P
Peter Walter
Researcher at RWTH Aachen University
Publications - 894
Citations - 91493
Peter Walter is an academic researcher from RWTH Aachen University. The author has contributed to research in topics: Endoplasmic reticulum & Signal recognition particle. The author has an hindex of 126, co-authored 841 publications receiving 71580 citations. Previous affiliations of Peter Walter include National Institutes of Health & University of Cologne.
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Journal ArticleDOI
Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus.
Caroline E. Shamu,Peter Walter +1 more
TL;DR: Molecular genetic and biochemical studies described here suggest that, as in the case of growth factor receptors of higher eukaryotic cells, Ire1p oligomerizes in response to the accumulation of unfolded proteins in the ER and is phosphorylated in trans by otherIre1p molecules as a result of oligomerization.
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Signal integration in the endoplasmic reticulum unfolded protein response
David Ron,Peter Walter +1 more
TL;DR: Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids.
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The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Peter Walter,David Ron +1 more
TL;DR: The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum, where they fold and assemble, and only properly assembled proteins advance from the ER to the cell surface.
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Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation
Kevin J. Travers,Christopher K Patil,Lisa Wodicka,David J. Lockhart,Jonathan S. Weissman,Peter Walter +5 more
TL;DR: The unfolded protein response and ERAD are dynamic responses required for the coordinated disposal of misfolded proteins even in the absence of acute stress.
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IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
Jonathan H. Lin,Han Li,Douglas Yasumura,Hannah R. Cohen,Chao Zhang,Barbara Panning,Kevan M. Shokat,Matthew M. LaVail,Peter Walter +8 more
TL;DR: There is a causal link between the duration of UPR branch signaling and life or death cell fate after ER stress, and key findings from studies in cell culture were recapitulated in photoreceptors expressing mutant rhodopsin in animal models of retinitis pigmentosa.