scholarly journals Network measures for protein folding state discrimination

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Giulia Menichetti ◽  
Piero Fariselli ◽  
Daniel Remondini
Keyword(s):  
Protein Folding ◽  
Network Measures ◽  
State Discrimination ◽  
Folding State

scholarly journals Impact of cellular health conditions on the protein folding state in mammalian cells

2017 ◽  
Vol 53 (81) ◽  
pp. 11245-11248 ◽  
Author(s):  
Kohsuke Inomata ◽  
Hajime Kamoshida ◽  
Masaomi Ikari ◽  
Yutaka Ito ◽  
Takanori Kigawa
Keyword(s):  
Protein Folding ◽  
Mammalian Cells ◽  
Health Conditions ◽  
Folding State

Cellular health conditions severely affect the protein folding state in mammalian cells.

scholarly journals Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

2018 ◽  
Vol 221 (3) ◽  
pp. 1230-1246 ◽  
Author(s):  
Andreas J. Meyer ◽  
Jan Riemer ◽  
Nicolas Rouhier
Keyword(s):  
Protein Folding ◽  
State Of The Art ◽  
Oxidative Protein Folding ◽  
Folding State

scholarly journals Modularity of the Hrd1 ERAD complex underlies its diverse client range

2010 ◽  
Vol 188 (5) ◽  
pp. 707-716 ◽  
Author(s):  
Kazue Kanehara ◽  
Wei Xie ◽  
Davis T.W. Ng
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Membrane Proteins ◽  
Secretory Protein ◽  
Modular Organization ◽  
Control Mechanisms ◽  
Core Complex ◽  
Er Quality Control ◽  
Folding State

Secretory protein folding is monitored by endoplasmic reticulum (ER) quality control mechanisms. Misfolded proteins are retained and targeted to ER-associated degradation (ERAD) pathways. At their core are E3 ubiquitin ligases, which organize factors that recognize, ubiquitinate, and translocate substrates. Of these, we report that the Hrd1 complex manages three distinct substrate classes. A core complex is required for all classes and is sufficient for some membrane proteins. The accessory factors Usa1p and Der1p adapt the complex to process luminal substrates. Their integration is sufficient to process molecules bearing glycan-independent degradation signals. The presence of Yos9p extends the substrate range by mediating the recognition of glycan-based degradation signals. This modular organization enables the Hrd1 complex to recognize topologically diverse substrates. The Hrd1 system does not directly evaluate the folding state of polypeptides. Instead, it does so indirectly, by recognizing specific embedded signals displayed upon misfolding.

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

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