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6 documents found
1: Title: Exploiting the kinesin-1 molecular motor to generate a virus membrane penetration site.
Journal: Nature communications (Nat Commun), Vol. 8, 2017 .
Snippet: Here we probe how the non-enveloped polyomavirus SV40 penetrates the endoplasmic reticulum (ER) membrane to reach the cytosol, a crucial infection step.
Affiliation: Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA. .
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2: Title: Tetrameric Assembly of K(+) Channels Requires ER-Located Chaperone Proteins.
Authors: Li, Kai, et.al. .
Journal: Molecular cell (Mol Cell), Vol. 65 (1): 52-65, 2017 .
Snippet: Human J-proteins DNAJB12 and DNAJB14 promoted tetrameric assembly of ERG (and Kv4.2) K(+) channel subunits through a heat shock protein (HSP) 70-independent mechanism, whereas a mutated DNAJB12 that did not undergo oligomerization itself failed to assemble ERG channel subunits into tetramers in vitro and in C. elegans.
Affiliation: Institute of Neuroscience and State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; University of Chinese Academy of Sciences, Shanghai 200031, PRC. Institute of Neuroscience and State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. Institute of Neuroscience and State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. Electronic address: sqcai@ion.ac.cn. .
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3: Title: Differential Genes Expression between Fertile and Infertile Spermatozoa Revealed by Transcriptome Analysis.
Authors: Bansal, Sandeep Kumar, et.al. .
Journal: PloS one, Vol. 10 (5): e0127007, 2015 .
Snippet: Some of these transcripts were related to heat shock proteins (DNAJB4, DNAJB14), testis specific genes (TCP11, TESK1, TSPYL1, ADAD1), and Y-chromosome genes (DAZ1, TSPYL1).
Affiliation: Division of Endocrinology, Central Drug Research Institute, Lucknow, India. Department of Urology, King George's Medical University (KGMU), Lucknow, India. .
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4: Title: Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure.
Authors: Goodwin, Edward C, et.al. .
Journal: PloS one, Vol. 9 (4): e94322, 2014 .
Snippet: DNAJB12 and DNAJB14 are transmembrane proteins in the endoplasmic reticulum (ER) that serve as co-chaperones for Hsc70/Hsp70 heat shock proteins.
Affiliation: Department of Genetics, Yale School of Medicine, New Haven, Connecticut, United States of America. Department of Cell Biology, Yale School of Medicine, New Haven, Connecticut, United States of America. Department of Genetics, Yale School of Medicine, New Haven, Connecticut, United States of America; Department of Therapeutic Radiology, Yale School of Medicine, New Haven, Connecticut, United States of America; Department of Molecular Biophysics & Biochemistry, Yale School of Medicine, New Haven, Connecticut, United States of America; Yale Cancer Center, New Haven, Connecticut, United States of America. .
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5: Title: A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum.
Journal: PLoS pathogens (Plos Pathog), Vol. 10 (3): e1004007, 2014 .
Snippet: We find the cytosolic SGTA-Hsc70 complex interacts with the ER transmembrane J-proteins DnaJB14 (B14) and DnaJB12 (B12), two cellular factors previously implicated in SV40 infection.
Affiliation: Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America; Cellular and Molecular Biology Graduate Program, Ann Arbor, Michigan, United States of America. Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America. .
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6: Title: A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins.
Authors: Sopha, Pattarawut, et.al. .
Journal: Cell structure and function (Cell Struct Funct), Vol. 37 (2): 177-87, 2012 .
Snippet: Remarkably, the overexpression of DNAJB14 accelerated the degradation of misfolded membrane proteins including a mutant of cystic fibrosis transmembrane conductance regulator (CFTRΔF508), but not that of a misfolded luminal protein.
Affiliation: Laboratory of Molecular and Cell Genetics, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan. .
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