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Selected Publication:
SHR Neuro Cancer Cardio Lipid Metab Microb
Toro, MA; Sánchez-Murcia, PA; Moreno, D; Ruiz-Santaquiteria, M; Alzate, JF; Negri, A; Camarasa, MJ; Gago, F; Velázquez, S; Jiménez-Ruiz, A.
Probing the dimerization interface of Leishmania infantum trypanothione reductase with site-directed mutagenesis and short peptides.
Chembiochem. 2013; 14(10):1212-1217
Doi: 10.1002/cbic.201200744
Web of Science
PubMed
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- Co-authors Med Uni Graz
- Sánchez Murcia Pedro Alejandro
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- Abstract:
- Binding at the interface: We tested the inhibitory activity of a set of peptide sequences derived from an α-helix of the dimeric trypanothione reductase from Leishmania infantum. Replacement of a glutamic acid residue with a lysine promoted monomer dissociation and enzyme inhibition. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Sequence -
- Leishmania infantum - enzymology
- Leishmania infantum - genetics
- Leishmania infantum - metabolism
- Models, Molecular -
- Molecular Sequence Data -
- Mutagenesis, Site-Directed -
- NADH, NADPH Oxidoreductases - chemistry
- NADH, NADPH Oxidoreductases - genetics
- NADH, NADPH Oxidoreductases - metabolism
- Peptides - chemistry
- Peptides - genetics
- Peptides - metabolism
- Protein Multimerization -
- Find related publications in this database (Keywords)
- dimer quantification assay
- enzyme models
- Leishmania
- protein-protein interactions
- trypanothione reductase