Hendershot, Linda M.

Chaperone systems of the endoplasmic reticulum [electronic resource] / Linda M. Hendershot. - London : Henry Stewart Talks, 2012. - 1 online resource (1 streaming video file (49 min.) : color, sound). - Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks, 2056-452X . - Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis. .

Animated audio-visual presentation with synchronized narration. Title from title frames.

Contents: 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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Mode of access: World Wide Web.

3159 Henry Stewart Talks


Cellular signal transduction.
Endoplasmic reticulum.
Molecular chaperones.
Protein folding.
Endoplasmic Reticulum.
Molecular Chaperones.
Protein Folding.
Signal Transduction.
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