Search Results - "KIMMIG, Philipp"

Regulated Ire1-dependent mRNA decay requires no-go mRNA degradation to maintain endoplasmic reticulum homeostasis in S. pombe by Guydosh, Nicholas R, Kimmig, Philipp, Walter, Peter, Green, Rachel

“…The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In , the ER membrane-resident…”
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Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis by Lu, Min, Lawrence, David A., Marsters, Scot, Acosta-Alvear, Diego, Kimmig, Philipp, Mendez, Aaron S., Paton, Adrienne W., Paton, James C., Walter, Peter, Ashkenazi, Avi

“…Protein folding by the endoplasmic reticulum (ER) is physiologically critical; its disruption causes ER stress and augments disease. ER stress activates the…”
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Functional mapping of yeast genomes by saturated transposition by Michel, Agnès H, Hatakeyama, Riko, Kimmig, Philipp, Arter, Meret, Peter, Matthias, Matos, Joao, De Virgilio, Claudio, Kornmann, Benoît

“…Yeast is a powerful model for systems genetics. We present a versatile, time- and labor-efficient method to functionally explore the genome using saturated…”
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The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis by Kimmig, Philipp, Diaz, Marcy, Zheng, Jiashun, Williams, Christopher C, Lang, Alexander, Aragón, Tomas, Li, Hao, Walter, Peter

“…The unfolded protein response (UPR) monitors the protein folding capacity of the endoplasmic reticulum (ER). In all organisms analyzed to date, the UPR drives…”
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Engineering ER-stress dependent non-conventional mRNA splicing by Li, Weihan, Okreglak, Voytek, Peschek, Jirka, Kimmig, Philipp, Zubradt, Meghan, Weissman, Jonathan S, Walter, Peter

“…The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The…”
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The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism by Santt, Olivier, Pfirrmann, Thorsten, Braun, Bernhard, Juretschke, Jeannette, Kimmig, Philipp, Scheel, Hartmut, Hofmann, Kay, Thumm, Michael, Wolf, Dieter H

“…Glucose-dependent regulation of carbon metabolism is a subject of intensive studies. We have previously shown that the switch from gluconeogenesis to…”
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Basic leucine zipper transcription factor Hac1 binds DNA in two distinct modes as revealed by microfluidic analyses by Fordyce, Polly M, Pincus, David, Kimmig, Philipp, Nelson, Christopher S, El-Samad, Hana, Walter, Peter, DeRisi, Joseph L

“…A quantitative understanding of how transcription factors interact with genomic target sites is crucial for reconstructing transcriptional networks in vivo…”
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The “Intracellular” Poly(3-Hydroxybutyrate) (PHB) Depolymerase of Rhodospirillum rubrum Is a Periplasm-Located Protein with Specificity for Native PHB and with Structural Similarity to Extracellular PHB Depolymerases by HANDRICK, René, REINHARDT, Simone, KIMMIG, Philipp, JENDROSSEK, Dieter

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Regulating ER Protein Folding Homeostasis By Distinctively Processing mRNAs by Li, Weihan, Okreglak, Voytek, Peschek, Jirka, Kimmig, Philipp, Walter, Peter

“…The endoplasmic reticulum (ER) is the major folding compartment for most secretory and plasma membrane proteins in the cell. A conserved signaling pathway, the…”
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Basic leucine zipper transcription factor Hac1 binds DNA in two distinct modes as revealed by microfluidic analyses by Fordyce, Polly M., Pincus, David, Kimmig, Philipp, Nelson, Christopher S., El-Samad, Hana, Walter, Peter, DeRisi, Joseph L.

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The "intracellular" poly(3-Hydroxybutyrate) (PHB) depolymerase of Rhodospirillum rubrum is a periplasm-located protein with specificity for native PHB and with structural by Handrick, Rene, Reinhardt, Simone, Kimmig, Philipp, Jendrossek, Dieter

“…Rhodospirillum rubrum possesses a putative intracellular poly(3-hydroxybutyrate) (PHB) depolymerase system consisting of a soluble PHB depolymerase, a…”
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