Title |
Identification and characterization of Iporin as a novel interaction partner for rab1
|
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Published in |
BMC Molecular and Cell Biology, March 2005
|
DOI | 10.1186/1471-2121-6-15 |
Pubmed ID | |
Authors |
Michael Bayer, Julia Fischer, Joachim Kremerskothen, Edith Ossendorf, Theodoros Matanis, Magdalena Konczal, Thomas Weide, Angelika Barnekow |
Abstract |
The small GTPase rab1a and its isoform rab1b are essential regulating components in the vesicle transport between the ER and the Golgi apparatus. Rab1 is thought to act as a molecular switch and can change between an active GTP-bound and an inactive GDP-bound conformation. To elucidate the function of rab1, several approaches have been established to isolate effector proteins, which interact with the activated conformation of rab1. To date p115, GM130, golgin-84 and MICAL have been identified as direct interacting partners. Together with rab1, these molecules are components of a protein complex, which mediates and regulates intracellular vesicle transport. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 3% |
Unknown | 35 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 10 | 28% |
Student > Ph. D. Student | 7 | 19% |
Professor > Associate Professor | 4 | 11% |
Student > Doctoral Student | 3 | 8% |
Lecturer | 2 | 6% |
Other | 5 | 14% |
Unknown | 5 | 14% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 20 | 56% |
Biochemistry, Genetics and Molecular Biology | 8 | 22% |
Immunology and Microbiology | 1 | 3% |
Medicine and Dentistry | 1 | 3% |
Unknown | 6 | 17% |