Study of the role of checkpoint proteins LMHUS1 and LMRAD9 in Leishmania genome plasticity (2015)
- Authors:
- Autor USP: TOSI, LUIZ RICARDO ORSINI - FMRP
- Unidade: FMRP
- Subjects: LEISHMANIA; AMPLIFICAÇÃO DE GENES
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Abstracts
- Conference titles: Annual Meeting of the Brazilian Society of Protozoology
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ABNT
OBONAGA GOMEZ, R. e DAMASCENO, J. D. e TOSI, Luíz Ricardo Orsini. Study of the role of checkpoint proteins LMHUS1 and LMRAD9 in Leishmania genome plasticity. 2015, Anais.. Caxambu: SBPz, 2015. . Acesso em: 24 abr. 2024. -
APA
Obonaga Gomez, R., Damasceno, J. D., & Tosi, L. R. O. (2015). Study of the role of checkpoint proteins LMHUS1 and LMRAD9 in Leishmania genome plasticity. In Abstracts. Caxambu: SBPz. -
NLM
Obonaga Gomez R, Damasceno JD, Tosi LRO. Study of the role of checkpoint proteins LMHUS1 and LMRAD9 in Leishmania genome plasticity. Abstracts. 2015 ;[citado 2024 abr. 24 ] -
Vancouver
Obonaga Gomez R, Damasceno JD, Tosi LRO. Study of the role of checkpoint proteins LMHUS1 and LMRAD9 in Leishmania genome plasticity. Abstracts. 2015 ;[citado 2024 abr. 24 ] - The 9-1-1 complex is involved in cell cycle checkpoint and gene amplification modulation in the protozoan Leishmania
- Isolamento e clonagem da RAB/GTPase YPT em Leishmania SPP
- LmYPT overexpression abolishes HTBF-mediated terbinafine resistance in Leishmania major
- The YIP1 protein of Leishmania major and its role in terbinafine resistance
- Characterization of differences in the expression of epissomal genes in leishmania major and leishmania braziliensis
- The role of chromosome context in site-directed disruption of subtelometric targets of Leishimania major
- YIP1 of Leishmania major: characterization and possible role in terbinafine resistance
- Leishmania major nuclear protein LMHUS1 protects DNA from damage
- A transposon toolkit for gene transfer and mutagenesis in protozoan parasites
- LmHus1 is required in the DNA damage response in Leishmania major and forms a complex with an unusual Rad9 homologue
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