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Chaperone systems of the endoplasmic reticulum / Linda M. Hendershot.
- Format:
- Video
- Author/Creator:
- Hendershot, Linda M., speaker, author.
- Series:
- Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis.
- Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks, 2056-452X
- Language:
- English
- Subjects (All):
- Cellular signal transduction.
- Endoplasmic reticulum.
- Molecular chaperones.
- Protein folding.
- Endoplasmic Reticulum.
- Molecular Chaperones.
- Protein Folding.
- Signal Transduction.
- Medical Subjects:
- Endoplasmic Reticulum.
- Molecular Chaperones.
- Protein Folding.
- Signal Transduction.
- Genre:
- Video recordings.
- Physical Description:
- 1 online resource (1 streaming video file (49 min.)) : color, sound.
- polychrome
- Place of Publication:
- London : Henry Stewart Talks, 2012.
- System Details:
- Mode of access: World Wide Web.
- video file
- 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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