Member database | Pfam |
Pfam type | family |
Short name | HSP90 |
Author | Finn RD;0000-0001-8626-2148 |
Sequence Ontology | 0100021 |
Description Imported from IPR001404
References Imported from IPR001404
1.Microbial molecular chaperones. Lund PA. Adv. Microb. Physiol. 44, 93-140, (2001). View articlePMID: 11407116
2.The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Pratt WB. Proc. Soc. Exp. Biol. Med. 217, 420-34, (1998). View articlePMID: 9521088
3.Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Johnson JL. Biochim Biophys Acta 1823, 607-13, (2012). PMID: 22008467
4.Hsp90 and co-chaperones twist the functions of diverse client proteins. Zuehlke A, Johnson JL. Biopolymers 93, 211-7, (2010). PMID: 19697319
5.Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA. Mol Cell 53, 330-43, (2014). PMID: 24462206
6.Identification of Hsp90 as a species independent H5N1 avian influenza A virus PB2 interacting protein. Jirakanwisal K, Srisutthisamphan K, Thepparit C, Suptawiwat O, Auewarakul P, Paemanee A, Roytrakul S, Smith DR. Comp Immunol Microbiol Infect Dis 43, 28-35, (2015). PMID: 26616658