Franklin

Chaperone systems of the endoplasmic reticulum / Linda M. Hendershot.

Author/Creator:
Hendershot, Linda M. , author
Publication:
London : Henry Stewart Talks, 2012.
Series:
Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis.
Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks, 2056-452X
Format/Description:
Video
1 online resource (1 streaming video file (49 min.)) : color, sound.
Subjects:
Cellular signal transduction.
Endoplasmic reticulum.
Molecular chaperones.
Protein folding.
Medical subjects:
Endoplasmic Reticulum.
Molecular Chaperones.
Protein Folding.
Signal Transduction.
System Details:
Mode of access: World Wide Web.
Contents:
Contents: Communication between cells
Angiogenesis
Secretion of effector molecules
Cell migration/homing
Proteins synthesis and 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.
Notes:
Animated audio-visual presentation with synchronized narration.
Title from title frames.
Publisher Number:
3159 Henry Stewart Talks
Access Restriction:
Restricted for use by site license.
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