Functional compartmentalization of Rad9 and Hus1 reveals diverse assembly of the 9-1-1 complex components during the DNA damage response in Leishmania
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Title
Functional compartmentalization of Rad9 and Hus1 reveals diverse assembly of the 9-1-1 complex components during the DNA damage response in Leishmania
Authors
Keywords
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Journal
MOLECULAR MICROBIOLOGY
Volume 101, Issue 6, Pages 1054-1068
Publisher
Wiley
Online
2016-06-16
DOI
10.1111/mmi.13441
References
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Note: Only part of the references are listed.- Association of the Rad9–Rad1–Hus1 checkpoint clamp with MYH DNA glycosylase and DNA
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- The Phyre2 web portal for protein modeling, prediction and analysis
- (2015) Lawrence A Kelley et al. Nature Protocols
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- (2015) Marie-Michelle Genois et al. NUCLEIC ACIDS RESEARCH
- The N-terminus of Mcm10 is important for interaction with the 9-1-1 clamp and in resistance to DNA damage
- (2014) Robert C. Alver et al. NUCLEIC ACIDS RESEARCH
- Genome-Wide Stochastic Adaptive DNA Amplification at Direct and Inverted DNA Repeats in the Parasite Leishmania
- (2014) Jean-Michel Ubeda et al. PLOS BIOLOGY
- Clamping down on mammalian meiosis
- (2013) Amy Lyndaker et al. CELL CYCLE
- LmHus1 is required for the DNA damage response inLeishmania majorand forms a complex with an unusual Rad9 homologue
- (2013) Jeziel D. Damasceno et al. MOLECULAR MICROBIOLOGY
- Conditional Inactivation of the DNA Damage Response Gene Hus1 in Mouse Testis Reveals Separable Roles for Components of the RAD9-RAD1-HUS1 Complex in Meiotic Chromosome Maintenance
- (2013) Amy M. Lyndaker et al. PLoS Genetics
- Rad9B responds to nucleolar stress through ATR and JNK signalling, and delays the G1-S transition
- (2012) A. J. Perez-Castro et al. JOURNAL OF CELL SCIENCE
- Heat induction of a novel Rad9 variant from a cryptic translation initiation site reduces mitotic commitment
- (2012) S. Janes et al. JOURNAL OF CELL SCIENCE
- Trypanosomal histone γH2A and the DNA damage response
- (2012) Lucy Glover et al. MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- Chromosome and gene copy number variation allow major structural change between species and strains of Leishmania
- (2011) M. B. Rogers et al. GENOME RESEARCH
- The Hus1 homologue of Leishmania major encodes a nuclear protein that participates in DNA damage response
- (2011) Vinicius S. Nunes et al. MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- DDK Phosphorylates Checkpoint Clamp Component Rad9 and Promotes Its Release from Damaged Chromatin
- (2010) Kanji Furuya et al. MOLECULAR CELL
- Trypanosome Prereplication Machinery Contains a Single Functional Orc1/Cdc6 Protein, Which Is Typical ofArchaea
- (2009) Patrícia Diogo de Melo Godoy et al. EUKARYOTIC CELL
- Crystal Structure of the Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex—Implications for Clamp Loading and Regulation
- (2009) Andrew S. Doré et al. MOLECULAR CELL
- Methylene tetrahydrofolate dehydrogenase/cyclohydrolase and the synthesis of 10-CHO-THF are essential inLeishmania major
- (2009) Silvane M. F. Murta et al. MOLECULAR MICROBIOLOGY
- ATR and Rad17 collaborate in modulating Rad9 localisation at sites of DNA damage
- (2008) A. L. Medhurst et al. JOURNAL OF CELL SCIENCE
- The Basic Cleft of RPA70N Binds Multiple Checkpoint Proteins, Including RAD9, To Regulate ATR Signaling
- (2008) X. Xu et al. MOLECULAR AND CELLULAR BIOLOGY
- -H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin
- (2008) A. Kinner et al. NUCLEIC ACIDS RESEARCH
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