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2. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. Seraphim TV; Alves MM; Silva IM; Gomes FE; Silva KP; Murta SM; Barbosa LR; Borges JC PLoS One; 2013; 8(6):e66822. PubMed ID: 23826147 [TBL] [Abstract][Full Text] [Related]
3. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Batista FAH; Seraphim TV; Santos CA; Gonzaga MR; Barbosa LRS; Ramos CHI; Borges JC Arch Biochem Biophys; 2016 Jun; 600():12-22. PubMed ID: 27103305 [TBL] [Abstract][Full Text] [Related]
4. Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. Batista FA; Almeida GS; Seraphim TV; Silva KP; Murta SM; Barbosa LR; Borges JC FEBS J; 2015 Jan; 282(2):388-406. PubMed ID: 25369258 [TBL] [Abstract][Full Text] [Related]
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6. Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities. Coto ALS; Seraphim TV; Batista FAH; Dores-Silva PR; Barranco ABF; Teixeira FR; Gava LM; Borges JC Int J Biol Macromol; 2018 Oct; 118(Pt A):693-706. PubMed ID: 29959008 [TBL] [Abstract][Full Text] [Related]
7. Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart. Tassone G; Mangani S; Botta M; Pozzi C Biochim Biophys Acta Proteins Proteom; 2018 Nov; 1866(11):1190-1198. PubMed ID: 30248409 [TBL] [Abstract][Full Text] [Related]
8. Discovery of small molecule inhibitors of Batista FAH; Ramos SL; Tassone G; Leitão A; Montanari CA; Botta M; Mori M; Borges JC J Enzyme Inhib Med Chem; 2020 Dec; 35(1):639-649. PubMed ID: 32048531 [TBL] [Abstract][Full Text] [Related]
10. Structural studies on the co-chaperone Hop and its complexes with Hsp90. Onuoha SC; Coulstock ET; Grossmann JG; Jackson SE J Mol Biol; 2008 Jun; 379(4):732-44. PubMed ID: 18485364 [TBL] [Abstract][Full Text] [Related]
15. Structure and mechanism of the Hsp90 molecular chaperone machinery. Pearl LH; Prodromou C Annu Rev Biochem; 2006; 75():271-94. PubMed ID: 16756493 [TBL] [Abstract][Full Text] [Related]
16. Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90. Wegele H; Muschler P; Bunck M; Reinstein J; Buchner J J Biol Chem; 2003 Oct; 278(41):39303-10. PubMed ID: 12890674 [TBL] [Abstract][Full Text] [Related]
17. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins. McLaughlin SH; Sobott F; Yao ZP; Zhang W; Nielsen PR; Grossmann JG; Laue ED; Robinson CV; Jackson SE J Mol Biol; 2006 Feb; 356(3):746-58. PubMed ID: 16403413 [TBL] [Abstract][Full Text] [Related]