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151019 ||| eng |
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|a Hendershot, Linda M.
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|a Chaperone systems of the endoplasmic reticulum
|h Elektronische Ressource
|c Linda M. Hendershot
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|a London
|b Henry Stewart Talks
|c 2012, 2012
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|a 1 online resource (1 streaming video file (49 min.)
|b color, sound)
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|a Communication between cells -- Angiogenesis -- Secretion of effector molecules -- Cell migration/homing -- Proteins synthesis & folding -- Molecular chaperone families in the ER -- Antibody formation -- BiP: a soluble Hsp70 protein -- ATPase and DnaK peptide binding domains -- CH1 domain -- The formation of disulfide bonds -- ATPase cycle of BiP -- Disruption of BiP/GRP78 gene in mice -- Highly virulent subtilase toxin -- BiP functions in ER -- ER DnaJ proteins -- Gal-4-BiP ATPase domain fusion protein -- BAP/Sil1: a nucleotide releasing factor -- Potential consequences of BAP/Sil1 loss and mutations -- The family of large Hsp70 proteins -- The two functions of GRP170 -- GRP94 as an essential gene- Immunophilins -- lymphoid specific chaperone: pERp1
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|a Endoplasmic Reticulum
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|a Molecular chaperones
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|a Signal Transduction
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|a Cellular signal transduction
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|a Endoplasmic reticulum
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|a Protein folding
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|a Protein Folding
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|a Molecular Chaperones
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|a eng
|2 ISO 639-2
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|b HST
|a Henry Stewart Talks
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|a Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks
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|a Animated audio-visual presentation with synchronized narration. - Title from title frames. - Mode of access: World Wide Web. - System requirements: Browser compatibility: updated Mozilla Firefox, Google Chrome, Safari or Internet Explorer 8+. Browser settings: enable JavaScript, enable cookies from the Henry Stewart Talks site. Required Desktop Browser plugins & viewers: Updated Adobe Flash Player & Adobe Acrobat Reader. Mobile device & operating system versions: Android v4.0+, iPhone 4+ (iOS v6.x+), iPad 2+ (iOS v6.x+), BlackBerry OS v7.0+, Windows Phone v6.5.1+
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|u https://hstalks.com/bs/p/641
|3 Series
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|u https://hstalks.com/bs/2225
|x Verlag
|z Streaming video file
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|a 570
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