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Cell biology of corn smut disease — Ustilago maydis as a model for biotrophic interactions
Current Opinion in Microbiology, ISSN 1369-5274, 2016, Volume 34, pp. 60 - 66
Highlights • Ustilago maydis is a biotrophic pathogen with dimorphic life-style. • Pathogenicity is directly linked with mating and morphological transition. •...
Pathology | TRANSPORT | PROTEIN | PATHOGENIC DEVELOPMENT | MAGNAPORTHE-ORYZAE | MICROBIOLOGY | EARLY ENDOSOME MOTILITY | SECRETED EFFECTOR | ENDOCYTOSIS | VIRULENCE | FILAMENTOUS FUNGI | PLANT INFECTION | Hyphae - metabolism | Zea mays - microbiology | Plant Diseases - microbiology | Ustilago - ultrastructure | Ustilago - genetics | Ustilago - cytology | Ustilago - physiology | Fungal Proteins - metabolism | Corn | Pornography | Cells | Imaging systems
Pathology | TRANSPORT | PROTEIN | PATHOGENIC DEVELOPMENT | MAGNAPORTHE-ORYZAE | MICROBIOLOGY | EARLY ENDOSOME MOTILITY | SECRETED EFFECTOR | ENDOCYTOSIS | VIRULENCE | FILAMENTOUS FUNGI | PLANT INFECTION | Hyphae - metabolism | Zea mays - microbiology | Plant Diseases - microbiology | Ustilago - ultrastructure | Ustilago - genetics | Ustilago - cytology | Ustilago - physiology | Fungal Proteins - metabolism | Corn | Pornography | Cells | Imaging systems
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 07/2018, Volume 430, Issue 14, pp. 2153 - 2163
Multi-subunit tethering complexes control membrane fusion events in eukaryotic cells. Class C core vacuole/endosome tethering (CORVET) and homotypic fusion and...
SPE-39 | VIPAS39 | VPS16B | X-linked intellectual disability (XLID) | Sec1/Munc18 | RECRUITMENT | MAMMALIAN CORVET | LYSOSOME FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | WASH COMPLEX | ALPHA-GRANULE BIOGENESIS | TRAFFICKING | EARLY ENDOSOME | BINDING PROTEIN | MATURATION | HOPS COMPLEX | Cellular proteins | Cells | GARP, Golgi-associated retrograde protein | HEK293T, human embryonic kidney 293T | Sec1 | CORVET, class C core vacuole | PI3KC3, class III phosphatidylinositol 3-kinase | XLID, X-linked intellectual disability | Munc18 | HOPS, homotypic fusion and vacuole protein sorting | CHEVI, class C homologs in endosome–vesicle interaction | BFDR, Bayesian false discovery rate | endosome tethering | EARP, endosome-associated recycling protein
SPE-39 | VIPAS39 | VPS16B | X-linked intellectual disability (XLID) | Sec1/Munc18 | RECRUITMENT | MAMMALIAN CORVET | LYSOSOME FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | WASH COMPLEX | ALPHA-GRANULE BIOGENESIS | TRAFFICKING | EARLY ENDOSOME | BINDING PROTEIN | MATURATION | HOPS COMPLEX | Cellular proteins | Cells | GARP, Golgi-associated retrograde protein | HEK293T, human embryonic kidney 293T | Sec1 | CORVET, class C core vacuole | PI3KC3, class III phosphatidylinositol 3-kinase | XLID, X-linked intellectual disability | Munc18 | HOPS, homotypic fusion and vacuole protein sorting | CHEVI, class C homologs in endosome–vesicle interaction | BFDR, Bayesian false discovery rate | endosome tethering | EARP, endosome-associated recycling protein
Journal Article
Molecular Biology of the Cell, ISSN 1059-1524, 11/2013, Volume 24, Issue 22, pp. 3522 - 3533
Lis1, Nudel/NudE, and dynactin are regulators of cytoplasmic dynein, a minus end-directed, microtubule (MT)-based motor required for proper spindle assembly...
CYTOPLASMIC DYNEIN | NEURONAL MIGRATION | XENOPUS EGG EXTRACTS | COILED-COIL DOMAIN | ASPERGILLUS-NIDULANS | MICROTUBULE-BINDING | INTRACELLULAR-LOCALIZATION | EARLY-ENDOSOME INTERACTION | ORGANELLE TRANSPORT | MOLECULAR-MECHANISMS | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Xenopus Proteins - genetics | Microtubule-Associated Proteins - metabolism | Zygote - metabolism | Male | Spermatozoa - metabolism | Microtubules - metabolism | Spindle Apparatus - metabolism | Gene Expression Regulation, Developmental | Escherichia coli - metabolism | Microtubules - ultrastructure | Female | Xenopus laevis - genetics | Xenopus laevis - growth & development | Nuclear Proteins - genetics | Spindle Apparatus - ultrastructure | Dyneins - metabolism | Recombinant Proteins - metabolism | Kinetochores - metabolism | Morphogenesis - genetics | Signal Transduction | Dynactin Complex | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Protein Transport | Kinetochores - ultrastructure | Animals | Escherichia coli - genetics | Xenopus laevis - metabolism | Protein Binding | Xenopus Proteins - metabolism | Dyneins - genetics | Zygote - chemistry
CYTOPLASMIC DYNEIN | NEURONAL MIGRATION | XENOPUS EGG EXTRACTS | COILED-COIL DOMAIN | ASPERGILLUS-NIDULANS | MICROTUBULE-BINDING | INTRACELLULAR-LOCALIZATION | EARLY-ENDOSOME INTERACTION | ORGANELLE TRANSPORT | MOLECULAR-MECHANISMS | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Xenopus Proteins - genetics | Microtubule-Associated Proteins - metabolism | Zygote - metabolism | Male | Spermatozoa - metabolism | Microtubules - metabolism | Spindle Apparatus - metabolism | Gene Expression Regulation, Developmental | Escherichia coli - metabolism | Microtubules - ultrastructure | Female | Xenopus laevis - genetics | Xenopus laevis - growth & development | Nuclear Proteins - genetics | Spindle Apparatus - ultrastructure | Dyneins - metabolism | Recombinant Proteins - metabolism | Kinetochores - metabolism | Morphogenesis - genetics | Signal Transduction | Dynactin Complex | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Protein Transport | Kinetochores - ultrastructure | Animals | Escherichia coli - genetics | Xenopus laevis - metabolism | Protein Binding | Xenopus Proteins - metabolism | Dyneins - genetics | Zygote - chemistry
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 10/2019, Volume 116, Issue 42, pp. 21291 - 21301
Vacuoles are essential organelles in plants, playing crucial roles, such as cellular material degradation, ion and metabolite storage, and turgor maintenance....
AUTOPHAGOSOME-LYSOSOME FUSION | small molecule | RAB7 | PROTEIN STORAGE VACUOLES | MULTIDISCIPLINARY SCIENCES | RABG3f | PREVACUOLAR COMPARTMENT | GOLGI NETWORK/EARLY ENDOSOME | TRAFFICKING | CELL-DEATH | retromer | CORE RETROMER | VPS35 | ARABIDOPSIS | PLANT-GROWTH | HOPS COMPLEX | Membranes | GTP | Target recognition | Turgor | Traffic | Phagosomes | Homology | Proteins | Receptors | Metabolites | Compartments | Traffic control | Protein transport | Fusion protein | Ethylmaleimide | Assembly | Anchoring | Adaptor proteins | Membrane fusion | Tethering | Maintenance | Adaptors | Organelles | Vacuoles | N-Ethylmaleimide | Basic Medicine | Biological Sciences | Medical and Health Sciences | Medicin och hälsovetenskap | Cell and Molecular Biology | Cell Biology | Naturvetenskap | Biologiska vetenskaper | Medicinska och farmaceutiska grundvetenskaper | Natural Sciences | Cellbiologi | Cell- och molekylärbiologi
AUTOPHAGOSOME-LYSOSOME FUSION | small molecule | RAB7 | PROTEIN STORAGE VACUOLES | MULTIDISCIPLINARY SCIENCES | RABG3f | PREVACUOLAR COMPARTMENT | GOLGI NETWORK/EARLY ENDOSOME | TRAFFICKING | CELL-DEATH | retromer | CORE RETROMER | VPS35 | ARABIDOPSIS | PLANT-GROWTH | HOPS COMPLEX | Membranes | GTP | Target recognition | Turgor | Traffic | Phagosomes | Homology | Proteins | Receptors | Metabolites | Compartments | Traffic control | Protein transport | Fusion protein | Ethylmaleimide | Assembly | Anchoring | Adaptor proteins | Membrane fusion | Tethering | Maintenance | Adaptors | Organelles | Vacuoles | N-Ethylmaleimide | Basic Medicine | Biological Sciences | Medical and Health Sciences | Medicin och hälsovetenskap | Cell and Molecular Biology | Cell Biology | Naturvetenskap | Biologiska vetenskaper | Medicinska och farmaceutiska grundvetenskaper | Natural Sciences | Cellbiologi | Cell- och molekylärbiologi
Journal Article
Frontiers in Plant Science, ISSN 1664-462X, 01/2016, Volume 6, Issue 2016, p. 1262
The dynamic localization of endosomal compartments labeled with targeted fluorescent protein tags is routinely followed by time lapse fluorescence microscopy...
Arabidopsis thaliana | Spinning disc microscopy | Interaction | Trafficking | Root hair | Development | Endosomes | Structured illumination microscopy | CLATHRIN-MEDIATED ENDOCYTOSIS | development | VESICULAR TRAFFICKING | GOLGI NETWORK/EARLY ENDOSOME | endosomes | LIVING PLANT-CELLS | PLANT SCIENCES | structured illumination microscopy | CELL PLATE FORMATION | root hair | PARTICLE TRACKING | interaction | POLLEN TUBES | spinning disc microscopy | trafficking | KISS-AND-RUN | TIP GROWTH | Roots (Botany) | Growth (Plants) | Observations | Growth
Arabidopsis thaliana | Spinning disc microscopy | Interaction | Trafficking | Root hair | Development | Endosomes | Structured illumination microscopy | CLATHRIN-MEDIATED ENDOCYTOSIS | development | VESICULAR TRAFFICKING | GOLGI NETWORK/EARLY ENDOSOME | endosomes | LIVING PLANT-CELLS | PLANT SCIENCES | structured illumination microscopy | CELL PLATE FORMATION | root hair | PARTICLE TRACKING | interaction | POLLEN TUBES | spinning disc microscopy | trafficking | KISS-AND-RUN | TIP GROWTH | Roots (Botany) | Growth (Plants) | Observations | Growth
Journal Article
Traffic, ISSN 1398-9219, 03/2008, Volume 9, Issue 3, pp. 366 - 379
Retromer is a heteromeric protein complex with important roles in endosomal membrane trafficking, most notably in the retrograde transport of lysosomal...
Vps29 | endosome | isothermal titration calorimetry | retromer | sorting nexin | fibronectin domain | Vps35 | arrestin | Vps26 | Sorting nexin | Arrestin | Fibronectin domain | Isothermal titration calorimetry | Endosome | Retromer | SORTING NEXIN-1 | MAMMALIAN RETROMER | DOWN-REGULATION | RECEPTOR | EARLY ENDOSOME | IDENTIFICATION | CELL BIOLOGY | REQUIRES RETROMER | RETROGRADE TRANSPORT | COMPONENT | Recombinant Proteins - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Arrestins - chemistry | Vesicular Transport Proteins - metabolism | Multiprotein Complexes | Vesicular Transport Proteins - genetics | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Vesicular Transport Proteins - chemistry | Recombinant Proteins - genetics | Endosomes - metabolism | Protein Interaction Mapping | Two-Hybrid System Techniques | Animals | Mice | In Vitro Techniques | Binding Sites | Proteins
Vps29 | endosome | isothermal titration calorimetry | retromer | sorting nexin | fibronectin domain | Vps35 | arrestin | Vps26 | Sorting nexin | Arrestin | Fibronectin domain | Isothermal titration calorimetry | Endosome | Retromer | SORTING NEXIN-1 | MAMMALIAN RETROMER | DOWN-REGULATION | RECEPTOR | EARLY ENDOSOME | IDENTIFICATION | CELL BIOLOGY | REQUIRES RETROMER | RETROGRADE TRANSPORT | COMPONENT | Recombinant Proteins - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Arrestins - chemistry | Vesicular Transport Proteins - metabolism | Multiprotein Complexes | Vesicular Transport Proteins - genetics | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Vesicular Transport Proteins - chemistry | Recombinant Proteins - genetics | Endosomes - metabolism | Protein Interaction Mapping | Two-Hybrid System Techniques | Animals | Mice | In Vitro Techniques | Binding Sites | Proteins
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2016, Volume 291, Issue 35, pp. 18239 - 18251
Cytoplasmic dynein drives the majority of minus end-directed vesicular and organelle motility in the cell. However, it remains unclear how dynein is spatially...
CYTOPLASMIC DYNEIN | COMPLEX | PROTEIN | cytoskeleton | MICROTUBULES | kinesin | BIOCHEMISTRY & MOLECULAR BIOLOGY | intracellular trafficking | AXONAL-TRANSPORT | dynein | microtubule | AUTOINHIBITION | CARGO | STRUCTURAL BASIS | EARLY ENDOSOMES | BINDING | Dyneins - metabolism | Peroxisomes - genetics | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Peroxisomes - metabolism | Dynactin Complex - metabolism | Microtubules - metabolism | Animals | Microtubules - genetics | Mice | Dyneins - genetics | HeLa Cells | COS Cells | Dynactin Complex - genetics | Cell Biology
CYTOPLASMIC DYNEIN | COMPLEX | PROTEIN | cytoskeleton | MICROTUBULES | kinesin | BIOCHEMISTRY & MOLECULAR BIOLOGY | intracellular trafficking | AXONAL-TRANSPORT | dynein | microtubule | AUTOINHIBITION | CARGO | STRUCTURAL BASIS | EARLY ENDOSOMES | BINDING | Dyneins - metabolism | Peroxisomes - genetics | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Peroxisomes - metabolism | Dynactin Complex - metabolism | Microtubules - metabolism | Animals | Microtubules - genetics | Mice | Dyneins - genetics | HeLa Cells | COS Cells | Dynactin Complex - genetics | Cell Biology
Journal Article
Biology of Reproduction, ISSN 0006-3363, 05/2010, Volume 82, Issue 5, pp. 930 - 939
Ubiquitin-specific peptidase 8 (USP8) is a deubiquitinating enzyme that works as a regulator of endosomal sorting and vesicle morphology in cultured cells. Its...
Acrosome biogenesis | USP8 | Spermatogenesis | Early endosome | VPS54 | Acrosome | STAM2 | Spermatid | Endosomes | DOMAIN | acrosome | UBIQUITIN | SPERMIOGENESIS | HRS-BINDING-PROTEIN | GOLGI-APPARATUS | DOWN-REGULATION | endosomes | MEMBRANE-PROTEIN | DEUBIQUITINATING ENZYME MUBPY | UBPY | TRANSPORT | REPRODUCTIVE BIOLOGY | acrosome biogenesis | spermatogenesis | early endosome | spermatid | Endopeptidases - metabolism | Spermatids - metabolism | Testis - metabolism | Testis - cytology | Acrosome - metabolism | Endosomal Sorting Complexes Required for Transport - metabolism | Male | Protein Transport - physiology | Spermatids - enzymology | Phosphoproteins - metabolism | Endosomes - metabolism | Protein Interaction Mapping | Microtubules - metabolism | Spermatogenesis - physiology | Animals | Testis - enzymology | Ubiquitin Thiolesterase - metabolism | Mice | Adaptor Proteins, Signal Transducing - metabolism
Acrosome biogenesis | USP8 | Spermatogenesis | Early endosome | VPS54 | Acrosome | STAM2 | Spermatid | Endosomes | DOMAIN | acrosome | UBIQUITIN | SPERMIOGENESIS | HRS-BINDING-PROTEIN | GOLGI-APPARATUS | DOWN-REGULATION | endosomes | MEMBRANE-PROTEIN | DEUBIQUITINATING ENZYME MUBPY | UBPY | TRANSPORT | REPRODUCTIVE BIOLOGY | acrosome biogenesis | spermatogenesis | early endosome | spermatid | Endopeptidases - metabolism | Spermatids - metabolism | Testis - metabolism | Testis - cytology | Acrosome - metabolism | Endosomal Sorting Complexes Required for Transport - metabolism | Male | Protein Transport - physiology | Spermatids - enzymology | Phosphoproteins - metabolism | Endosomes - metabolism | Protein Interaction Mapping | Microtubules - metabolism | Spermatogenesis - physiology | Animals | Testis - enzymology | Ubiquitin Thiolesterase - metabolism | Mice | Adaptor Proteins, Signal Transducing - metabolism
Journal Article
Journal of Investigative Dermatology, ISSN 0022-202X, 01/2015, Volume 135, Issue 1, pp. 229 - 237
We previously identified the NK cell receptor KIR3DL2 as a valuable diagnostic and prognostic marker for the detection of the tumoral T cell burden of Sézary...
DIAGNOSIS | RECOGNITION | DNA | RELEVANCE | GROWTH | PERIPHERAL-BLOOD | EARLY ENDOSOMES | CPG | EXPRESSION | CLONE | DERMATOLOGY | Mycosis Fungoides - immunology | Apoptosis - drug effects | Humans | Receptors, KIR3DL2 - immunology | CD4-Positive T-Lymphocytes - immunology | Signal Transduction - immunology | Mycosis Fungoides - metabolism | Phosphorylation - immunology | Phosphorylation - drug effects | Oligodeoxyribonucleotides - metabolism | STAT3 Transcription Factor - metabolism | Sezary Syndrome - immunology | Oligodeoxyribonucleotides - immunology | Skin Neoplasms - immunology | CD4-Positive T-Lymphocytes - metabolism | Cells, Cultured | Skin Neoplasms - metabolism | Receptors, KIR3DL2 - metabolism | Apoptosis - immunology | Sezary Syndrome - metabolism | Signal Transduction - drug effects | Ligands | STAT3 Transcription Factor - immunology | Oligodeoxyribonucleotides - pharmacology | CD4-Positive T-Lymphocytes - drug effects
DIAGNOSIS | RECOGNITION | DNA | RELEVANCE | GROWTH | PERIPHERAL-BLOOD | EARLY ENDOSOMES | CPG | EXPRESSION | CLONE | DERMATOLOGY | Mycosis Fungoides - immunology | Apoptosis - drug effects | Humans | Receptors, KIR3DL2 - immunology | CD4-Positive T-Lymphocytes - immunology | Signal Transduction - immunology | Mycosis Fungoides - metabolism | Phosphorylation - immunology | Phosphorylation - drug effects | Oligodeoxyribonucleotides - metabolism | STAT3 Transcription Factor - metabolism | Sezary Syndrome - immunology | Oligodeoxyribonucleotides - immunology | Skin Neoplasms - immunology | CD4-Positive T-Lymphocytes - metabolism | Cells, Cultured | Skin Neoplasms - metabolism | Receptors, KIR3DL2 - metabolism | Apoptosis - immunology | Sezary Syndrome - metabolism | Signal Transduction - drug effects | Ligands | STAT3 Transcription Factor - immunology | Oligodeoxyribonucleotides - pharmacology | CD4-Positive T-Lymphocytes - drug effects
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 10/2007, Volume 14, Issue 10, pp. 904 - 911
Synaptotagmin-1 is the calcium sensor for neuronal exocytosis, but the mechanism by which it triggers membrane fusion is not fully understood. Here we show...
SYNAPTIC EXOCYTOSIS | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HOMOTYPIC FUSION | T-SNARE | PLASMA-MEMBRANE | MOTIF | CELL BIOLOGY | BIOPHYSICS | SNARE COMPLEX | IN-VIVO | CA2+ BINDING | EARLY ENDOSOMES | Peptide Fragments - metabolism | Calcium - metabolism | Multiprotein Complexes | Rats | Synaptotagmin I - genetics | Animals | Synaptotagmin I - metabolism | Liposomes - metabolism | Neurons - metabolism | Phospholipids - metabolism | Membrane Fusion - physiology | Peptide Fragments - genetics | SNARE Proteins - metabolism
SYNAPTIC EXOCYTOSIS | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HOMOTYPIC FUSION | T-SNARE | PLASMA-MEMBRANE | MOTIF | CELL BIOLOGY | BIOPHYSICS | SNARE COMPLEX | IN-VIVO | CA2+ BINDING | EARLY ENDOSOMES | Peptide Fragments - metabolism | Calcium - metabolism | Multiprotein Complexes | Rats | Synaptotagmin I - genetics | Animals | Synaptotagmin I - metabolism | Liposomes - metabolism | Neurons - metabolism | Phospholipids - metabolism | Membrane Fusion - physiology | Peptide Fragments - genetics | SNARE Proteins - metabolism
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 10/2004, Volume 11, Issue 10, pp. 975 - 983
Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and...
BOUND FORM | SMALL GTPASE RAB5 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GUANINE-NUCLEOTIDE EXCHANGE | FUNCTIONAL SPECIFICITY | CELL BIOLOGY | MEMBRANE-FUSION | SIGNAL-TRANSDUCTION | GDP-DISSOCIATION INHIBITOR | BIOPHYSICS | GDP/GTP EXCHANGE | EARLY ENDOSOMES | rab GTP-Binding Proteins - metabolism | Amino Acid Sequence | Vesicular Transport Proteins - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Vesicular Transport Proteins - chemistry | rab5 GTP-Binding Proteins - metabolism | Sequence Homology, Amino Acid | Endocytosis | rab5 GTP-Binding Proteins - chemistry | Protein Binding | Protein Conformation | rab GTP-Binding Proteins - chemistry | Physiological aspects | Research | Structure | Membrane proteins
BOUND FORM | SMALL GTPASE RAB5 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GUANINE-NUCLEOTIDE EXCHANGE | FUNCTIONAL SPECIFICITY | CELL BIOLOGY | MEMBRANE-FUSION | SIGNAL-TRANSDUCTION | GDP-DISSOCIATION INHIBITOR | BIOPHYSICS | GDP/GTP EXCHANGE | EARLY ENDOSOMES | rab GTP-Binding Proteins - metabolism | Amino Acid Sequence | Vesicular Transport Proteins - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Vesicular Transport Proteins - chemistry | rab5 GTP-Binding Proteins - metabolism | Sequence Homology, Amino Acid | Endocytosis | rab5 GTP-Binding Proteins - chemistry | Protein Binding | Protein Conformation | rab GTP-Binding Proteins - chemistry | Physiological aspects | Research | Structure | Membrane proteins
Journal Article
Journal of Cell Science, ISSN 0021-9533, 08/2012, Volume 125, Issue 16, pp. 3827 - 3839
Integrins are the primary receptors of cells adhering to the extracellular matrix, and play key roles in various cellular processes including migration,...
Integrin | Endocytic recycling | Cell migration | SNARE | TUMOR PROGRESSION | CHO-CELLS | MEDIATED CLEAVAGE | HOMOTYPIC FUSION | MOLECULAR PROFILES | LAMININ ISOFORMS | CELL BIOLOGY | SNARE COMPLEX | TRANS-GOLGI NETWORK | GENE-EXPRESSION | EARLY ENDOSOMES | Immunohistochemistry | Vesicle-Associated Membrane Protein 3 - metabolism | Humans | Cell Growth Processes - physiology | Integrins - metabolism | Endosomes - metabolism | Protein Transport | Chemotaxis - physiology | Transfection | Qa-SNARE Proteins - biosynthesis | Cell Adhesion - physiology | Qa-SNARE Proteins - metabolism | Cell Line, Tumor | Qa-SNARE Proteins - genetics | HeLa Cells | SNARE Proteins - metabolism | Vesicle-Associated Membrane Protein 3 - genetics
Integrin | Endocytic recycling | Cell migration | SNARE | TUMOR PROGRESSION | CHO-CELLS | MEDIATED CLEAVAGE | HOMOTYPIC FUSION | MOLECULAR PROFILES | LAMININ ISOFORMS | CELL BIOLOGY | SNARE COMPLEX | TRANS-GOLGI NETWORK | GENE-EXPRESSION | EARLY ENDOSOMES | Immunohistochemistry | Vesicle-Associated Membrane Protein 3 - metabolism | Humans | Cell Growth Processes - physiology | Integrins - metabolism | Endosomes - metabolism | Protein Transport | Chemotaxis - physiology | Transfection | Qa-SNARE Proteins - biosynthesis | Cell Adhesion - physiology | Qa-SNARE Proteins - metabolism | Cell Line, Tumor | Qa-SNARE Proteins - genetics | HeLa Cells | SNARE Proteins - metabolism | Vesicle-Associated Membrane Protein 3 - genetics
Journal Article
Virus Research, ISSN 0168-1702, 04/2013, Volume 173, Issue 1, pp. 42 - 57
► ASFV entry by dynamin-dependent and clathrin-mediated endocytosis or macropinocytosis. ► Endosomal maturation, Rab7 GTPase and acidification of late...
PIKfyve | Clathrin | Rab GTPases | Early endosome | ER stress | African swine fever virus | Autophagy | Virus entry | HDAC6 | Cholesterol | Unfolded protein response | PP1 | eIF2α | Endocytosis | PI3K | Dynamin | Bcl2 | Beclin1 | Late endosome | Caspases | ASFV | Macropinocytosis | Apoptosis | EIF2α | STRUCTURAL PROTEIN | CYTOPLASMIC DYNEIN | BCL-2 HOMOLOG | ALPHA-SUBUNIT | eIF2 alpha | IN-VITRO | VIROLOGY | CATALYTIC SUBUNIT | MEMBRANE-PROTEIN | INITIATION-FACTOR 2 | HERPES-SIMPLEX-VIRUS | ENDOPLASMIC-RETICULUM | Host-Pathogen Interactions | Animals | Virus Replication | Cell Survival | Swine | African Swine Fever Virus - physiology | Virus Uncoating | Virus Internalization | Virus diseases | Hog cholera | G proteins
PIKfyve | Clathrin | Rab GTPases | Early endosome | ER stress | African swine fever virus | Autophagy | Virus entry | HDAC6 | Cholesterol | Unfolded protein response | PP1 | eIF2α | Endocytosis | PI3K | Dynamin | Bcl2 | Beclin1 | Late endosome | Caspases | ASFV | Macropinocytosis | Apoptosis | EIF2α | STRUCTURAL PROTEIN | CYTOPLASMIC DYNEIN | BCL-2 HOMOLOG | ALPHA-SUBUNIT | eIF2 alpha | IN-VITRO | VIROLOGY | CATALYTIC SUBUNIT | MEMBRANE-PROTEIN | INITIATION-FACTOR 2 | HERPES-SIMPLEX-VIRUS | ENDOPLASMIC-RETICULUM | Host-Pathogen Interactions | Animals | Virus Replication | Cell Survival | Swine | African Swine Fever Virus - physiology | Virus Uncoating | Virus Internalization | Virus diseases | Hog cholera | G proteins
Journal Article