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Article: Structural Requirements for Activity of Mind bomb1 in Notch Signaling.

Cao, Ruili / Gozlan, Oren / Tveriakhina, Lena / Zhou, Haixia / Jiang, Hanjie / Cole, Philip A / Aster, Jon C / Sprinzak, David / Blacklow, Stephen C

bioRxiv : the preprint server for biology

2024

Abstract: Mind bomb 1 (MIB1) is a RING E3 ligase that ubiquitinates Notch ligands, a necessary step for induction of Notch signaling. The structural basis for binding of the JAG1 ligand by the N-terminal region of MIB1 is known, yet how the ankyrin (ANK) and RING ... ...

Abstract	Mind bomb 1 (MIB1) is a RING E3 ligase that ubiquitinates Notch ligands, a necessary step for induction of Notch signaling. The structural basis for binding of the JAG1 ligand by the N-terminal region of MIB1 is known, yet how the ankyrin (ANK) and RING domains of MIB1 cooperate to catalyze ubiquitin transfer from E2~Ub to Notch ligands remains unclear. Here, we show that the third RING domain and adjacent coiled coil region of MIB1 (ccRING3) drives MIB1 dimerization and that ubiquitin transfer activity of MIB1 relies solely on RING3. We report x-ray crystal structures of a UbcH5B-ccRING3 complex as a fusion protein and of the ANK region. Directly tethering the N-terminal region to ccRING3 forms a minimal MIB1 protein, which is sufficient to induce a Notch response in receiver cells. Together, these studies define the functional elements of an E3 ligase needed for ligands to induce a Notch signaling response.
Language	English
Publishing date	2024-03-03
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.03.01.582834
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Article ; Online: Temporal dynamics and stoichiometry in human Notch signaling from Notch synaptic complex formation to nuclear entry of the Notch intracellular domain.

Tveriakhina, Lena / Scanavachi, Gustavo / Egan, Emily D / Da Cunha Correia, Ricardo Bango / Martin, Alexandre P / Rogers, Julia M / Yodh, Jeremy S / Aster, Jon C / Kirchhausen, Tom / Blacklow, Stephen C

Developmental cell

2024

Abstract: Mammalian Notch signaling occurs when the binding of Delta or Jagged to Notch stimulates the proteolytic release of the Notch intracellular domain (NICD), which enters the nucleus to control target gene expression. To determine the temporal dynamics of ... ...

Abstract	Mammalian Notch signaling occurs when the binding of Delta or Jagged to Notch stimulates the proteolytic release of the Notch intracellular domain (NICD), which enters the nucleus to control target gene expression. To determine the temporal dynamics of events associated with Notch signaling under native conditions, we fluorescently tagged Notch and Delta at their endogenous genomic loci and visualized them upon pairing of receiver (Notch) and sender (Delta) cells as a function of time after cell contact. At contact sites, Notch and Delta immediately accumulated at 1:1 stoichiometry in synapses, which resolved by 15-20 min after contact. Synapse formation preceded the entrance of the Notch extracellular domain into the sender cell and accumulation of NICD in the nucleus of the receiver cell, which approached a maximum after ∼45 min and was prevented by chemical and genetic inhibitors of signaling. These findings directly link Notch-Delta synapse dynamics to NICD production with spatiotemporal precision.
Language	English
Publishing date	2024-03-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2024.03.021
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Article ; Online: A spatiotemporal Notch interaction map from plasma membrane to nucleus.

Martin, Alexandre P / Bradshaw, Gary A / Eisert, Robyn J / Egan, Emily D / Tveriakhina, Lena / Rogers, Julia M / Dates, Andrew N / Scanavachi, Gustavo / Aster, Jon C / Kirchhausen, Tom / Kalocsay, Marian / Blacklow, Stephen C

Science signaling

2023 Volume 16, Issue 796, Page(s) eadg6474

Abstract: Notch signaling relies on ligand-induced proteolysis of the transmembrane receptor Notch to liberate a nuclear effector that drives cell fate decisions. Upon ligand binding, sequential cleavage of Notch by the transmembrane protease ADAM10 and the ... ...

Abstract	Notch signaling relies on ligand-induced proteolysis of the transmembrane receptor Notch to liberate a nuclear effector that drives cell fate decisions. Upon ligand binding, sequential cleavage of Notch by the transmembrane protease ADAM10 and the intracellular protease γ-secretase releases the Notch intracellular domain (NICD), which translocates to the nucleus and forms a complex that induces target gene transcription. To map the location and timing of the individual steps required for the proteolysis and movement of Notch from the plasma membrane to the nucleus, we used proximity labeling with quantitative, multiplexed mass spectrometry to monitor the interaction partners of endogenous NOTCH2 after ligand stimulation in the presence of a γ-secretase inhibitor and as a function of time after inhibitor removal. Our studies showed that γ-secretase-mediated cleavage of NOTCH2 occurred in an intracellular compartment and that formation of nuclear complexes and recruitment of chromatin-modifying enzymes occurred within 45 min of inhibitor washout. These findings provide a detailed spatiotemporal map tracking the path of Notch from the plasma membrane to the nucleus and identify signaling events that are potential targets for modulating Notch activity.
MeSH term(s)	Amyloid Precursor Protein Secretases/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Ligands ; Receptors, Notch/genetics ; Receptors, Notch/metabolism ; Cell Membrane/metabolism ; Signal Transduction ; Receptor, Notch1/genetics
Chemical Substances	Amyloid Precursor Protein Secretases (EC 3.4.-) ; Ligands ; Receptors, Notch ; Receptor, Notch1
Language	English
Publishing date	2023-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.adg6474
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Article: Temporal Dynamics and Stoichiometry in Notch Signaling - from Notch Synaptic Complex Formation to NICD Nuclear Entry.

Tveriakhina, Lena / Scanavachi, Gustavo / Egan, Emily D / Correia, Ricardo Bango Da Cunha / Martin, Alexandre P / Rogers, Julia M / Yodh, Jeremy S / Aster, Jon C / Kirchhausen, Tom / Blacklow, Stephen C

bioRxiv : the preprint server for biology

2023

Abstract: Mammalian Notch signaling occurs when binding of Delta or Jagged to Notch stimulates proteolytic release of the Notch intracellular domain (NICD), which enters the nucleus to regulate target gene expression. To determine the temporal dynamics of events ... ...

Abstract	Mammalian Notch signaling occurs when binding of Delta or Jagged to Notch stimulates proteolytic release of the Notch intracellular domain (NICD), which enters the nucleus to regulate target gene expression. To determine the temporal dynamics of events associated with Notch signaling under native conditions, we fluorescently tagged Notch and Delta at their endogenous genomic loci and visualized them upon pairing of receiver (Notch) and sender (Delta) cells as a function of time after cell contact. At contact sites, Notch and Delta immediately accumulated at 1:1 stoichiometry in synapses, which resolved by 15-20 min after contact. Synapse formation preceded entrance of the Notch extracellular domain into the sender cell and accumulation of NICD in the nucleus of the receiver cell, which approached a maximum after ∼45 min and was prevented by chemical and genetic inhibitors of signaling. These findings directly link Notch-Delta synapse dynamics to NICD production with unprecedented spatiotemporal precision.
Language	English
Publishing date	2023-09-28
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.09.27.559780
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Article ; Online: The ectodomains determine ligand function in vivo and selectivity of DLL1 and DLL4 toward NOTCH1 and NOTCH2 in vitro.

Tveriakhina, Lena / Schuster-Gossler, Karin / Jarrett, Sanchez M / Andrawes, Marie B / Rohrbach, Meike / Blacklow, Stephen C / Gossler, Achim

eLife

2018 Volume 7

Abstract: DLL1 and DLL4 are Notch ligands with high structural similarity but context-dependent functional differences. Here, we analyze their functional divergence using cellular co-culture assays, biochemical studies, and in vivo experiments. DLL1 and DLL4 ... ...

Abstract	DLL1 and DLL4 are Notch ligands with high structural similarity but context-dependent functional differences. Here, we analyze their functional divergence using cellular co-culture assays, biochemical studies, and in vivo experiments. DLL1 and DLL4 activate NOTCH1 and NOTCH2 differently in cell-based assays and this discriminating potential lies in the region between the N-terminus and EGF repeat three. Mice expressing chimeric ligands indicate that the ectodomains dictate ligand function during somitogenesis, and that during myogenesis even regions C-terminal to EGF3 are interchangeable. Substitution of NOTCH1-interface residues in the MNNL and DSL domains of DLL1 with the corresponding amino acids of DLL4, however, does not disrupt DLL1 function in vivo. Collectively, our data show that DLL4 preferentially activates NOTCH1 over NOTCH2, whereas DLL1 is equally effective in activating NOTCH1 and NOTCH2, establishing that the ectodomains dictate selective ligand function in vivo, and that features outside the known binding interface contribute to their differences.
MeSH term(s)	Animals ; DNA Mutational Analysis ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Transgenic ; Protein Binding ; Protein Domains ; Protein Interaction Mapping ; Receptor, Notch1/metabolism ; Receptor, Notch2/metabolism ; Recombinant Proteins/metabolism
Chemical Substances	DLL4 protein, mouse ; Dlk1 protein, mouse ; Intercellular Signaling Peptides and Proteins ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Notch1 protein, mouse ; Notch2 protein, mouse ; Receptor, Notch1 ; Receptor, Notch2 ; Recombinant Proteins
Language	English
Publishing date	2018-10-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.40045
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Article ; Online: The FOXJ1 target

Beckers, Anja / Adis, Christian / Schuster-Gossler, Karin / Tveriakhina, Lena / Ott, Tim / Fuhl, Franziska / Hegermann, Jan / Boldt, Karsten / Serth, Katrin / Rachev, Ev / Alten, Leonie / Kremmer, Elisabeth / Ueffing, Marius / Blum, Martin / Gossler, Achim

Development (Cambridge, England)

2020 Volume 147, Issue 21

Abstract: Cilia are complex cellular protrusions consisting of hundreds of proteins. Defects in ciliary structure and function, many of which have not been characterised molecularly, cause ciliopathies: a heterogeneous group of human syndromes. Here, we report on ... ...

Abstract	Cilia are complex cellular protrusions consisting of hundreds of proteins. Defects in ciliary structure and function, many of which have not been characterised molecularly, cause ciliopathies: a heterogeneous group of human syndromes. Here, we report on the FOXJ1 target gene
MeSH term(s)	Animals ; Axoneme/metabolism ; Basal Bodies/metabolism ; Brain/embryology ; Brain/metabolism ; Cilia/metabolism ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/metabolism ; Embryonic Development ; Epithelial Cells/metabolism ; Fluorescence ; Forkhead Transcription Factors/metabolism ; Hydrocephalus/pathology ; Infertility, Male/pathology ; Lung/metabolism ; Male ; Mice, Knockout ; Mucociliary Clearance ; Mucus/metabolism ; Mutation/genetics ; Protein Transport ; Sperm Motility ; Spermatozoa/metabolism ; Spermatozoa/ultrastructure ; Xenopus laevis/embryology ; Xenopus laevis/metabolism
Chemical Substances	Cfap206 protein, mouse ; Cytoskeletal Proteins ; FOXJ1 protein, mouse ; Forkhead Transcription Factors
Language	English
Publishing date	2020-06-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.188052
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Article ; Online: CFAP43 modulates ciliary beating in mouse and Xenopus.

Rachev, Ev / Schuster-Gossler, Karin / Fuhl, Franziska / Ott, Tim / Tveriakhina, Lena / Beckers, Anja / Hegermann, Jan / Boldt, Karsten / Mai, Michaela / Kremmer, Elisabeth / Ueffing, Marius / Blum, Martin / Gossler, Achim

Developmental biology

2019 Volume 459, Issue 2, Page(s) 109–125

Abstract: Malfunctions of motile cilia cause a variety of developmental defects and diseases in humans and animal model organisms. Defects include impaired mucociliary clearance of the airways, sperm immotility, hydrocephalus and organ laterality. Here, we ... ...

Abstract	Malfunctions of motile cilia cause a variety of developmental defects and diseases in humans and animal model organisms. Defects include impaired mucociliary clearance of the airways, sperm immotility, hydrocephalus and organ laterality. Here, we characterize the evolutionary conserved Cfap43 gene by loss-of-function experiments in the mouse and the frog Xenopus laevis. Cfap43 is expressed in tissues carrying motile cilia and acts as a target gene of the transcription factor FOXJ1, which is essential for the induction of motile ciliogenesis. We show that CFAP43, a protein of unknown biochemical function, localizes to the ciliary axoneme. CFAP43 is involved in the regulation of the beating frequency of tracheal cilia and loss of CFAP43 causes severe mucus accumulation in the nasal cavity. Likewise, morphant and crispant frog embryos revealed impaired function of motile cilia of the larval epidermis, a model for airway mucociliary epithelia. CFAP43 participates in the formation of flagellar axonemes during spermatogenesis as mice mutant for Cfap43 display male infertility, consistent with observations in male sterile patients. In addition, mice mutant for Cfap43 display early onset hydrocephalus. Together, these results confirm the role of CFAP43 in the male reproductive tract and pinpoint additional functions in airway epithelia mucus clearance and brain development.
MeSH term(s)	Animals ; Cilia/metabolism ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Epidermal Cells/metabolism ; Forkhead Transcription Factors/metabolism ; Hydrocephalus/genetics ; Infertility, Male/genetics ; Male ; Mice ; Mice, Knockout ; Sperm Tail/metabolism ; Spermatogenesis/genetics ; Spermatozoa/metabolism ; Trachea/cytology ; Xenopus Proteins/genetics ; Xenopus Proteins/metabolism ; Xenopus laevis
Chemical Substances	Cfap43 protein, mouse ; Cytoskeletal Proteins ; FOXJ1 protein, mouse ; Forkhead Transcription Factors ; Xenopus Proteins
Language	English
Publishing date	2019-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2019.12.010
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Article ; Online: Context-Dependent Functional Divergence of the Notch Ligands DLL1 and DLL4 In Vivo.

Preuße, Kristina / Tveriakhina, Lena / Schuster-Gossler, Karin / Gaspar, Cláudia / Rosa, Alexandra Isabel / Henrique, Domingos / Gossler, Achim / Stauber, Michael

PLoS genetics

2015 Volume 11, Issue 6, Page(s) e1005328

Abstract: Notch signalling is a fundamental pathway that shapes the developing embryo and sustains adult tissues by direct communication between ligand and receptor molecules on adjacent cells. Among the ligands are two Delta paralogues, DLL1 and DLL4, that are ... ...

Abstract	Notch signalling is a fundamental pathway that shapes the developing embryo and sustains adult tissues by direct communication between ligand and receptor molecules on adjacent cells. Among the ligands are two Delta paralogues, DLL1 and DLL4, that are conserved in mammals and share a similar structure and sequence. They activate the Notch receptor partly in overlapping expression domains where they fulfil redundant functions in some processes (e.g. maintenance of the crypt cell progenitor pool). In other processes, however, they appear to act differently (e.g. maintenance of foetal arterial identity) raising the questions of how similar DLL1 and DLL4 really are and which mechanism causes the apparent context-dependent divergence. By analysing mice that conditionally overexpress DLL1 or DLL4 from the same genomic locus (Hprt) and mice that express DLL4 instead of DLL1 from the endogenous Dll1 locus (Dll1Dll4ki), we found functional differences that are tissue-specific: while DLL1 and DLL4 act redundantly during the maintenance of retinal progenitors, their function varies in the presomitic mesoderm (PSM) where somites form in a Notch-dependent process. In the anterior PSM, every cell expresses both Notch receptors and ligands, and DLL1 is the only activator of Notch while DLL4 is not endogenously expressed. Transgenic DLL4 cannot replace DLL1 during somitogenesis and in heterozygous Dll1Dll4ki/+ mice, the Dll1Dll4ki allele causes a dominant segmentation phenotype. Testing several aspects of the complex Notch signalling system in vitro, we found that both ligands have a similar trans-activation potential but that only DLL4 is an efficient cis-inhibitor of Notch signalling, causing a reduced net activation of Notch. These differential cis-inhibitory properties are likely to contribute to the functional divergence of DLL1 and DLL4.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Animals ; Calcium-Binding Proteins ; Extremities/embryology ; Gene Expression Regulation, Developmental ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mesoderm/metabolism ; Mice, Transgenic ; Protein Structure, Tertiary ; Receptors, Notch/metabolism ; Retina/embryology ; Signal Transduction
Chemical Substances	Adaptor Proteins, Signal Transducing ; Calcium-Binding Proteins ; DLL4 protein, mouse ; Dlk1 protein, mouse ; Intercellular Signaling Peptides and Proteins ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Receptors, Notch
Language	English
Publishing date	2015-06-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1005328
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Article ; Online: The Mammalian Orthologs of Drosophila Lgd, CC2D1A and CC2D1B, Function in the Endocytic Pathway, but Their Individual Loss of Function Does Not Affect Notch Signalling.

Drusenheimer, Nadja / Migdal, Bernhard / Jäckel, Sandra / Tveriakhina, Lena / Scheider, Kristina / Schulz, Katharina / Gröper, Jieny / Köhrer, Karl / Klein, Thomas

PLoS genetics

2015 Volume 11, Issue 12, Page(s) e1005749

Abstract: CC2D1A and CC2D1B belong to the evolutionary conserved Lgd protein family with members in all multi-cellular animals. Several functions such as centrosomal cleavage, involvement in signalling pathways, immune response and synapse maturation have been ... ...

Abstract	CC2D1A and CC2D1B belong to the evolutionary conserved Lgd protein family with members in all multi-cellular animals. Several functions such as centrosomal cleavage, involvement in signalling pathways, immune response and synapse maturation have been described for CC2D1A. Moreover, the Drosophila melanogaster ortholog Lgd was shown to be involved in the endosomal trafficking of the Notch receptor and other transmembrane receptors and physically interacts with the ESCRT-III component Shrub/CHMP4. To determine if this function is conserved in mammals we generated and characterized Cc2d1a and Cc2d1b conditional knockout mice. While Cc2d1b deficient mice displayed no obvious phenotype, we found that Cc2d1a deficient mice as well as conditional mutants that lack CC2D1A only in the nervous system die shortly after birth due to respiratory distress. This finding confirms the suspicion that the breathing defect is caused by the central nervous system. However, an involvement in centrosomal function could not be confirmed in Cc2d1a deficient MEF cells. To analyse an influence on Notch signalling, we generated intestine specific Cc2d1a mutant mice. These mice did not display any alterations in goblet cell number, proliferating cell number or expression of the Notch reporter Hes1-emGFP, suggesting that CC2D1A is not required for Notch signalling. However, our EM analysis revealed that the average size of endosomes of Cc2d1a mutant cells, but not Cc2d1b mutant cells, is increased, indicating a defect in endosomal morphogenesis. We could show that CC2D1A and its interaction partner CHMP4B are localised on endosomes in MEF cells, when the activity of the endosomal protein VPS4 is reduced. This indicates that CC2D1A cycles between the cytosol and the endosomal membrane. Additionally, in rescue experiments in D. melanogaster, CC2D1A and CC2D1B were able to functionally replace Lgd. Altogether our data suggest a functional conservation of the Lgd protein family in the ESCRT-III mediated process in metazoans.
MeSH term(s)	Animals ; Animals, Newborn ; Centrosome/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Endocytosis/physiology ; Endosomal Sorting Complexes Required for Transport ; Endosomes/metabolism ; Epithelium/metabolism ; Female ; Gene Expression Regulation, Developmental ; Intestinal Mucosa/metabolism ; Intestines/pathology ; Male ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; Receptor, Notch1/genetics ; Receptor, Notch1/metabolism ; Receptors, Notch/genetics ; Receptors, Notch/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Signal Transduction/genetics ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; Vesicular Transport Proteins/metabolism
Chemical Substances	CC2D1B protein, mouse ; CHMP4B protein, mouse ; Drosophila Proteins ; Endosomal Sorting Complexes Required for Transport ; Freud-1 protein, mouse ; Notch1 protein, mouse ; Receptor, Notch1 ; Receptors, Notch ; Repressor Proteins ; Tumor Suppressor Proteins ; Vesicular Transport Proteins ; l(2)gd1 protein, Drosophila
Language	English
Publishing date	2015-12-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1005749
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