Search Results - "Hipp, Mark S."

PolyQ Proteins Interfere with Nuclear Degradation of Cytosolic Proteins by Sequestering the Sis1p Chaperone by Park, Sae-Hun, Kukushkin, Yury, Gupta, Rajat, Chen, Taotao, Konagai, Ayano, Hipp, Mark S., Hayer-Hartl, Manajit, Hartl, F. Ulrich

“…Dysfunction of protein quality control contributes to the cellular pathology of polyglutamine (polyQ) expansion diseases and other neurodegenerative disorders…”
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Molecular chaperone functions in protein folding and proteostasis by Kim, Yujin E, Hipp, Mark S, Bracher, Andreas, Hayer-Hartl, Manajit, Hartl, F Ulrich

“…The biological functions of proteins are governed by their three-dimensional fold. Protein folding, maintenance of proteome integrity, and protein homeostasis…”
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Proteostasis impairment in protein-misfolding and -aggregation diseases by Hipp, Mark S, Park, Sae-Hun, Hartl, F. Ulrich

“…Highlights • Cells possess a complex proteostasis network (PN) to ensure protein homeostasis. • Aggregates permanently engage molecular chaperones and other PN…”
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In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment by Guo, Qiang, Lehmer, Carina, Martínez-Sánchez, Antonio, Rudack, Till, Beck, Florian, Hartmann, Hannelore, Pérez-Berlanga, Manuela, Frottin, Frédéric, Hipp, Mark S., Hartl, F. Ulrich, Edbauer, Dieter, Baumeister, Wolfgang, Fernández-Busnadiego, Rubén

“…Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link…”
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The endoplasmic reticulum: A hub of protein quality control in health and disease by Vincenz-Donnelly, Lisa, Hipp, Mark S.

“…One third of the eukaryotic proteome is synthesized at the endoplasmic reticulum (ER), whose unique properties provide a folding environment substantially…”
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In Situ Architecture and Cellular Interactions of PolyQ Inclusions by Bäuerlein, Felix J.B., Saha, Itika, Mishra, Archana, Kalemanov, Maria, Martínez-Sánchez, Antonio, Klein, Rüdiger, Dudanova, Irina, Hipp, Mark S., Hartl, F. Ulrich, Baumeister, Wolfgang, Fernández-Busnadiego, Rubén

“…Expression of many disease-related aggregation-prone proteins results in cytotoxicity and the formation of large intracellular inclusion bodies. To gain…”
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In situ architecture of neuronal α-Synuclein inclusions by Trinkaus, Victoria A., Riera-Tur, Irene, Martínez-Sánchez, Antonio, Bäuerlein, Felix J. B., Guo, Qiang, Arzberger, Thomas, Baumeister, Wolfgang, Dudanova, Irina, Hipp, Mark S., Hartl, F. Ulrich, Fernández-Busnadiego, Rubén

“…The molecular architecture of α-Synuclein (α-Syn) inclusions, pathognomonic of various neurodegenerative disorders, remains unclear. α-Syn inclusions were long…”
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Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons by Riemenschneider, Henrick, Guo, Qiang, Bader, Jakob, Frottin, Frédéric, Farny, Daniel, Kleinberger, Gernot, Haass, Christian, Mann, Matthias, Hartl, F. Ulrich, Baumeister, Wolfgang, Hipp, Mark S, Meissner, Felix, Fernández‐Busnadiego, Rubén, Edbauer, Dieter

“…Aggregation of the multifunctional RNA‐binding protein TDP‐43 defines large subgroups of amyotrophic lateral sclerosis and frontotemporal dementia and…”
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The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model by Yuste-Checa, Patricia, Trinkaus, Victoria A., Riera-Tur, Irene, Imamoglu, Rahmi, Schaller, Theresa F., Wang, Huping, Dudanova, Irina, Hipp, Mark S., Bracher, Andreas, Hartl, F. Ulrich

“…Spreading of aggregate pathology across brain regions acts as a driver of disease progression in Tau-related neurodegeneration, including Alzheimer’s disease…”
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Spatiotemporal Proteomic Profiling of Huntington’s Disease Inclusions Reveals Widespread Loss of Protein Function by Hosp, Fabian, Gutiérrez-Ángel, Sara, Schaefer, Martin H., Cox, Jürgen, Meissner, Felix, Hipp, Mark S., Hartl, F.-Ulrich, Klein, Rüdiger, Dudanova, Irina, Mann, Matthias

“…Aggregation of polyglutamine-expanded huntingtin exon 1 (HttEx1) in Huntington’s disease (HD) proceeds from soluble oligomers to late-stage inclusions. The…”
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Sis1 potentiates the stress response to protein aggregation and elevated temperature by Klaips, Courtney L., Gropp, Michael H. M., Hipp, Mark S., Hartl, F. Ulrich

“…Cells adapt to conditions that compromise protein conformational stability by activating various stress response pathways, but the mechanisms used in sensing…”
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Molecular and structural architecture of polyQ aggregates in yeast by Gruber, Anselm, Hornburg, Daniel, Antonin, Matthias, Krahmer, Natalie, Collado, Javier, Schaffer, Miroslava, Zubaite, Greta, Lüchtenborg, Christian, Sachsenheimer, Timo, Brügger, Britta, Mann, Matthias, Baumeister, Wolfgang, Hartl, F. Ulrich, Hipp, Mark S., Fernández-Busnadiego, Rubén

“…Huntington’s disease is caused by the expansion of a polyglutamine (polyQ) tract in the N-terminal exon of huntingtin (HttEx1), but the cellular mechanisms…”
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Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation by Trentini, Débora Broch, Pecoraro, Matteo, Tiwary, Shivani, Cox, Jürgen, Mann, Matthias, Hipp, Mark S., Hartl, F. Ulrich

“…Mammalian cells present a fingerprint of their proteome to the adaptive immune system through the display of endogenous peptides on MHC-I complexes…”
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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system by Saha, Itika, Yuste-Checa, Patricia, Da Silva Padilha, Miguel, Guo, Qiang, Körner, Roman, Holthusen, Hauke, Trinkaus, Victoria A., Dudanova, Irina, Fernández-Busnadiego, Rubén, Baumeister, Wolfgang, Sanders, David W., Gautam, Saurabh, Diamond, Marc I., Hartl, F. Ulrich, Hipp, Mark S.

“…Amyloid-like aggregates of the microtubule-associated protein Tau are associated with several neurodegenerative disorders including Alzheimer’s disease. The…”
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Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease by Hipp, Mark S, Patel, Chetan N, Bersuker, Kirill, Riley, Brigit E, Kaiser, Stephen E, Shaler, Thomas A, Brandeis, Michael, Kopito, Ron R

“…Pathognomonic accumulation of ubiquitin (Ub) conjugates in human neurodegenerative diseases, such as Huntington's disease, suggests that highly aggregated…”
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Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model by Frottin, Frédéric, Pérez-Berlanga, Manuela, Hartl, F Ulrich, Hipp, Mark S

“…The most frequent genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia is a G 4 C 2 repeat expansion in the C9orf72 gene. This expansion…”
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An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space by Bie, Anne Sigaard, Cömert, Cagla, Körner, Roman, Corydon, Thomas J., Palmfeldt, Johan, Hipp, Mark S., Hartl, F. Ulrich, Bross, Peter

“…The HSP60/HSP10 chaperonin assists folding of proteins in the mitochondrial matrix space by enclosing them in its central cavity. The chaperonin forms part of…”
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Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection by Riley, Brigit E, Kaiser, Stephen E, Shaler, Thomas A, Ng, Aylwin C.Y, Hara, Taichi, Hipp, Mark S, Lage, Kasper, Xavier, Ramnik J, Ryu, Kwon-Yul, Taguchi, Keiko, Yamamoto, Masayuki, Tanaka, Keiji, Mizushima, Noboru, Komatsu, Masaaki, Kopito, Ron R

“…Genetic ablation of autophagy in mice leads to liver and brain degeneration accompanied by the appearance of ubiquitin (Ub) inclusions, which has been…”
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High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins by Vincenz‐Donnelly, Lisa, Holthusen, Hauke, Körner, Roman, Hansen, Erik C, Presto, Jenny, Johansson, Jan, Sawarkar, Ritwick, Hartl, F Ulrich, Hipp, Mark S

“…Protein aggregation is associated with neurodegeneration and various other pathologies. How specific cellular environments modulate the aggregation of disease…”
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Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome by Ripaud, Leslie, Chumakova, Victoria, Antonin, Matthias, Hastie, Alex R., Pinkert, Stefan, Kömer, Roman, Ruff, Kiersten M., Pappu, Rohit V., Hornburg, Daniel, Mann, Matthias, Hartl, F. Ulrich, Hipp, Mark S.

“…Expansion of a poly-glutamine (polyQ) repeat in a group of functionally unrelated proteins is the cause of several inherited neurodegenerative disorders,…”
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