Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Jobst, Greeve"'
Autor:
Dominik P, Modest, Uwe M, Martens, Jorge, Riera-Knorrenschild, Jobst, Greeve, Axel, Florschütz, Swen, Wessendorf, Thomas, Ettrich, Stephan, Kanzler, Dominik, Nörenberg, Jens, Ricke, Max, Seidensticker, Swantje, Held, Petra, Buechner-Steudel, Jens, Atzpodien, Volker, Heinemann, Thomas, Seufferlein, Andrea, Tannapfel, Anke C, Reinacher-Schick, Michael, Geissler
Publikováno v:
Journal of clinical oncology : official journal of the American Society of Clinical Oncology. 37(35)
This trial investigated the addition of panitumumab to triplet chemotherapy with fluorouracil/folinic acid, oxaliplatin, and irinotecan (FOLFOXIRI) in a two-to-one randomized, controlled, open-label, phase II trial in patients with untreatedThe prima
Publikováno v:
Molecular Immunology. 43:295-307
Activation-induced cytidine deaminase (AID) is indispensable for immunoglobulin maturation by somatic hypermutations and class switch recombination and is supposed to deaminate cytidines in DNA, while its homolog APOBEC-1 edits apolipoprotein (apo) B
Publikováno v:
Nucleic Acids Research
Linker, Katrin; Pautz, Andrea; Fechir, Marcel; Hubrich, Thomas; Greeve, Jobst; Kleinert, Hartmut (2005). Involvement of KSRP in the post-transcriptional regulation of human iNOS expression–complex interplay of KSRP with TTP and HuR. Nucleic acids research, 33(15), pp. 4813-4827. Oxford University Press 10.1093/nar/gki797
Linker, Katrin; Pautz, Andrea; Fechir, Marcel; Hubrich, Thomas; Greeve, Jobst; Kleinert, Hartmut (2005). Involvement of KSRP in the post-transcriptional regulation of human iNOS expression–complex interplay of KSRP with TTP and HuR. Nucleic acids research, 33(15), pp. 4813-4827. Oxford University Press 10.1093/nar/gki797
We purified the KH-type splicing regulatory protein (KSRP) as a protein interacting with the 3'-untranslated region (3'-UTR) of the human inducible nitric oxide (iNOS) mRNA. Immunodepletion of KSRP enhanced iNOS 3'-UTR RNA stability in in vitro-degra
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1577:384-394
Editing of apolipoprotein (apo) B mRNA in liver limits the plasma LDL levels in horses, dogs, rats or mice. Species such as man or rabbit do not edit the hepatic apo B mRNA and are therefore susceptible to atherosclerosis and coronary artery disease
Publikováno v:
Molecular Immunology. 43:1924-1926
Publikováno v:
Nucleic Acids Research. 19:1197-1201
Human apolipoprotein (apo) B mRNA is edited in a tissue specific reaction, to convert glutamine codon 2153 (CAA) to a stop translation codon. The RNA editing product templates and hybridises as uridine, but the chemical nature of this reaction and th
Publikováno v:
Nucleic Acids Research. 19:3569-3576
Intestinal apolipoprotein B mRNA is edited at nucleotide 6666 by a C to U transition resulting in a translational stop codon. The enzymatic properties of the editing activity were characterised in vitro using rat enterocyte cytosolic extract. The edi
Autor:
Marianne Bonvin, Jobst Greeve
Publikováno v:
Current opinion in infectious diseases. 21(3)
APOBEC3 editing enzymes inhibit retroviruses by cytidine deamination in minus-strand cDNA, leading to G to A hypermutated proviruses, and by less well characterized inhibition of retroviral replication independently of catalysis. This review focuses
Autor:
Daniel Candinas, Daniel Inderbitzin, Simon Wain-Hobson, Jobst Greeve, Isabell Greeve, Jean-Pierre Vartanian, Adrian Keogh, François Achermann, Marianne Bonvin, Deborah Stroka, Peter Sommer
Publikováno v:
Hepatology
Hepatology, Wiley-Blackwell, 2006, 43 (6), pp.1364-74. ⟨10.1002/hep.21187⟩
Hepatology, 2006, 43 (6), pp.1364-74. ⟨10.1002/hep.21187⟩
Hepatology, Wiley-Blackwell, 2006, 43 (6), pp.1364-74. ⟨10.1002/hep.21187⟩
Hepatology, 2006, 43 (6), pp.1364-74. ⟨10.1002/hep.21187⟩
International audience; Hypermutations in hepatitis B virus (HBV) DNA by APOBEC3 cytidine deaminases have been detected in vitro and in vivo, and APOBEC3G (A3G) and APOBEC3F (A3F) have been shown to inhibit the replication of HBV in vitro, but the pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7d5c8419aae9525490522a1d6be450
https://hal-riip.archives-ouvertes.fr/pasteur-00683855
https://hal-riip.archives-ouvertes.fr/pasteur-00683855
Publikováno v:
Biochimica et biophysica acta. 1680(1)
Editing of apolipoprotein (apo) B mRNA is mediated by an enzyme-complex that consists of the catalytic cytidine deaminase APOBEC-1 and the mRNA binding protein APOBEC-1 complementation factor or APOBEC-1 stimulating protein (ACF/ASP). Here we describ