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Dataset.

Supplemental Material Fine-tuning of the Hsc70-based human protein disaggregase machinery by the distinctive C-terminal extension of Apg2

Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331446
Digital.CSIC. Repositorio Institucional del CSIC
  • Cabrera, Yovana
  • Bernardo-Seisdedos, Ganeko
  • Dublang, Leire
  • Albesa-Jové, David
  • Orozco, Natalia
  • Viguera, Ana Rosa
  • Millet, Óscar
  • Muga, Arturo
  • Moro, Fernando
8 pages. -- Table 1. SAXS data collection and processing. -- Figure S1: Binding of nucleotides does not promote significant conformational changes in Apg2 and Apg2C tertiary structure. -- Figure S2: Characterization of the interaction of Apg2ΔC with Hsc70 in the absence of nucleotides by SPR. -- Fig. S3: NMR chemical shift perturbation analysis. -- Fig- S4: Apg2IDR interacts with Hsc70 with 2-fold reduced affinity in the presence of nucleotides., Peer reviewed
 
DOI: http://hdl.handle.net/10261/331446
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331446

HANDLE: http://hdl.handle.net/10261/331446
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331446
 
Ver en: http://hdl.handle.net/10261/331446
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331446
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Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331446
Dataset. 2022

SUPPLEMENTAL MATERIAL FINE-TUNING OF THE HSC70-BASED HUMAN PROTEIN DISAGGREGASE MACHINERY BY THE DISTINCTIVE C-TERMINAL EXTENSION OF APG2

Digital.CSIC. Repositorio Institucional del CSIC
  • Cabrera, Yovana
  • Bernardo-Seisdedos, Ganeko
  • Dublang, Leire
  • Albesa-Jové, David
  • Orozco, Natalia
  • Viguera, Ana Rosa
  • Millet, Óscar
  • Muga, Arturo
  • Moro, Fernando
8 pages. -- Table 1. SAXS data collection and processing. -- Figure S1: Binding of nucleotides does not promote significant conformational changes in Apg2 and Apg2C tertiary structure. -- Figure S2: Characterization of the interaction of Apg2ΔC with Hsc70 in the absence of nucleotides by SPR. -- Fig. S3: NMR chemical shift perturbation analysis. -- Fig- S4: Apg2IDR interacts with Hsc70 with 2-fold reduced affinity in the presence of nucleotides., Peer reviewed

HANDLE: http://hdl.handle.net/10261/331446


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