The endoplasmic reticulum proteostasis network profoundly shapes the protein sequence space accessible to HIV envelope

The sequence space accessible to evolving proteins can be enhanced by cellular chaperones that assist biophysically defective clients in navigating complex folding landscapes. It is also possible, at least in theory, for proteostasis mechanisms that promote strict quality control to greatly constrai...

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Veröffentlicht in:	PLoS biology 2022-02, Vol.20 (2), p.e3001569-e3001569
Hauptverfasser:	Yoon, Jimin, Nekongo, Emmanuel E, Patrick, Jessica E, Hui, Tiffani, Phillips, Angela M, Ponomarenko, Anna I, Hendel, Samuel J, Sebastian, Rebecca M, Zhang, Yu Meng, Butty, Vincent L, Ogbunugafor, C Brandon, Lin, Yu-Shan, Shoulders, Matthew D
Format:	Artikel
Sprache:	eng
Schlagworte:	Accessibility Amino acid sequence Antibodies Biology and Life Sciences Cellular stress response Chaperones Dihydrofolate reductase Endoplasmic reticulum Endoplasmic Reticulum - metabolism Endoplasmic Reticulum Stress - genetics Engineering and Technology Genes Genetic aspects Health aspects HIV HIV (Viruses) HIV Infections - metabolism Human immunodeficiency virus Humans Immunological tolerance Influenza Kinases Medicine and Health Sciences Molecular Chaperones - metabolism Mutation Pathways Patient outcomes Physiological aspects Protein folding Proteins Proteostasis Quality control Research and Analysis Methods Transcription factors Unfolded Protein Response Viruses
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