Title |
Immunophilins: for the love of proteins
|
---|---|
Published in |
Cellular and Molecular Life Sciences, October 2006
|
DOI | 10.1007/s00018-006-6215-3 |
Pubmed ID | |
Authors |
S. Barik |
Abstract |
Immunophilins are chaperones that may also exhibit peptidylprolyl isomerase (PPIase) activity. This review summarizes our knowledge of the two largest families of immunophilins, namely cyclophilin and FK506-binding protein, and a novel chimeric dual-family immunophilin, named FK506- and cyclosporin-binding protein (FCBP). The larger members of each family are modular in nature, consisting of multiple PPIase and/or protein-protein interaction domains. Despite the apparent difference in their sequence and three-dimensional structure, the three families encode similar enzymatic and biological functions. Recent studies have revealed that many immunophilins possess a chaperone function independent of PPIase activity. Knockout animal studies have confirmed multiple essential roles of immunophilins in physiology and development. An immunophilin is indeed a natural 'protein-philin' (Greek 'philin' = friend) that interacts with proteins to guide their proper folding and assembly. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 3 | 2% |
United Kingdom | 2 | 2% |
Ireland | 1 | <1% |
Brazil | 1 | <1% |
Unknown | 123 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 34 | 26% |
Researcher | 19 | 15% |
Student > Master | 16 | 12% |
Student > Bachelor | 14 | 11% |
Student > Doctoral Student | 9 | 7% |
Other | 18 | 14% |
Unknown | 20 | 15% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 49 | 38% |
Biochemistry, Genetics and Molecular Biology | 30 | 23% |
Medicine and Dentistry | 10 | 8% |
Immunology and Microbiology | 7 | 5% |
Chemistry | 5 | 4% |
Other | 9 | 7% |
Unknown | 20 | 15% |