287 related articles for article (PubMed ID: 29959008)
1. 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]
2. 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]
3. Purification and characterization of a novel and conserved TPR-domain protein that binds both Hsp90 and Hsp70 and is expressed in all developmental stages of Leishmania major.
Araujo SA; Martins GH; Quel NG; Aragão AZB; Morea EGO; Borges JC; Houry WA; Cano MIN; Ramos CHI
Biochimie; 2021 Mar; 182():51-60. PubMed ID: 33421500
[TBL] [Abstract][Full Text] [Related]
4. Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity.
Angeletti PC; Walker D; Panganiban AT
Cell Stress Chaperones; 2002 Jul; 7(3):258-68. PubMed ID: 12482202
[TBL] [Abstract][Full Text] [Related]
5. In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70.
Prasad BD; Goel S; Krishna P
PLoS One; 2010 Sep; 5(9):e12761. PubMed ID: 20856808
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.
Liou ST; Wang C
Arch Biochem Biophys; 2005 Mar; 435(2):253-63. PubMed ID: 15708368
[TBL] [Abstract][Full Text] [Related]
8. Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering.
Seraphim TV; Silva KP; Dores-Silva PR; Barbosa LR; Borges JC
Int J Biol Macromol; 2017 Apr; 97():503-512. PubMed ID: 28104372
[TBL] [Abstract][Full Text] [Related]
9. Structural and functional studies of Leishmania braziliensis Hsp90.
Silva KP; Seraphim TV; Borges JC
Biochim Biophys Acta; 2013 Jan; 1834(1):351-61. PubMed ID: 22910377
[TBL] [Abstract][Full Text] [Related]
10. Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.
Carrigan PE; Sikkink LA; Smith DF; Ramirez-Alvarado M
Protein Sci; 2006 Mar; 15(3):522-32. PubMed ID: 16452615
[TBL] [Abstract][Full Text] [Related]
11. Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
Assimon VA; Southworth DR; Gestwicki JE
Biochemistry; 2015 Dec; 54(48):7120-31. PubMed ID: 26565746
[TBL] [Abstract][Full Text] [Related]
12. The co-chaperone SGT of Leishmania donovani is essential for the parasite's viability.
Ommen G; Chrobak M; Clos J
Cell Stress Chaperones; 2010 Jul; 15(4):443-55. PubMed ID: 19953351
[TBL] [Abstract][Full Text] [Related]
13. Low resolution structural characterization of the Hsp70-interacting protein - Hip - from Leishmania braziliensis emphasizes its high asymmetry.
Dores-Silva PR; Silva ER; Gomes FE; Silva KP; Barbosa LR; Borges JC
Arch Biochem Biophys; 2012 Apr; 520(2):88-98. PubMed ID: 22387434
[TBL] [Abstract][Full Text] [Related]
14. The assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complex.
Trcka F; Durech M; Man P; Hernychova L; Muller P; Vojtesek B
J Biol Chem; 2014 Apr; 289(14):9887-901. PubMed ID: 24567332
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Revealing the interaction mode of the highly flexible Sorghum bicolor Hsp70/Hsp90 organizing protein (Hop): A conserved carboxylate clamp confers high affinity binding to Hsp90.
Adão R; Zanphorlin LM; Lima TB; Sriranganadane D; Dahlström KM; Pinheiro GMS; Gozzo FC; Barbosa LRS; Ramos CHI
J Proteomics; 2019 Jan; 191():191-201. PubMed ID: 29425735
[TBL] [Abstract][Full Text] [Related]
17. The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90.
Gaiser AM; Brandt F; Richter K
J Mol Biol; 2009 Aug; 391(3):621-34. PubMed ID: 19559711
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery.
Chen S; Smith DF
J Biol Chem; 1998 Dec; 273(52):35194-200. PubMed ID: 9857057
[TBL] [Abstract][Full Text] [Related]
20. Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.
Graf C; Stankiewicz M; Nikolay R; Mayer MP
Biochemistry; 2010 Mar; 49(10):2121-9. PubMed ID: 20146531
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]