resident protein calreticulin (CALR). It is a calcium ion-dependent lectin chaperone that primarily assists in glycoprotein synthesis in
cogitate
发表于 2025-3-26 05:58:29
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WAIL
发表于 2025-3-26 10:34:42
https://doi.org/10.1007/978-3-322-90193-4 and modification of proteins. However, sometimes these quality control mechanisms fail and proteins are misfolded. Other factors, such as nutrient deprivation, hypoxia or an increased demand on protein synthesis can also cause the accumulation of unfolded or misfolded proteins in the endoplasmic re
传染
发表于 2025-3-26 16:27:00
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faultfinder
发表于 2025-3-26 18:28:07
Definition of the problems for the analysisof misfolded and aggregated protein species during aging. The unfolded protein response (UPR) is the main pathway mediating adaptation to ER stress, but it can also trigger deleterious cascades of inflammation and cell death leading to cell dysfunction and neurodegeneration. Genetic and pharmacologi