Endonuclease domain

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PAXgene Blood RNA Kit (PreAnalytiX, Hombrechtikon, Switzerland). (1)
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-- (1)
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Metabolite Name

Tricyclo[3.3.1.1(3,7)]decane-1-carboxamide, n-[2-(benzoylamino)-6-benzothiazolyl]- (1)
Timosaponin a-iii (1)
S-adenosyl-l-methionine (1)
Pcb 52 (1)
N-(tert-butyl)benzenesulfonamide (1)
N-(6-aminohexyl)-1-chloronaphthalene-5-sulfonamide (1)
N-(2-aminoethyl)-5-isoquinolinesulfonamide (1)
Arg-Pro-Arg (1)
6-bromoquinolin-2-ol (1)
4,7-dichloroquinoline (1)
4,5-epoxy-7z,10z,13z,16z,19z-docosapentaenoic acid, methyl ester (1)
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2-((4r)-4-((3r,5s,9s,10s,13r,14s,17r)-3-hydroxy-10,13-dimethyl-7-oxohexadecahydro-1h-cyclopenta[a]phenanthren-17-yl)pentanamido)ethane-1-sulfonic acid (1)
1h-1,2,3-triazole-1-octanamide, n-[1,1'-biphenyl]-2-yl-4-(3-pyridinyl)- (1)
1,2-benzenediamine, 4-methyl-n1-(3-phenylpropyl)- (1)
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Study type

Transcription profiling by array (758)
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Lab affiliation

Biocev-Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic (1)
CRUK/MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford, OX3 7DQ, UK (1)
Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Philipps-University Marburg, Marburg, Germany (1)
Department of Environmental and Biological Sciences, University of Tuscia, Viterbo, Italy (1)
Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried/Munich, Germany (1)
Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany (1)
EMBL, SCB, Heidelberg, Germany (1)
Faculty of Science, Charles University, 12800 Prague, Czech Republic (1)
IMB, Ackermannweg 4, 55128 Mainz (1)
Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France (1)
MOE Key Laboratory of Gene Function and Regulation and Guangzhou Key Laboratory of Healthy Aging Research, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China (1)
Max Planck Institute of Biochemistry (1)
Principle investigator (1)
State Key Laboratory of Microbial Technology, Microbiology and Biotechnology Institute, Shandong University (1)
University of Halle Department of Biochemistry Germany (1)
University of Liège, Genetics and Physiology of Microalgae, InBios/Phytosystems research unit, 4000 Liège, Belgium (1)
VIB Center for Medical Biotechnology / Department of Biomolecular Medicine, Ghent University (1)
Zentrum für Molekulare Biologie der University Heidelberg (ZMBH), Core Facility for mass spectrometry and proteomics, Im Neuenheimer Feld 282, 69120 Heid3elberg, Germany (1)

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The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans

Purpose: Pre-ribosomal RNA is cleaved at defined sites, but many endonucleases involved in 18S rRNA release are not known. We apply an in vivo cross-linking technique coupled with deep sequencing (CRAC) that captures transcriptome-wide interactions between a yeast candidate pre-rRNA endonuclease (Ut...

ORGANISM(S): Saccharomyces cerevisiae

2016-04-01 | E-GEOD-75991 | biostudies-arrayexpress

Endonuclease domain of non-LTR retrotransposons: loss-of-function mutants and modeling of the R2Bm endonuclease.

Not available

S-EPMC4838377 | biostudies-literature

Crystal structures of Lymphocytic choriomeningitis virus endonuclease domain complexed with diketo-acid ligands.

Not available

S-EPMC5947727 | biostudies-literature

The Cap-Snatching SFTSV Endonuclease Domain Is an Antiviral Target.

Not available

S-EPMC7214099 | biostudies-literature

The endonuclease domain of the LINE-1 ORF2 protein can tolerate multiple mutations.

Not available

S-EPMC4837594 | biostudies-literature

Structural characterization of a novel KH-domain containing plant chloroplast endonuclease.

Not available

S-EPMC6137056 | biostudies-literature

Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression.

Not available

S-EPMC2662267 | biostudies-literature

High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI.

Not available

S-EPMC137108 | biostudies-literature

Identification of proteins associated with the decapping complex and the endonuclease DNE1 in Arabidopsis

In this work, we used an unbiased approach coupling immunoprecipitations (IPs) and mass spectrometry to define the interactome of the decapping activator DCP1 and the decapping enzyme DCP2. In addition we unravel the interactome of the endonuclease DNE1 harboring an endoribonuclease domain of the NY...

ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress)

2021-11-16 | PXD020780 | Pride

The endonuclease domain of MutL interacts with the β sliding clamp.

Not available

S-EPMC3028594 | biostudies-literature

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