LIVIVO - Search results -

Search results

Result 1 - 10 of total 17

Search options

Article ; Online: The Dual Targeting of FcRn and FcγRs

Monnet, Céline / Jacque, Emilie / de Romeuf, Christophe / Fontayne, Alexandre / Abache, Toufik / Fournier, Nathalie / Dupont, Gilles / Derache, Delphine / Engrand, Anais / Bauduin, Aurélie / Terrier, Aurélie / Seifert, Alexander / Beghin, Cécile / Longue, Alain / Masiello, Nicholas / Danino, Laetitia / Nogre, Michel / Raia, Anais / Dhainaut, Frederic /

Fauconnier, Louis / Togbe, Dieudonnée / Reitinger, Carmen / Nimmerjahn, Falk / Stevens, Wil / Chtourou, Sami / Mondon, Philippe

Frontiers in immunology

2021 Volume 12, Page(s) 728322

Abstract: Novel molecules that directly target the neonatal Fc receptor (FcRn) and/or Fc gamma receptors (FcγRs) are emerging as promising treatments for immunoglobulin G (IgG)-dependent autoimmune pathologies. Mutated Fc regions and monoclonal antibodies that ... ...

Abstract	Novel molecules that directly target the neonatal Fc receptor (FcRn) and/or Fc gamma receptors (FcγRs) are emerging as promising treatments for immunoglobulin G (IgG)-dependent autoimmune pathologies. Mutated Fc regions and monoclonal antibodies that target FcRn are currently in clinical development and hold promise for reducing the levels of circulating IgG. Additionally, engineered structures containing multimeric Fc regions allow the dual targeting of FcRn and FcγRs; however, their tolerance needs to first be validated in phase I clinical studies. Here, for the first time, we have developed a modified monomeric recombinant Fc optimized for binding to all FcRns and FcγRs without the drawback of possible tolerance associated with FcγR cross-linking. A rational approach using Fc engineering allowed the selection of LFBD192, an Fc with a combination of six mutations that exhibits improved binding to human FcRn and FcγR as well as mouse FcRn and FcγRIV. The potency of LFBD192 was compared with that of intravenous immunoglobulin (IVIg), an FcRn blocker (Fc-MST-HN), and a trimeric Fc that blocks FcRn and/or immune complex-mediated cell activation through FcγR without triggering an immune reaction in several
MeSH term(s)	Animals ; Antirheumatic Agents/metabolism ; Antirheumatic Agents/pharmacology ; Arthritis, Experimental/genetics ; Arthritis, Experimental/immunology ; Arthritis, Experimental/metabolism ; Arthritis, Experimental/prevention & control ; Autoimmunity/drug effects ; Binding, Competitive ; Complement C5a/metabolism ; Female ; Histocompatibility Antigens Class I/genetics ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin Fc Fragments/pharmacology ; Interleukin-2/metabolism ; Jurkat Cells ; Kinetics ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Phagocytosis/drug effects ; Platelet Aggregation/drug effects ; Protein Binding ; Protein Engineering ; Receptors, Fc/antagonists & inhibitors ; Receptors, Fc/genetics ; Receptors, Fc/immunology ; Receptors, Fc/metabolism ; Receptors, IgG/antagonists & inhibitors ; Receptors, IgG/genetics ; Receptors, IgG/immunology ; Receptors, IgG/metabolism ; Secretory Pathway ; Signal Transduction ; THP-1 Cells ; Mice
Chemical Substances	Antirheumatic Agents ; Histocompatibility Antigens Class I ; IL2 protein, human ; Immunoglobulin Fc Fragments ; Interleukin-2 ; Receptors, Fc ; Receptors, IgG ; Complement C5a (80295-54-1) ; Fc receptor, neonatal (TW3XAW0RCY)
Language	English
Publishing date	2021-08-26
Publishing country	Switzerland
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.728322
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article: Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector Functions.

Monnet, Céline / Jorieux, Sylvie / Urbain, Rémi / Fournier, Nathalie / Bouayadi, Khalil / De Romeuf, Christophe / Behrens, Christian K / Fontayne, Alexandre / Mondon, Philippe

Frontiers in immunology

2015 Volume 6, Page(s) 39

Abstract: Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which ... ...

Abstract	Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which among other functions, protects IgG from catabolism. FcRn binds the Fc domain of IgG at an acidic pH ensuring that endocytosed IgG will not be degraded in lysosomal compartments and will then be released into the bloodstream. Consistent with this mechanism of action, several Fc-engineered IgG with increased FcRn affinity and conserved pH dependency were designed and resulted in longer half-life in vivo in human FcRn-transgenic mice (hFcRn), cynomolgus monkeys, and recently in healthy humans. These IgG variants were usually obtained by in silico approaches or directed mutagenesis in the FcRn-binding site. Using random mutagenesis, combined with a pH-dependent phage display selection process, we isolated IgG variants with improved FcRn-binding, which exhibited longer in vivo half-life in hFcRn mice. Interestingly, many mutations enhancing Fc/FcRn interaction were located at a distance from the FcRn-binding site validating our random molecular approach. Directed mutagenesis was then applied to generate new variants to further characterize our IgG variants and the effect of the mutations selected. Since these mutations are distributed over the whole Fc sequence, binding to other Fc effectors, such as complement C1q and FcγRs, was dramatically modified, even by mutations distant from these effectors' binding sites. Hence, we obtained numerous IgG variants with increased FcRn-binding and different binding patterns to other Fc effectors, including variants without any effector function, providing distinct "fit-for-purpose" Fc molecules. We therefore provide evidence that half-life and effector functions should be optimized simultaneously as mutations can have unexpected effects on all Fc receptors that are critical for IgG therapeutic efficacy.
Language	English
Publishing date	2015
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606827-8
ISSN	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2015.00039
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Fc Sialylation Prolongs Serum Half-Life of Therapeutic Antibodies.

Bas, Mathilde / Terrier, Aurélie / Jacque, Emilie / Dehenne, Aurélie / Pochet-Béghin, Virginie / Beghin, Cécile / Dezetter, Anne-Sophie / Dupont, Gilles / Engrand, Anaïs / Beaufils, Benjamin / Mondon, Philippe / Fournier, Nathalie / de Romeuf, Christophe / Jorieux, Sylvie / Fontayne, Alexandre / Mars, Lennart T / Monnet, Céline

Journal of immunology (Baltimore, Md. : 1950)

2019 Volume 202, Issue 5, Page(s) 1582–1594

Abstract: ... The long ... ...

Abstract	The long serum
MeSH term(s)	Animals ; Antibodies/blood ; Antibodies/chemistry ; Antibodies/therapeutic use ; HEK293 Cells ; Half-Life ; Humans ; Immunoglobulin Fc Fragments/blood ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin G/blood ; Immunoglobulin G/chemistry ; Immunoglobulin G/therapeutic use ; Mice ; Mice, Knockout
Chemical Substances	Antibodies ; Immunoglobulin Fc Fragments ; Immunoglobulin G
Language	English
Publishing date	2019-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1800896
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.37: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 28: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Borna disease virus blocks potentiation of presynaptic activity through inhibition of protein kinase C signaling.

Volmer, Romain / Monnet, Céline / Gonzalez-Dunia, Daniel

PLoS pathogens

2006 Volume 2, Issue 3, Page(s) e19

Abstract: Infection by Borna disease virus (BDV) enables the study of the molecular mechanisms whereby a virus can persist in the central nervous system and lead to altered brain function in the absence of overt cytolysis and inflammation. This neurotropic virus ... ...

Abstract	Infection by Borna disease virus (BDV) enables the study of the molecular mechanisms whereby a virus can persist in the central nervous system and lead to altered brain function in the absence of overt cytolysis and inflammation. This neurotropic virus infects a wide variety of vertebrates and causes behavioral diseases. The basis of BDV-induced behavioral impairment remains largely unknown. Here, we investigated whether BDV infection of neurons affected synaptic activity, by studying the rate of synaptic vesicle (SV) recycling, a good indicator of synaptic activity. Vesicular cycling was visualized in cultured hippocampal neurons synapses, using an assay based on the uptake of an antibody directed against the luminal domain of synaptotagmin I. BDV infection did not affect elementary presynaptic functioning, such as spontaneous or depolarization-induced vesicular cycling. In contrast, infection of neurons with BDV specifically blocked the enhancement of SV recycling that is observed in response to stimuli-induced synaptic potentiation, suggesting defects in long-term potentiation. Studies of signaling pathways involved in synaptic potentiation revealed that this blockade was due to a reduction of the phosphorylation by protein kinase C (PKC) of proteins that regulate SV recycling, such as myristoylated alanine-rich C kinase substrate (MARCKS) and Munc18-1/nSec1. Moreover, BDV interference with PKC-dependent phosphorylation was identified downstream of PKC activation. We also provide evidence suggesting that the BDV phosphoprotein interferes with PKC-dependent phosphorylation. Altogether, our results reveal a new mechanism by which a virus can cause synaptic dysfunction and contribute to neurobehavioral disorders.
MeSH term(s)	Animals ; Borna Disease/physiopathology ; Borna Disease/virology ; Borna disease virus/physiology ; Cells, Cultured ; Enzyme Activation ; Molecular Sequence Data ; Neurons/physiology ; Presynaptic Terminals/physiology ; Protein Kinase C/metabolism ; Rats ; Signal Transduction/physiology ; Synapses/physiology ; Synaptic Vesicles/physiology
Chemical Substances	Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2006-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.0020019
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Affinity maturation of antibodies: optimized methods to generate high-quality ScFv libraries and isolate IgG candidates by high-throughput screening.

Renaut, Laurence / Monnet, Céline / Dubreuil, Olivier / Zaki, Ouafa / Crozet, Fabien / Bouayadi, Khalil / Kharrat, Hakim / Mondon, Philippe

Methods in molecular biology (Clifton, N.J.)

2012 Volume 907, Page(s) 451–461

Abstract: As a growing number of therapeutic antibodies are developed, robust methods to efficiently improve the affinity and/or specificity of antibody candidates are needed. Here we describe our powerful platform that combines scFv affinity maturation and IgG ... ...

Abstract	As a growing number of therapeutic antibodies are developed, robust methods to efficiently improve the affinity and/or specificity of antibody candidates are needed. Here we describe our powerful platform that combines scFv affinity maturation and IgG high-throughput screening. After creating diversity with our random mutagenesis technology (MutaGen™), the scFv libraries are fully cleaned using a fusion system introducing the beta-lactamase gene to select in-frame and stop codon free variants on the basis of ampicillin resistance. The high-quality scFv libraries thereby constructed are then selected on the target in vitro using phage display technology. Contrary to standard procedures, instead of producing a limited number of affinity matured scFv as IgG molecules, we developed a cloning system to directly transfer the entire pool of selected scFv into an IgG expression vector permitting rapid IgG small-scale production (96 wells) in mammalian cells. Our integrated process allows us to generate high-quality scFv libraries and test numerous IgG variants, increasing the chances to select the best therapeutic antibody candidate.
MeSH term(s)	Ampicillin/pharmacology ; Antibody Affinity/drug effects ; Antibody Affinity/immunology ; Cell Line ; Cloning, Molecular ; Genetic Vectors/genetics ; High-Throughput Screening Assays/methods ; Humans ; Immunoglobulin G/biosynthesis ; Immunoglobulin G/genetics ; Immunoglobulin G/isolation & purification ; Open Reading Frames/genetics ; Peptide Library ; Single-Chain Antibodies/biosynthesis
Chemical Substances	Immunoglobulin G ; Peptide Library ; Single-Chain Antibodies ; Ampicillin (7C782967RD)
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-61779-974-7_26
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells.

Monnet, Céline / Gavard, Julie / Mège, René-Marc / Sobel, André

FEBS letters

2004 Volume 576, Issue 1-2, Page(s) 114–118

Abstract: The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the ... ...

Abstract	The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering.
MeSH term(s)	Animals ; Antibodies, Monoclonal/metabolism ; Blotting, Western ; Butadienes/pharmacology ; Cells, Cultured ; Enzyme Inhibitors/pharmacology ; Fluorescent Antibody Technique, Indirect ; Mice ; Microscopy, Confocal ; Microtubule Proteins/metabolism ; Mitogen-Activated Protein Kinase 1/drug effects ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3/drug effects ; Mitogen-Activated Protein Kinase 3/metabolism ; Neurons/physiology ; Nitriles/pharmacology ; Phosphoproteins/metabolism ; Phosphorylation/drug effects ; PrPC Proteins/physiology ; Quinazolines ; RNA, Small Interfering/antagonists & inhibitors ; Stathmin ; Tyrphostins/pharmacology
Chemical Substances	Antibodies, Monoclonal ; Butadienes ; Enzyme Inhibitors ; Microtubule Proteins ; Nitriles ; Phosphoproteins ; PrPC Proteins ; Quinazolines ; RNA, Small Interfering ; Stathmin ; Stmn1 protein, mouse ; Tyrphostins ; U 0126 ; tyrphostin AG 1478 (170449-18-0) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24)
Language	English
Publishing date	2004-10-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2004.08.076
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.B 282: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Combined glyco- and protein-Fc engineering simultaneously enhance cytotoxicity and half-life of a therapeutic antibody.

Monnet, Céline / Jorieux, Sylvie / Souyris, Nathalie / Zaki, Ouafa / Jacquet, Alexandra / Fournier, Nathalie / Crozet, Fabien / de Romeuf, Christophe / Bouayadi, Khalil / Urbain, Rémi / Behrens, Christian K / Mondon, Philippe / Fontayne, Alexandre

mAbs

2014 Volume 6, Issue 2, Page(s) 422–436

Abstract: While glyco-engineered monoclonal antibodies (mAbs) with improved antibody-dependent cell-mediated cytotoxicity (ADCC) are reaching the market, extensive efforts have also been made to improve their pharmacokinetic properties to generate biologically ... ...

Abstract	While glyco-engineered monoclonal antibodies (mAbs) with improved antibody-dependent cell-mediated cytotoxicity (ADCC) are reaching the market, extensive efforts have also been made to improve their pharmacokinetic properties to generate biologically superior molecules. Most therapeutic mAbs are human or humanized IgG molecules whose half-life is dependent on the neonatal Fc receptor FcRn. FcRn reduces IgG catabolism by binding to the Fc domain of endocytosed IgG in acidic lysosomal compartments, allowing them to be recycled into the blood. Fc-engineered mAbs with increased FcRn affinity resulted in longer in vivo half-life in animal models, but also in healthy humans. These Fc-engineered mAbs were obtained by alanine scanning, directed mutagenesis or in silico approach of the FcRn binding site. In our approach, we applied a random mutagenesis technology (MutaGen™) to generate mutations evenly distributed over the whole Fc sequence of human IgG1. IgG variants with improved FcRn-binding were then isolated from these Fc-libraries using a pH-dependent phage display selection process. Two successive rounds of mutagenesis and selection were performed to identify several mutations that dramatically improve FcRn binding. Notably, many of these mutations were unpredictable by rational design as they were located distantly from the FcRn binding site, validating our random molecular approach. When produced on the EMABling(®) platform allowing effector function increase, our IgG variants retained both higher ADCC and higher FcRn binding. Moreover, these IgG variants exhibited longer half-life in human FcRn transgenic mice. These results clearly demonstrate that glyco-engineering to improve cytotoxicity and protein-engineering to increase half-life can be combined to further optimize therapeutic mAbs.
MeSH term(s)	Animals ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/pharmacokinetics ; Antibody-Dependent Cell Cytotoxicity/genetics ; Cell Surface Display Techniques ; Cytotoxicity, Immunologic/genetics ; Glycosylation ; Half-Life ; Histocompatibility Antigens Class I/genetics ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunoglobulin G/genetics ; Immunoglobulin G/metabolism ; Immunotherapy/methods ; Immunotherapy/trends ; Mice ; Mice, Transgenic ; Mutagenesis, Site-Directed ; Mutation/genetics ; Protein Engineering/methods ; Receptors, Fc/genetics ; Receptors, Fc/metabolism ; Receptors, IgG/antagonists & inhibitors ; Receptors, IgG/immunology ; Receptors, IgG/metabolism
Chemical Substances	Antibodies, Monoclonal ; FCGR3A protein, human ; Fc gamma receptor IIA ; Histocompatibility Antigens Class I ; Immunoglobulin G ; Receptors, Fc ; Receptors, IgG ; Fc receptor, neonatal (TW3XAW0RCY)
Language	English
Publishing date	2014-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2537838-7
ISSN	1942-0870 ; 1942-0870
ISSN (online)	1942-0870
ISSN	1942-0870
DOI	10.4161/mabs.27854
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: N-cadherin activation substitutes for the cell contact control in cell cycle arrest and myogenic differentiation: involvement of p120 and beta-catenin.

Gavard, Julie / Marthiens, Véronique / Monnet, Céline / Lambert, Mireille / Mège, René Marc

The Journal of biological chemistry

2004 Volume 279, Issue 35, Page(s) 36795–36802

Abstract: N-cadherin is expressed throughout skeletal myogenesis and has been proposed to be involved in the differentiation program of myogenic precursors. Here, we further characterize the N-cadherin involvement and its mechanism of action at the onset of ... ...

Abstract	N-cadherin is expressed throughout skeletal myogenesis and has been proposed to be involved in the differentiation program of myogenic precursors. Here, we further characterize the N-cadherin involvement and its mechanism of action at the onset of differentiation, through controlled N-cadherin activation by plating isolated C2 myoblasts on surfaces coated with a chimeric Ncad-Fc homophilic ligand (N-cadherin ectodomain fused to the immunoglobulin G Fc fragment). We show that N-cadherin activation substitutes for the cell density in myogenic differentiation by promoting myogenin and troponin T expression. In addition, N-cadherin adhesion participates to the associated cell cycle arrest through the nuclear accumulation of cyclin-dependent kinase inhibitors p21 and p27. Mouse primary myoblast cultures exhibited similar responses to N-cadherin as C2 cells. RNA interference knockdowns of the N-cadherin-associated cytoplasmic proteins p120 and beta-catenin produced opposite effects on the differentiation pathway. p120 silencing resulted in a decreased myogenic differentiation, associated with a reduction in cadherin-catenin content, which may explain its action on myogenic differentiation. beta-Catenin silencing led to a stimulatory effect on myogenin expression, without any effect on cell cycle. Our results demonstrate that N-cadherin adhesion may account for cell-cell contact-dependent cell cycle arrest and differentiation of myogenic cells, involving regulation through p120 and beta-catenins.
MeSH term(s)	Animals ; Blotting, Western ; Bromodeoxyuridine/pharmacology ; Cadherins/chemistry ; Cadherins/metabolism ; Cell Adhesion ; Cell Communication ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Lineage ; Cells, Cultured ; Cyclin-Dependent Kinase Inhibitor p27 ; Cytoskeletal Proteins/metabolism ; DNA/metabolism ; Gene Silencing ; Immunoglobulin Fragments/chemistry ; Immunoglobulin G/chemistry ; Ligands ; Mice ; Muscle Cells/metabolism ; Protein Binding ; RNA Interference ; RNA, Small Interfering/metabolism ; Time Factors ; Trans-Activators/metabolism ; Transfection ; Troponin T/chemistry ; Tumor Suppressor Proteins/metabolism ; beta Catenin ; p120 GTPase Activating Protein/metabolism
Chemical Substances	CTNNB1 protein, mouse ; Cadherins ; Cdkn1b protein, mouse ; Cell Cycle Proteins ; Cytoskeletal Proteins ; Immunoglobulin Fragments ; Immunoglobulin G ; Ligands ; RNA, Small Interfering ; Trans-Activators ; Troponin T ; Tumor Suppressor Proteins ; beta Catenin ; p120 GTPase Activating Protein ; Cyclin-Dependent Kinase Inhibitor p27 (147604-94-2) ; DNA (9007-49-2) ; Bromodeoxyuridine (G34N38R2N1)
Language	English
Publishing date	2004-06-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M401705200
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: La régulation de l'adherence cellulaire par la région cytoplasmique des cadhérines.

Gavard, Julie / Marthiens, Véronique / Monnet, Céline / Boscher, Cécile / Lambert, Mireille / Mège, René-Marc

Journal de la Societe de biologie

2004 Volume 198, Issue 4, Page(s) 365–374

Abstract: Juxtacrine cell interactions associated to cadherin-mediated cell-cell adhesion play a major role in the organization and homeostasis of tissues. Here, we review the intracellular molecules and regulations controlling the formation of cell-cell contacts ... ...

Title translation	Regulation of cell adhesion by the cadherin cytoplasmic domain.
Abstract	Juxtacrine cell interactions associated to cadherin-mediated cell-cell adhesion play a major role in the organization and homeostasis of tissues. Here, we review the intracellular molecules and regulations controlling the formation of cell-cell contacts initiated by homophilic interactions of cadherin ectodomain. These regulations involve proteins associated to cadherin cytoplasmic tail, named catenins, their association to the actin cytoskeleton and the stability of these complexes at the cell membrane. The underlying molecular mechanisms, which participate in the formation of dynamic cell-cell contacts, are intensively investigated.
MeSH term(s)	Actins/physiology ; Animals ; Cadherins/chemistry ; Cadherins/physiology ; Cell Adhesion/physiology ; Cell Communication/physiology ; Cell Membrane/physiology ; Cytoskeleton/physiology ; Homeostasis ; Humans
Chemical Substances	Actins ; Cadherins
Language	French
Publishing date	2004
Publishing country	France
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	1476234-1
ISSN	1760-6128 ; 1295-0661
ISSN (online)	1760-6128
ISSN	1295-0661
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.67: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Proteomic analysis reveals selective impediment of neuronal remodeling upon Borna disease virus infection.

Suberbielle, Elsa / Stella, Alexandre / Pont, Frédéric / Monnet, Céline / Mouton, Emmanuelle / Lamouroux, Lucile / Monsarrat, Bernard / Gonzalez-Dunia, Daniel

Journal of virology

2008 Volume 82, Issue 24, Page(s) 12265–12279

Abstract: The neurotropic virus Borna disease virus (BDV) persists in the central nervous systems of a wide variety of vertebrates and causes behavioral disorders. BDV represents an intriguing example of a virus whose persistence in neurons leads to altered brain ... ...

Abstract	The neurotropic virus Borna disease virus (BDV) persists in the central nervous systems of a wide variety of vertebrates and causes behavioral disorders. BDV represents an intriguing example of a virus whose persistence in neurons leads to altered brain function in the absence of overt cytolysis and inflammation. The bases of BDV-induced behavioral impairment remain largely unknown. To better characterize the neuronal response to BDV infection, we compared the proteomes of primary cultures of cortical neurons with and without BDV infection. We used two-dimensional liquid chromatography fractionation, followed by protein identification by nanoliquid chromatography-tandem mass spectrometry. This analysis revealed distinct changes in proteins implicated in neurotransmission, neurogenesis, cytoskeleton dynamics, and the regulation of gene expression and chromatin remodeling. We also demonstrated the selective interference of BDV with processes related to the adaptative response of neurons, i.e., defects in proteins regulating synaptic function, global rigidification of the cytoskeleton network, and altered expression of transcriptional and translational repressors. Thus, this work provides a global view of the neuronal changes induced by BDV infection together with new clues to understand the mechanisms underlying the selective interference with neuronal plasticity and remodeling that characterizes BDV persistence.
MeSH term(s)	Amino Acid Sequence ; Animals ; Borna disease virus/physiology ; Cells, Cultured ; Chromosomes/genetics ; Cytoskeleton/metabolism ; Databases, Protein ; Gene Expression Regulation ; Histones/metabolism ; Mass Spectrometry ; Neurons/metabolism ; Proteomics ; RNA, Messenger/genetics ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Histones ; RNA, Messenger
Language	English
Publishing date	2008-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01615-08
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

In stock of ZB MED Cologne/Königswinter

Zs.A 609: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

To top

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito