Localisation of Theiler's murine encephalomyelitis virus protein 2C to the golgi apparatus using antibodies generated against a peptide region:
- Jauka, Tembisa, Mutsvunguma, Lorraine Z, Boshoff, Aileen, Edkins, Adrienne L, Knox, Caroline M
- Authors: Jauka, Tembisa , Mutsvunguma, Lorraine Z , Boshoff, Aileen , Edkins, Adrienne L , Knox, Caroline M
- Date: 2010
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165074 , vital:41206 , DOI: 10.1016/j.jviromet.2010.05.009
- Description: The picornavirus 2C protein is highly conserved and indispensible for virus replication. Polyclonal antibodies against Theiler's murine encephalomyelitis virus (TMEV) 2C protein were generated by immunisation of rabbits with a peptide comprising amino acids 31–210 of the protein. Antibodies were used to investigate the localisation of 2C in infected cells by indirect immunofluorescence and confocal microscopy. Analysis of infected cells revealed that the distribution of 2C changed during infection.
- Full Text:
- Date Issued: 2010
- Authors: Jauka, Tembisa , Mutsvunguma, Lorraine Z , Boshoff, Aileen , Edkins, Adrienne L , Knox, Caroline M
- Date: 2010
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165074 , vital:41206 , DOI: 10.1016/j.jviromet.2010.05.009
- Description: The picornavirus 2C protein is highly conserved and indispensible for virus replication. Polyclonal antibodies against Theiler's murine encephalomyelitis virus (TMEV) 2C protein were generated by immunisation of rabbits with a peptide comprising amino acids 31–210 of the protein. Antibodies were used to investigate the localisation of 2C in infected cells by indirect immunofluorescence and confocal microscopy. Analysis of infected cells revealed that the distribution of 2C changed during infection.
- Full Text:
- Date Issued: 2010
General structural and functional features of molecular chaperones:
- Edkins, Adrienne L, Boshoff, Aileen
- Authors: Edkins, Adrienne L , Boshoff, Aileen
- Date: 2014
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164808 , vital:41174 , ISBN 978-94-007-7437-7 , DOI: 10.1007/978-94-007-7438-4_2
- Description: Molecular chaperones are a group of structurally diverse and highly conserved ubiquitous proteins. They play crucial roles in facilitating the correct folding of proteins in vivo by preventing protein aggregation or facilitating the appropriate folding and assembly of proteins. Heat shock proteins form the major class of molecular chaperones that are responsible for protein folding events in the cell. This is achieved by ATP-dependent (folding machines) or ATP-independent mechanisms (holders). Heat shock proteins are induced by a variety of stresses, besides heat shock. The large and varied heat shock protein class is categorised into several subfamilies based on their sizes in kDa namely, small Hsps (HSPB), Hsp40 (DNAJ), Hsp60 (HSPD/E; Chaperonins), Hsp70 (HSPA), Hsp90 (HSPC), and Hsp100.
- Full Text:
- Date Issued: 2014
- Authors: Edkins, Adrienne L , Boshoff, Aileen
- Date: 2014
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164808 , vital:41174 , ISBN 978-94-007-7437-7 , DOI: 10.1007/978-94-007-7438-4_2
- Description: Molecular chaperones are a group of structurally diverse and highly conserved ubiquitous proteins. They play crucial roles in facilitating the correct folding of proteins in vivo by preventing protein aggregation or facilitating the appropriate folding and assembly of proteins. Heat shock proteins form the major class of molecular chaperones that are responsible for protein folding events in the cell. This is achieved by ATP-dependent (folding machines) or ATP-independent mechanisms (holders). Heat shock proteins are induced by a variety of stresses, besides heat shock. The large and varied heat shock protein class is categorised into several subfamilies based on their sizes in kDa namely, small Hsps (HSPB), Hsp40 (DNAJ), Hsp60 (HSPD/E; Chaperonins), Hsp70 (HSPA), Hsp90 (HSPC), and Hsp100.
- Full Text:
- Date Issued: 2014
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