نتائج البحث - "Endosomes."

1

The N- or C-terminal cytoplasmic regions of P4-ATPases determine their cellular localization

المؤلفون: Hye-Won Shin, Tomoki Naito, Ryo Shigetomi, Kazuhisa Nakayama, Yusuke Kosugi, Hiroyuki Takatsu, Sayuri Okamoto

المساهمون: Lee Kong Chian School of Medicine (LKCMedicine)

المصدر: Molecular Biology of the Cell

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95d57e3f0ef8abf88b8656d9d8cec0eb
http://hdl.handle.net/2433/260999

2

The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory protein and confers differential cargo sorting

المؤلفون: Elizabeth Conibear, Michael Davey, Beverly Wendland, Shawn T. Whitfield, Lymarie Maldonado-Báez, Nandini Raghuram, Helen E. Burston, Björn D. M. Bean

المصدر: Molecular Biology of the Cell

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e37c876ff35fd99fd525badec16b580
https://doi.org/10.1091/mbc.e15-09-0621

3

GGA3 mediates TrkA endocytic recycling to promote sustained Akt phosphorylation and cell survival

المؤلفون: Christine Lavoie, Xuezhi Li, Pierre Lavigne

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: animal structures, Cell Survival, Endosome, Golgi Apparatus, Endocytic recycling, Endosomes, Biology, Tropomyosin receptor kinase A, PC12 Cells, 12. Responsible consumption, 03 medical and health sciences, 0302 clinical medicine, Cell Movement, Animals, Humans, Low-affinity nerve growth factor receptor, Amino Acid Sequence, Phosphorylation, Receptor, trkA, Molecular Biology, Protein kinase B, 030304 developmental biology, 0303 health sciences, ADP-Ribosylation Factors, Cell Membrane, Biological Transport, Articles, Cell Biology, Rats, Cell biology, Transport protein, Oncogene Protein v-akt, Adaptor Proteins, Vesicular Transport, Protein Transport, HEK293 Cells, nervous system, ADP-Ribosylation Factor 6, Membrane Trafficking, Signal transduction, 030217 neurology & neurosurgery, Protein Binding, Signal Transduction

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf06687afe63c9798b87b4ff73471469
https://doi.org/10.1091/mbc.e15-02-0087

4

KIF5B transports BNIP-2 to regulate p38 mitogen-activated protein kinase activation and myoblast differentiation

المؤلفون: Feiya Wang, Hao Ren, Li Li Chew, Boon Chuan Low, Peng Yi, Hongwei Ouyang, Yi Ting Zhou, Xiaoxia Cong, Ziwang Zhang, Yan Luo, Liling Zheng

المصدر: Molecular Biology of the Cell

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e194d30221dc2ef123668dc1858b5a2
https://doi.org/10.1091/mbc.e14-03-0797

5

Notch signaling from the endosome requires a conserved dileucine motif

المؤلفون: Li Zheng, Nicole C. Waxmonsky, Sean D. Conner, Erika B. Sorensen, Cosmo A. Saunders

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: Endosome, Amino Acid Motifs, Molecular Sequence Data, Notch signaling pathway, Endosomes, Protein Sorting Signals, Biology, Mice, 03 medical and health sciences, 0302 clinical medicine, Lysosome, medicine, Animals, Humans, Amino Acid Sequence, Receptor, Notch1, Molecular Biology, Conserved Sequence, rab5 GTP-Binding Proteins, 030304 developmental biology, 0303 health sciences, Dipeptides, Articles, Cell Biology, Cell biology, Transport protein, Protein Transport, medicine.anatomical_structure, Amino Acid Substitution, Notch proteins, Membrane Trafficking, Hes3 signaling axis, Endosomal transport, Mutagenesis, Site-Directed, Amyloid Precursor Protein Secretases, Signal transduction, Lysosomes, 030217 neurology & neurosurgery, HeLa Cells, Signal Transduction

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c5a1b34d3ef4fce7a1d1c10a25b14e1
https://doi.org/10.1091/mbc.e12-02-0081

6

Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins

المؤلفون: Gregory S. Payne, Giancarlo Costaguta, Sabine Gorynia, Duilio Cascio, Lydia Daboussi, Todd C. Lorenz

المساهمون: Glick, Benjamin S

المصدر: Molecular biology of the cell, vol 23, iss 22
Molecular Biology of the Cell

مصطلحات موضوعية: Protein Structure, Saccharomyces cerevisiae Proteins, 1.1 Normal biological development and functioning, Clathrin adaptor complex, Molecular Sequence Data, Small G Protein, Endosomes, GTPase, Crystallography, X-Ray, Medical and Health Sciences, Clathrin, Clathrin coat, Conserved sequence, 03 medical and health sciences, 0302 clinical medicine, Underpinning research, Protein Interaction Mapping, Amino Acid Sequence, Molecular Biology, Conserved Sequence, Monomeric GTP-Binding Proteins, 030304 developmental biology, 0303 health sciences, Crystallography, biology, Adaptor Proteins, Biological Transport, Articles, Cell Biology, Biological Sciences, Protein Structure, Tertiary, Cell biology, Vesicular Transport, Adaptor Proteins, Vesicular Transport, Membrane Trafficking, rab GTP-Binding Proteins, X-Ray, biology.protein, ADP-Ribosylation Factor 1, Clathrin adaptor proteins, Generic health relevance, Rab, Sequence Alignment, Tertiary, 030217 neurology & neurosurgery, trans-Golgi Network, Developmental Biology

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f943e7d499f8ab9ef86ef821ff211bc6
https://doi.org/10.1091/mbc.e12-07-0507

7

Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer

المؤلفون: Da Jia, Timothy S. Gomez, Michael K. Rosen, Daniel D. Billadeau

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: Repetitive Sequences, Amino Acid, SNX27, Retromer, Endosome, Amino Acid Motifs, Molecular Sequence Data, Vesicular Transport Proteins, Endosomes, macromolecular substances, Plasma protein binding, Biology, WASH complex, 03 medical and health sciences, VPS35, 0302 clinical medicine, Animals, Humans, Immunoprecipitation, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, 0303 health sciences, Binding Sites, Microscopy, Confocal, Microfilament Proteins, Articles, Cell Biology, Actins, Transport protein, Cell biology, Luminescent Proteins, Protein Transport, Membrane Trafficking, VPS29, Mutation, Cattle, Electrophoresis, Polyacrylamide Gel, 030217 neurology & neurosurgery, HeLa Cells, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cb2ae95856b1afe09b844a8b157aab5
https://doi.org/10.1091/mbc.e11-12-1059

8

The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p inSaccharomyces cerevisiae

المؤلفون: Tom H. Stevens, Gregory C. Finnigan, Victor Hanson-Smith, Benjamin D. Houser, Hae J. Park

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: Vacuolar Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins, Endosome, Protein subunit, Molecular Sequence Data, Saccharomyces cerevisiae, Golgi Apparatus, Endosomes, Vacuole, Biology, Gene Knockout Techniques, 03 medical and health sciences, symbols.namesake, hemic and lymphatic diseases, Consensus Sequence, Organelle, Protein Isoforms, V-ATPase, Amino Acid Sequence, Molecular Biology, reproductive and urinary physiology, Late endosome, 030304 developmental biology, 0303 health sciences, 030302 biochemistry & molecular biology, Intracellular Membranes, Articles, Cell Biology, Golgi apparatus, biology.organism_classification, female genital diseases and pregnancy complications, Recombinant Proteins, Protein Structure, Tertiary, Protein Subunits, Protein Transport, Biochemistry, Membrane Trafficking, Vacuoles, symbols, Sequence Alignment, Gene Deletion

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd95a0baf153178397ba3a8e614160f7
https://doi.org/10.1091/mbc.e11-03-0244

9

TheCaenorhabditis elegansGARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology

المؤلفون: Nikhil Sasidharan, Mandy Hannemann, Jan Hegermann, S. A. Rensing, Markus Zweckstetter, Min-Kyu Cho, Stefan Eimer, Sabine Koenig, L. Luo, Michael Ailion

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: Endosome, Protein subunit, Molecular Sequence Data, Vesicular Transport Proteins, Golgi Apparatus, Exocyst, Endosomes, Conserved sequence, 03 medical and health sciences, symbols.namesake, Two-Hybrid System Techniques, Animals, Amino Acid Sequence, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Transport Vesicles, Molecular Biology, Conserved Sequence, Phylogeny, 030304 developmental biology, SNARE complex assembly, 0303 health sciences, biology, 030302 biochemistry & molecular biology, GARP complex, Articles, Cell Biology, Golgi apparatus, biology.organism_classification, Cell biology, Golgi-associated retrograde protein (GARP) complex, lysosomal defects, Membrane Trafficking, Multiprotein Complexes, symbols, Lysosomes, SNARE Proteins

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c51c90adf59ea0941d92f29425fd6e4
https://doi.org/10.1091/mbc.e10-06-0493

10

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis

المؤلفون: Takuma Kishimoto, Helena Friesen, Harvey T. McMahon, Frank Sicheri, Christoph F. Kurat, Ji-Young Youn, Wei Ye, Sepp D. Kohlwein, Derek F. Ceccarelli, William Mike Henne, Brenda J. Andrews

المصدر: Molecular Biology of the Cell

مصطلحات موضوعية: Saccharomyces cerevisiae Proteins, Surface Properties, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Endosomes, Saccharomyces cerevisiae, Biology, Endocytosis, Models, Biological, Protein Structure, Secondary, Structure-Activity Relationship, 03 medical and health sciences, 0302 clinical medicine, BAR domain, Amino Acid Sequence, Protein Structure, Quaternary, Molecular Biology, 030304 developmental biology, Sphingolipids, 0303 health sciences, Cell Membrane, Microfilament Proteins, Articles, Cell Biology, Yeast, Protein Structure, Tertiary, Cell biology, Cytoskeletal Proteins, Protein Transport, Membrane Trafficking, Mutation, Mutant Proteins, 030217 neurology & neurosurgery, Function (biology), Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::867d14c0eed054f2a56a8923d729eecc
https://doi.org/10.1091/mbc.e10-03-0181

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