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Keywords: Protein folding
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Journal Articles
J Cell Sci (2020) 133 (22): jcs251983.
Published: 27 November 2020
... pathway. Endoplasmic reticulum Membrane protein Protein folding Ribosome Translation Eukaryotic cells can expend up to 30% of their energy resources on the production of new proteins ( Buttgereit and Brand, 1995 ). One reason that protein synthesis accounts for such a large proportion...
Journal Articles
J Cell Sci (2020) 133 (21): jcs240366.
Published: 10 November 2020
...-retention motif and rely on ERp44 for their intracellular localization are considered ERp44 partners ( Anelli et al., 2003 ; Otsu et al., 2006 ; Kakihana et al., 2013 ). We define them as partners as they are enzymes involved in protein folding and processing in the early secretory pathway (a job shared...
Journal Articles
J Cell Sci (2020) 133 (8): jcs241976.
Published: 30 April 2020
... sensitivity demonstrates the requirement for a membrane protein to shuttle electrons from the cytosol to the ER. These results provide compelling evidence for the crucial role of the cytosol in regulating ER redox homeostasis, ensuring correct protein folding and facilitating the degradation of misfolded ER...
Journal Articles
J Cell Sci (2020) 133 (8): jcs243519.
Published: 24 April 2020
... is an important factor facilitating membrane protein biogenesis. Here we discuss the broad cellular and organismal responsibilities overseen by client proteins requiring the EMC for maturation. EMC Membrane protein Protein quality control Protein folding The eukaryotic endoplasmic reticulum (ER...
Journal Articles
J Cell Sci (2020) 133 (3): jcs231340.
Published: 04 February 2020
..., have yielded many new insights into the main gate of the secretory pathway. Cryo-EM Endoplasmic reticulum N-glycosylation Protein folding Translocon The endoplasmic reticulum (ER) is the starting point of the secretory pathway ( Johnson and van Waes, 1999 ). Freshly synthesized...
Includes: Supplementary data
Journal Articles
J Cell Sci (2015) 128 (6): 1180–1192.
Published: 15 March 2015
... due to a change in the stoichiometry of PP1 components. Taken together, these results indicate that association with the regulatory subunits Sds22 and Ypi1 prevents misfolding and aggregation of Glc7. Chaperone Protein folding Protein phosphatase 1 Cdc48 Shp1 Type 1 protein serine...
Includes: Supplementary data
Journal Articles
J Cell Sci (2012) 125 (21): 5073–5083.
Published: 01 November 2012
... and in vitro assays, we show that proteins in the process of synthesis/folding are particularly sensitive to arsenite-induced aggregation, that arsenite interferes with protein folding by acting on unfolded polypeptides, and that arsenite directly inhibits chaperone activity. Thus, folding inhibition...
Includes: Supplementary data
Journal Articles
J Cell Sci (2010) 123 (5): 787–794.
Published: 01 March 2010
... from the mammalian unfolded protein response regulates expression of endoplasmic reticulum chaperones in non-stressed cells . EMBO J. 16 , 7207 - 7216 . Christis C. , Lubsen N. H. , Braakman I. ( 2008 ). Protein folding includes oligomerization-examples from the endoplasmic...
Includes: Supplementary data
Journal Articles
J Cell Sci (2009) 122 (18): 3322–3329.
Published: 15 September 2009
...., Becker, K., Schleyer, M., Guiard, B., Tropschug, M., Horwich, A. L., Pfanner, N. and Neupert, W. ( 1991 ). Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. J. Cell Biol. 115 , 1601 -1609. Zehe, C., Engling, A., Wegehingel, S., Schäfer, T. and Nickel, W...
Journal Articles
J Cell Sci (2008) 121 (5): 717–723.
Published: 01 March 2008
... for immunofluorescence detection of GM130. HSP90 Molecular chaperones Protein folding Radicicol Heat shock protein 90 kDa (hereafter termed HSP90) works in an ATP-dependent manner to regulate the activity of a limited subset of medically relevant signalling proteins such as steroid hormone receptors...
Journal Articles
J Cell Sci (2006) 119 (21): 4373–4380.
Published: 01 November 2006
... chaperones has revealed important new information on the mechanisms regulating protein folding and quality control. Tight regulation of N -glycan modifications is crucial to maintain protein quality control, to ensure the synthesis of functional polypeptides and to avoid constipation of the ER with folding...
Journal Articles
J Cell Sci (2006) 119 (14): 2863–2869.
Published: 15 July 2006
.... e-mail: minton@helix.nih.gov 23 5 2006 © The Company of Biologists Limited 2006 2006 Protein associations Protein stability Protein folding Macromolecular crowding Macromolecular confinement Macromolecular adsorption Although the time when a living cell was regarded...
Journal Articles
J Cell Sci (2006) 119 (4): 615–623.
Published: 15 February 2006
... that ERp57 participates in glycoprotein biogenesis either alone or in tandem with calnexin and calreticulin. e-mail: david.williams@utoronto.ca 22 12 2005 © The Company of Biologists Limited 2006 2006 Calnexin Calreticulin Endoplasmic reticulum Quality control Protein folding...
Journal Articles
J Cell Sci (2005) 118 (12): 2775–2784.
Published: 15 June 2005
... temperature-sensitive characteristics to SI Q1098P ( Fig. 2 ). * Author for correspondence (e-mail: hassan.naim@tiho-hannover.de ) 9 3 2005 © The Company of Biologists Limited 2005 2005 Sucrase-isomaltase ER-quality control cis-Golgi ERGIC Protein folding Phenylalanine-based...
Journal Articles
J Cell Sci (2005) 118 (7): 1485–1492.
Published: 01 April 2005
...Zlatka Kostova; Dieter H. Wolf In the endoplasmic reticulum (ER), N -linked glycans (N-glycans) function as signals to recruit the lectin chaperones involved in protein folding, quality control and ER-associated degradation. We undertook a systematic study of the four N-glycans of mutated...
Journal Articles
J Cell Sci (2004) 117 (18): 4055–4066.
Published: 15 August 2004
...Takunari Yoneda; Cristina Benedetti; Fumihiko Urano; Scott G. Clark; Heather P. Harding; David Ron Protein folding in the mitochondria is assisted by nuclear-encoded compartment-specific chaperones but regulation of the expression of their encoding genes is poorly understood. We found...
Includes: Supplementary data
Journal Articles
J Cell Sci (2004) 117 (15): 3367–3377.
Published: 01 July 2004
... of Geneva, 1211 Geneva 4, Switzerland ‡ Present address: Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, UK 23 2 2004 © The Company of Biologists Limited 2004 2004 Actin Nemaline myopathy Actin polymerization Protein folding...
Journal Articles
J Cell Sci (2004) 117 (6): 907–918.
Published: 22 February 2004
...Philippe Collin; Pascale B. Beauregard; Aram Elagöz; Luis A. Rokeach Calnexin is a molecular chaperone playing key roles in protein folding and the quality control of this process in the endoplasmic reticulum. We, and others, have previously demonstrated that cnx1 + , the gene encoding...
Journal Articles
J Cell Sci (2002) 115 (21): 3983–3990.
Published: 01 November 2002
... of a myosin II-containing progenitor for actomyosin ring assembly in fission yeast. Curr. Biol. 12 , 724 -729. * Author for correspondence (e-mail: hepstein@bcm.tmc.edu ) © The Company of Biologists Limited 2002 2002 UCS Myosin chaperone UNC-45 Protein folding Myosins...
Journal Articles
J Cell Sci (2002) 115 (14): 2809–2816.
Published: 15 July 2002
...., Grammatikakis, A., Tsichlis, P. N. and Cochran, B. H. ( 1999 ). p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function. Mol. Cell Biol. 19 , 1661 -1672. Hartl, F. U. ( 1996 ). Molecular chaperones in cellular protein folding. Nature 381 , 571 -579. Hartl, F. U. and Hayer-Hartl...