Journalism students’ motivations and expectations of their work in comparative perspective:
- Hanusch, Folker, Mellado, Claudia, Boshoff, Priscilla A, Humanes, María Luisa, De León, Salvador, Pereira, Fabio, Márquez Ramírez, Mireya, Roses, Sergio, Subervi, Federico, Wyss, Vinzenz, Yez, Lyuba
- Authors: Hanusch, Folker , Mellado, Claudia , Boshoff, Priscilla A , Humanes, María Luisa , De León, Salvador , Pereira, Fabio , Márquez Ramírez, Mireya , Roses, Sergio , Subervi, Federico , Wyss, Vinzenz , Yez, Lyuba
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/143425 , vital:38245 , DOI: 10.1177/1077695814554295
- Description: Based on a survey of 4,393 journalism students in Australia, Brazil, Chile, Mexico, South Africa, Spain, Switzerland, and the United States, this study provides much-needed comparative evidence about students’ motivations for becoming journalists, their future job plans, and expectations. Findings show not only an almost universal decline in students’ desire to work in journalism by the end of their program but also important national differences in terms of the journalistic fields in which they want to work, as well as their job expectations. The results reinforce the need to take into account national contexts when examining journalism education across the globe.
- Full Text:
- Date Issued: 2015
- Authors: Hanusch, Folker , Mellado, Claudia , Boshoff, Priscilla A , Humanes, María Luisa , De León, Salvador , Pereira, Fabio , Márquez Ramírez, Mireya , Roses, Sergio , Subervi, Federico , Wyss, Vinzenz , Yez, Lyuba
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/143425 , vital:38245 , DOI: 10.1177/1077695814554295
- Description: Based on a survey of 4,393 journalism students in Australia, Brazil, Chile, Mexico, South Africa, Spain, Switzerland, and the United States, this study provides much-needed comparative evidence about students’ motivations for becoming journalists, their future job plans, and expectations. Findings show not only an almost universal decline in students’ desire to work in journalism by the end of their program but also important national differences in terms of the journalistic fields in which they want to work, as well as their job expectations. The results reinforce the need to take into account national contexts when examining journalism education across the globe.
- Full Text:
- Date Issued: 2015
Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function
- Tastan Bishop, Özlem, Edkins, Adrienne L, Blatch, Gregory L
- Authors: Tastan Bishop, Özlem , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/126932 , vital:35936 , https://doi.10.1002/jez.b.22541
- Description: Molecular chaperones and their associated co‐chaperones play an important role in preserving and regulating the active conformational state of cellular proteins. The chaperone complement of the Indonesian Coelacanth, Latimeria menadoensis, was elucidated using transcriptomic sequences. Heat shock protein 90 (Hsp90) and heat shock protein 40 (Hsp40) chaperones, and associated cochaperones were focused on, and homologous human sequences were used to search the sequence databases. Coelacanth homologs of the cytosolic, mitochondrial and endoplasmic reticulum (ER) homologs of human Hsp90 were identified, as well as all of the major co‐chaperones of the cytosolic isoform. Most of the human Hsp40s were found to have coelacanth homologs, and the data suggested that all of the chaperone machinery for protein folding at the ribosome, protein translocation to cellular compartments such as the ER and protein degradation were conserved. Some interesting similarities and differences were identified when interrogating human, mouse, and zebrafish homologs. For example, DnaJB13 is predicted to be a non‐functional Hsp40 in humans, mouse, and zebrafish due to a corrupted histidine‐proline‐aspartic acid (HPD) motif, while the coelacanth homolog has an intact HPD. These and other comparisons enabled important functional and evolutionary questions to be posed for future experimental studies.
- Full Text:
- Date Issued: 2014
- Authors: Tastan Bishop, Özlem , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/126932 , vital:35936 , https://doi.10.1002/jez.b.22541
- Description: Molecular chaperones and their associated co‐chaperones play an important role in preserving and regulating the active conformational state of cellular proteins. The chaperone complement of the Indonesian Coelacanth, Latimeria menadoensis, was elucidated using transcriptomic sequences. Heat shock protein 90 (Hsp90) and heat shock protein 40 (Hsp40) chaperones, and associated cochaperones were focused on, and homologous human sequences were used to search the sequence databases. Coelacanth homologs of the cytosolic, mitochondrial and endoplasmic reticulum (ER) homologs of human Hsp90 were identified, as well as all of the major co‐chaperones of the cytosolic isoform. Most of the human Hsp40s were found to have coelacanth homologs, and the data suggested that all of the chaperone machinery for protein folding at the ribosome, protein translocation to cellular compartments such as the ER and protein degradation were conserved. Some interesting similarities and differences were identified when interrogating human, mouse, and zebrafish homologs. For example, DnaJB13 is predicted to be a non‐functional Hsp40 in humans, mouse, and zebrafish due to a corrupted histidine‐proline‐aspartic acid (HPD) motif, while the coelacanth homolog has an intact HPD. These and other comparisons enabled important functional and evolutionary questions to be posed for future experimental studies.
- Full Text:
- Date Issued: 2014
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