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Keywords: Protein folding
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Membrane Trafficking
J Cell Sci (2023) 136 (2): jcs260656.
Published: 19 January 2023
... Ellgaard , L. , Mccaul , N. , Chatsisvili , A. and Braakman , I. ( 2016 ). Co- and post-translational protein folding in the ER . Traffic 17 , 615 - 638 . 10.1111/tra.12392 Ellgaard , L. , Sevier , C. S. and Bulleid , N. J. ( 2018 ). How are proteins reduced...
Journal Articles
J Cell Sci (2020) 133 (22): jcs251983.
Published: 27 November 2020
... how errors in membrane protein biogenesis can trigger co-translational degradation that employs machinery of the ribosome-associated quality control pathway. Endoplasmic reticulum Membrane protein Protein folding Ribosome Translation Eukaryotic cells can expend up to 30...
Journal Articles
J Cell Sci (2020) 133 (21): jcs240366.
Published: 10 November 2020
... involved in oxidative protein folding ( Zito et al., 2010 ; Zito, 2013 ). Prx4, together with glutathione peroxidase 7 and 8, scavenges H 2 O 2 molecules that might accumulate in the ER as a byproduct of oxidative folding or NADPH oxidase 4 (NOX4) activity ( Ramming and Appenzeller-Herzog, 2013...
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
... responsibilities overseen by client proteins requiring the EMC for maturation. EMC Membrane protein Protein quality control Protein folding The eukaryotic endoplasmic reticulum (ER) houses the machinery responsible for biogenesis of secreted and integral membrane proteins. Insertion, folding...
Journal Articles
J Cell Sci (2020) 133 (3): jcs231340.
Published: 4 February 2020
...., 2005 ; Dudek et al., 2005 , 2002 ). The unfolded protein response (UPR) reduces the load of translated ER proteins and increases the ER-folding capacity upon stress through the initiation of a transcription program that increases the protein-folding capacity and decreases further protein...
Includes: Supplementary data
Journal Articles
J Cell Sci (2015) 128 (6): 1180–1192.
Published: 15 March 2015
... 01 2015 © 2015. Published by The Company of Biologists Ltd 2015 * Author for correspondence ( reyhuei@gate.sinica.edu.tw ) Competing interests The authors declare no competing or financial interests. Chaperone Protein folding Protein phosphatase 1 Cdc48 Shp1...
Includes: Supplementary data
Journal Articles
J Cell Sci (2012) 125 (21): 5073–5083.
Published: 1 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: 1 March 2010
... a general strategy for both non-secretory and specialized secretory cells. * Present address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK ‡ Author for correspondence ( i.braakman@uu.nl ) 3 12 2009 © 2010. 2010 Protein folding Folding stress...
Includes: Supplementary data
Journal Articles
J Cell Sci (2009) 122 (18): 3322–3329.
Published: 15 September 2009
... The Company of Biologists Limited 2009 2009 Unconventional protein secretion Non-classical export Membrane translocation Fibroblast growth factor 2 FGF2 Protein folding Quality control The molecular mechanisms of unconventional secretory processes have been a long-standing mystery...
Journal Articles
J Cell Sci (2008) 121 (5): 717–723.
Published: 1 March 2008
... identify a new role for HSP90 in protein sorting, pointing to a central role for this molecular chaperone in the cell. 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...
Journal Articles
J Cell Sci (2006) 119 (21): 4373–4380.
Published: 1 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
.... B. ( 1997 ). Macromolecular crowding: effects on actin polymerization. Biophys. Chem. 66 , 57 -66. Martin, J. ( 2002 ). Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding. Biochemistry 41 , 5050 -5055. May, A. and Huehns...
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
... retention of SI Q1098P in ERGIC and cis-Golgi in phenotype II of CSID. Sucrase-isomaltase ER-quality control cis-Golgi ERGIC Protein folding Phenylalanine-based motif A physiological malfunction in many genetic disorders is elicited by an altered folding determinant in a protein due...
Journal Articles
J Cell Sci (2005) 118 (7): 1485–1492.
Published: 1 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: 1 July 2004
... 2004 © The Company of Biologists Limited 2004 2004 Actin Nemaline myopathy Actin polymerization Protein folding Myopathy Actin mutations We did not express the non-folding mutants from category I but we did express representative mutants from categories II, III and IV...
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: 1 November 2002
...-mail: hepstein@bcm.tmc.edu ) © The Company of Biologists Limited 2002 2002 UCS Myosin chaperone UNC-45 Protein folding Myosins are a large family of protein motors that contain at least 18 different classes. They interact with actin filaments to generate a broad spectrum of eukaryotic cell...