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  1. Artikel ; Online: Myogenic vasoconstriction requires G

    Chennupati, Ramesh / Wirth, Angela / Favre, Julie / Li, Rui / Bonnavion, Rémy / Jin, Young-June / Wietelmann, Astrid / Schweda, Frank / Wettschureck, Nina / Henrion, Daniel / Offermanns, Stefan

    eLife

    2019  Band 8

    Abstract: Myogenic vasoconstriction is an autoregulatory function of small arteries. Recently, G-protein ... that small arteries from mice with smooth muscle-specific loss of G ...

    Abstract Myogenic vasoconstriction is an autoregulatory function of small arteries. Recently, G-protein-coupled receptors have been involved in myogenic vasoconstriction, but the downstream signalling mechanisms and the in-vivo-function of this myogenic autoregulation are poorly understood. Here, we show that small arteries from mice with smooth muscle-specific loss of G
    Mesh-Begriff(e) Animals ; GTP-Binding Protein alpha Subunits, G12-G13/deficiency ; GTP-Binding Protein alpha Subunits, G12-G13/metabolism ; Mice, Inbred C57BL ; Rho Guanine Nucleotide Exchange Factors/deficiency ; Rho Guanine Nucleotide Exchange Factors/metabolism ; Vascular Resistance ; Vasoconstriction
    Chemische Substanzen Arhgef12 protein, mouse ; Rho Guanine Nucleotide Exchange Factors ; GTP-Binding Protein alpha Subunits, G12-G13 (EC 3.6.5.1)
    Sprache Englisch
    Erscheinungsdatum 2019-09-24
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.49374
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Centrosomal AKAP350 modulates the G

    Mattaloni, Stella M / Ferretti, Anabela C / Tonucci, Facundo M / Favre, Cristián / Goldenring, James R / Larocca, M Cecilia

    Cellular logistics

    2013  Band 3, Heft 1, Seite(n) e26331

    Abstract: ... in the progression of the cell cycle. Our results showed that interference with AKAP350 expression inhibits G ...

    Abstract AKAP350 (AKAP450/AKAP9/CG-NAP) is an A-kinase anchoring protein, which recruits multiple signaling proteins to the Golgi apparatus and the centrosomes. Several proteins recruited to the centrosomes by this scaffold participate in the regulation of the cell cycle. Previous studies indicated that AKAP350 participates in centrosome duplication. In the present study we specifically assessed the role of AKAP350 in the progression of the cell cycle. Our results showed that interference with AKAP350 expression inhibits G
    Sprache Englisch
    Erscheinungsdatum 2013-09-12
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2682440-1
    ISSN 2159-2799 ; 2159-2780
    ISSN (online) 2159-2799
    ISSN 2159-2780
    DOI 10.4161/cl.26331
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: hnRNP A1-mediated translational regulation of the G quadruplex-containing RON receptor tyrosine kinase mRNA linked to tumor progression.

    Cammas, Anne / Lacroix-Triki, Magali / Pierredon, Sandra / Le Bras, Morgane / Iacovoni, Jason S / Teulade-Fichou, Marie-Paule / Favre, Gilles / Roché, Henri / Filleron, Thomas / Millevoi, Stefania / Vagner, Stéphan

    Oncotarget

    2016  Band 7, Heft 13, Seite(n) 16793–16805

    Abstract: ... untranslated region of the RON mRNA and activates its translation through G-quadruplex RNA secondary structures ...

    Abstract The expression and role of RNA binding proteins (RBPs) controlling mRNA translation during tumor progression remains largely uncharacterized. Analysis by immunohistochemistry of the expression of hnRNP A1, hnRNPH, RBM9/FOX2, SRSF1/ASF/SF2, SRSF2/SC35, SRSF3/SRp20, SRSF7/9G8 in breast tumors shows that the expression of hnRNP A1, but not the other tested RBPs, is associated with metastatic relapse. Strikingly, hnRNP A1, a nuclear splicing regulator, is also present in the cytoplasm of tumor cells of a subset of patients displaying exceedingly worse prognosis. Expression of a cytoplasmic mutant of hnRNP A1 leads to increased translation of the mRNA encoding the tyrosine kinase receptor RON/MTS1R, known for its function in tumor dissemination, and increases cell migration in vitro. hnRNP A1 directly binds to the 5' untranslated region of the RON mRNA and activates its translation through G-quadruplex RNA secondary structures. The correlation between hnRNP A1 and RON tumoral expression suggests that these findings hold clinical relevance.
    Mesh-Begriff(e) Breast Neoplasms/genetics ; Breast Neoplasms/mortality ; Breast Neoplasms/pathology ; Disease Progression ; Female ; Gene Expression Regulation, Neoplastic/physiology ; Heterogeneous Nuclear Ribonucleoprotein A1/genetics ; Heterogeneous Nuclear Ribonucleoprotein A1/metabolism ; Humans ; Kaplan-Meier Estimate ; Protein Biosynthesis/physiology ; RNA, Messenger ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor Protein-Tyrosine Kinases/metabolism
    Chemische Substanzen Heterogeneous Nuclear Ribonucleoprotein A1 ; RNA, Messenger ; hnRNPA1 protein, human ; RON protein (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1)
    Sprache Englisch
    Erscheinungsdatum 2016-02-29
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2560162-3
    ISSN 1949-2553 ; 1949-2553
    ISSN (online) 1949-2553
    ISSN 1949-2553
    DOI 10.18632/oncotarget.7589
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: The novel inhibitor of the heterotrimeric G-protein complex, BIM-46187, elicits anti-hyperalgesic properties and synergizes with morphine.

    Favre-Guilmard, Christine / Zeroual-Hider, Hamida / Soulard, Chantal / Touvay, Caroline / Chabrier, Pierre-Etienne / Prevost, Grégoire / Auguet, Michel

    European journal of pharmacology

    2008  Band 594, Heft 1-3, Seite(n) 70–76

    Abstract: ... 1,2a]-pyrazine dimer, hydrochloride) is an inhibitor of the heterotrimeric G-protein complex ... signalling. Since many mediators of pain act through G-protein coupled receptors, the anti-hyperalgesic ... used in pain management and act through specific G-protein-coupled receptors, the effects of BIM-46187 ...

    Abstract BIM-46187 (7-[2-amino-1-oxo-3-thio-propyl]-8-cyclohexylmethyl-2-phenyl-5,6,7,8-tetrahydro-imidazo-[1,2a]-pyrazine dimer, hydrochloride) is an inhibitor of the heterotrimeric G-protein complex signalling. Since many mediators of pain act through G-protein coupled receptors, the anti-hyperalgesic effects of BIM-46187 were assessed on experimental models of pain. In addition since opioids are widely used in pain management and act through specific G-protein-coupled receptors, the effects of BIM-46187 on the analgesic properties of morphine have also been investigated. BIM-46187 elicited a dose dependent analgesic effect in the models of carrageenan-induced hyperalgesia (0.1-1 mg/kg; i.v.) and chronic constriction injury (0.3-3 mg/kg; i.v.) in rats. BIM-46187, however, up to 10 mg/kg did not modify the paw oedema induced by carrageenan excluding an anti-inflammatory effect. In addition, at these doses, the compound was not sedative as shown by the lack of effect on the motor performance in the rotarod test. The combination of BIM-46187 and morphine (ratio 1/1) resulted in an unexpected synergistic effect in the model of carrageenan-induced hyperalgesia and in the chronic constriction injury model in rats when evaluated by isobolographic analysis. This synergy allowed a reduction of at least 20 fold in the dose of each compound. Conversely, the drug combination did not increase the side effects of morphine as assessed in the rotarod test. In conclusion, BIM-46187 elicits a potent anti-hyperalgesic effect and strongly synergizes with morphine. This work highlights the role of heterotrimeric G-protein complexes in pain and supports further investigations of the use of BIM-46187 alone, or in combination with low doses of morphine, in the management of pain.
    Mesh-Begriff(e) Analgesics, Non-Narcotic/pharmacology ; Analgesics, Opioid/pharmacology ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Carrageenan ; Constriction, Pathologic/pathology ; Cyclohexanes/pharmacology ; Drug Synergism ; Edema/chemically induced ; Edema/pathology ; Heterotrimeric GTP-Binding Proteins/antagonists & inhibitors ; Hyperalgesia/chemically induced ; Hyperalgesia/drug therapy ; Male ; Morphine/pharmacology ; Pain Measurement/drug effects ; Peripheral Nervous System Diseases/chemically induced ; Peripheral Nervous System Diseases/pathology ; Peripheral Nervous System Diseases/psychology ; Psychomotor Performance/drug effects ; Pyrazines/pharmacology ; Rats ; Rats, Sprague-Dawley
    Chemische Substanzen 7-(2-amino-1-oxo-3-thio-propyl)-8-cyclohexylmethyl-2-phenyl-5,6,7,8-tetrahydro-imidazo-(1,2a)-pyrazine dimer, hydrochloride ; Analgesics, Non-Narcotic ; Analgesics, Opioid ; Anti-Inflammatory Agents, Non-Steroidal ; Cyclohexanes ; Pyrazines ; Morphine (76I7G6D29C) ; Carrageenan (9000-07-1) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
    Sprache Englisch
    Erscheinungsdatum 2008-10-10
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 80121-5
    ISSN 1879-0712 ; 0014-2999
    ISSN (online) 1879-0712
    ISSN 0014-2999
    DOI 10.1016/j.ejphar.2008.07.016
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Human replication protein A unfolds telomeric G-quadruplexes.

    Salas, Tonatiuh Romero / Petruseva, Irina / Lavrik, Olga / Bourdoncle, Anne / Mergny, Jean-Louis / Favre, Alain / Saintomé, Carole

    Nucleic acids research

    2006  Band 34, Heft 17, Seite(n) 4857–4865

    Abstract: G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation ... near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures ... fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded ...

    Abstract G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation during S phase. It has been suggested that the replication protein A (RPA) could unwind and maintain single-stranded DNA in a state amenable to the binding of telomeric components. We show here that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence. Analyses by native gel electrophoresis, cross-linking and fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded. In addition, quadruplex opening by hRPA is much faster than observed with the complementary DNA, demonstrating that this protein efficiently unfolds G-quartets. A two-step mechanism accounting for the binding of hRPA to G-quadruplexes is proposed. These data point to the involvement of hRPA in regulation of telomere maintenance.
    Mesh-Begriff(e) DNA/chemistry ; DNA/metabolism ; Fluorescence Resonance Energy Transfer ; G-Quadruplexes ; Guanine/chemistry ; Humans ; Models, Biological ; Nucleic Acid Conformation ; Oligonucleotides/chemistry ; Replication Protein A/metabolism ; Telomere/chemistry
    Chemische Substanzen Oligonucleotides ; Replication Protein A ; Guanine (5Z93L87A1R) ; DNA (9007-49-2)
    Sprache Englisch
    Erscheinungsdatum 2006
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205588-5
    ISSN 1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
    ISSN (online) 1362-4962 ; 1746-8272
    ISSN 0305-1048 ; 0261-3166
    DOI 10.1093/nar/gkl564
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.

    Skillman, Kristen M / Daher, Wassim / Ma, Christopher I / Soldati-Favre, Dominique / Sibley, L David

    Biochemistry

    2012  Band 51, Heft 12, Seite(n) 2486–2495

    Abstract: Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments ... ...

    Abstract Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments required for motility relies on a small repertoire of actin-binding proteins. Previous studies have shown that apicomplexan formins and profilin exhibit canonical functions on heterologous actins from higher eukaryotes; however, their biochemical properties on parasite actins are unknown. We therefore analyzed the impact of T. gondii profilin (TgPRF) and FH1-FH2 domains of two formin isoforms in T. gondii (TgFRM1 and TgFRM2) on the polymerization of T. gondii actin (TgACTI). Our findings based on in vitro assays demonstrate that TgFRM1-FH1-FH2 and TgFRM2-FH1-FH2 dramatically enhanced TgACTI polymerization in the absence of profilin, making them the sole protein factors known to initiate polymerization of this normally unstable actin. In addition, T. gondii formin domains were shown to both initiate polymerization and induce bundling of TgACTI filaments; however, they did not rely on TgPRF for these activities. In contrast, TgPRF sequestered TgACTI monomers, thus inhibiting polymerization even in the presence of formins. Collectively, these findings provide insight into the unusual control mechanisms of actin dynamics within the parasite.
    Mesh-Begriff(e) Actin Cytoskeleton/metabolism ; Actins/chemistry ; Actins/metabolism ; Nucleotides/metabolism ; Profilins/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Protozoan Proteins/metabolism ; Toxoplasma/cytology ; Toxoplasma/metabolism
    Chemische Substanzen Actins ; Nucleotides ; Profilins ; Protozoan Proteins
    Sprache Englisch
    Erscheinungsdatum 2012-03-16
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi201704y
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel: Human replication protein A unfolds telomeric G-quadruplexes

    Salas, Tonatiuh Romero / Petruseva, Irina / Lavrik, Olga / Bourdoncle, Anne / Mergny, Jean-Louis / Favre, Alain / Saintomé, Carole

    Nucleic acids research. 2006 Oct., v. 34, no. 17

    2006  

    Abstract: G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation ... near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures ... fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded ...

    Abstract G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation during S phase. It has been suggested that the replication protein A (RPA) could unwind and maintain single-stranded DNA in a state amenable to the binding of telomeric components. We show here that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence. Analyses by native gel electrophoresis, cross-linking and fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded. In addition, quadruplex opening by hRPA is much faster than observed with the complementary DNA, demonstrating that this protein efficiently unfolds G-quartets. A two-step mechanism accounting for the binding of hRPA to G-quadruplexes is proposed. These data point to the involvement of hRPA in regulation of telomere maintenance.
    Schlagwörter complementary DNA ; crosslinking ; energy transfer ; fluorescence ; gel electrophoresis ; humans ; interphase ; single-stranded DNA ; telomerase ; telomeres
    Sprache Englisch
    Erscheinungsverlauf 2006-10
    Umfang p. 4857-4865.
    Dokumenttyp Artikel
    ZDB-ID 186809-3
    ISSN 0301-5610 ; 0305-1048
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkl564
    Datenquelle NAL Katalog (AGRICOLA)

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  8. Artikel: Toxoplasma gondii Profilin Acts Primarily To Sequester G-Actin While Formins Efficiently Nucleate Actin Filament Formation in Vitro

    Skillman, Kristen M / Daher Wassim / Ma Christopher I / Soldati-Favre Dominique / Sibley L. David

    Biochemistry. 2012 Mar. 27, v. 51, no. 12

    2012  

    Abstract: Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments ... ...

    Abstract Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments required for motility relies on a small repertoire of actin-binding proteins. Previous studies have shown that apicomplexan formins and profilin exhibit canonical functions on heterologous actins from higher eukaryotes; however, their biochemical properties on parasite actins are unknown. We therefore analyzed the impact of T. gondii profilin (TgPRF) and FH1-FH2 domains of two formin isoforms in T. gondii (TgFRM1 and TgFRM2) on the polymerization of T. gondii actin (TgACTI). Our findings based on in vitro assays demonstrate that TgFRM1-FH1-FH2 and TgFRM2-FH1-FH2 dramatically enhanced TgACTI polymerization in the absence of profilin, making them the sole protein factors known to initiate polymerization of this normally unstable actin. In addition, T. gondii formin domains were shown to both initiate polymerization and induce bundling of TgACTI filaments; however, they did not rely on TgPRF for these activities. In contrast, TgPRF sequestered TgACTI monomers, thus inhibiting polymerization even in the presence of formins. Collectively, these findings provide insight into the unusual control mechanisms of actin dynamics within the parasite.
    Schlagwörter Toxoplasma gondii ; actin ; eukaryotic cells ; in vitro studies ; microfilaments ; parasites ; polymerization
    Sprache Englisch
    Erscheinungsverlauf 2012-0327
    Umfang p. 2486-2495.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi201704y
    Datenquelle NAL Katalog (AGRICOLA)

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  9. Buch ; Dissertation / Habilitation: Contribution à l'étude du jaune d'indigo 3 G Ciba

    Favre, Francois

    1943  

    Verfasserangabe François Favre
    Umfang 54 S.
    Verlag Fragnière
    Erscheinungsort Fribourg
    Erscheinungsland Schweiz
    Dokumenttyp Buch ; Dissertation / Habilitation
    Dissertation / Habilitation Freiburg [Schweiz], Naturwiss. Diss
    HBZ-ID HT008521591
    Datenquelle Katalog ZB MED Medizin, Gesundheit

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  10. Artikel: Prognostic relevance of surface markers in adult de novo acute myeloblastic leukemias: a prospective study of the Groupe d'Etude Immunologique des Leucémies (G.E.I.L.).

    Casasnovas, R O / Solary, E / Campos, L / Maynadie, M / Favre, M / Bremend, J L / Garand, R / Béné, M C / Faure, G

    Leukemia & lymphoma

    1994  Band 13 Suppl 1, Seite(n) 7–10

    Mesh-Begriff(e) Adolescent ; Adult ; Aged ; Antigens, Surface/analysis ; Humans ; Immunophenotyping ; Leukemia, Myeloid, Acute/immunology ; Middle Aged ; Prognosis ; Prospective Studies
    Chemische Substanzen Antigens, Surface
    Sprache Englisch
    Erscheinungsdatum 1994
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Multicenter Study ; Research Support, Non-U.S. Gov't
    ZDB-ID 1042374-6
    ISSN 1029-2403 ; 1042-8194
    ISSN (online) 1029-2403
    ISSN 1042-8194
    DOI 10.3109/10428199409052665
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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