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  1. Book ; Online ; Thesis: Nachahmungsschutz und Schutzrechtskumulation am Beispiel von Modekreationen

    Farkas, Thomas [Verfasser]

    2016  

    Author's details Thomas Farkas
    Keywords Recht ; Law
    Subject code sg340
    Language German
    Publisher Nomos Verlagsgesellschaft mbH & Co. KG
    Publishing place Baden-Baden
    Document type Book ; Online ; Thesis
    ISBN 978-3-8452-6649-7 ; 3-8452-6649-X
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  2. Article ; Online: Structural determinants underlying permeant discrimination of the Cx43 hemichannel.

    Nielsen, Brian Skriver / Zonta, Francesco / Farkas, Thomas / Litman, Thomas / Nielsen, Morten Schak / MacAulay, Nanna

    The Journal of biological chemistry

    2019  Volume 294, Issue 45, Page(s) 16789–16803

    Abstract: Connexin (Cx) gap junction channels comprise two hemichannels in neighboring cells, and their permeability is well-described, but permeabilities of the single Cx hemichannel remain largely unresolved. Moreover, determination of isoform-specific Cx ... ...

    Abstract Connexin (Cx) gap junction channels comprise two hemichannels in neighboring cells, and their permeability is well-described, but permeabilities of the single Cx hemichannel remain largely unresolved. Moreover, determination of isoform-specific Cx hemichannel permeability is challenging because of concurrent expression of other channels with similar permeability profiles and inhibitor sensitivities. The mammalian Cx hemichannels Cx30 and Cx43 are gated by extracellular divalent cations, removal of which promotes fluorescent dye uptake in both channels but atomic ion conductance only through Cx30. To determine the molecular determinants of this difference, here we employed chimeras and mutagenesis of predicted pore-lining residues in Cx43. We expressed the mutated channels in
    MeSH term(s) Amino Acid Sequence ; Cell Membrane/metabolism ; Connexin 43/chemistry ; Connexin 43/metabolism ; Electrophysiological Phenomena ; Molecular Dynamics Simulation ; Permeability ; Porosity ; Protein Conformation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Substrate Specificity
    Chemical Substances Connexin 43 ; Protein Isoforms
    Language English
    Publishing date 2019-09-25
    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.RA119.007732
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: C10orf99/GPR15L Regulates Proinflammatory Response of Keratinocytes and Barrier Formation of the Skin.

    Dainichi, Teruki / Nakano, Yuri / Doi, Hiromi / Nakamizo, Satoshi / Nakajima, Saeko / Matsumoto, Reiko / Farkas, Thomas / Wong, Pui Mun / Narang, Vipin / Moreno Traspas, Ricardo / Kawakami, Eiryo / Guttman-Yassky, Emma / Dreesen, Oliver / Litman, Thomas / Reversade, Bruno / Kabashima, Kenji

    Frontiers in immunology

    2022  Volume 13, Page(s) 825032

    Abstract: The epidermis, outermost layer of the skin, forms a barrier and is involved in innate and adaptive immunity in an organism. Keratinocytes participate in all these three protective processes. However, a regulator of keratinocyte protective responses ... ...

    Abstract The epidermis, outermost layer of the skin, forms a barrier and is involved in innate and adaptive immunity in an organism. Keratinocytes participate in all these three protective processes. However, a regulator of keratinocyte protective responses against external dangers and stresses remains elusive. We found that upregulation of the orphan gene
    MeSH term(s) Animals ; Antimicrobial Cationic Peptides/metabolism ; DNA-Binding Proteins/metabolism ; Dermatitis, Atopic/metabolism ; Humans ; Inflammation/genetics ; Inflammation/metabolism ; Keratinocytes/metabolism ; Ligands ; Mice ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism
    Chemical Substances Antimicrobial Cationic Peptides ; C10orf99 protein, human ; DNA-Binding Proteins ; Ligands ; Receptors, G-Protein-Coupled
    Language English
    Publishing date 2022-02-22
    Publishing country Switzerland
    Document type 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.2022.825032
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  4. Article ; Online: Identification of small molecule inhibitors of phosphatidylinositol 3-kinase and autophagy.

    Farkas, Thomas / Daugaard, Mads / Jäättelä, Marja

    The Journal of biological chemistry

    2011  Volume 286, Issue 45, Page(s) 38904–38912

    Abstract: Macroautophagy (hereafter autophagy) is a lysosomal catabolic pathway that controls cellular homeostasis and survival. It has recently emerged as an attractive target for the treatment of a variety of degenerative diseases and cancer. The targeting of ... ...

    Abstract Macroautophagy (hereafter autophagy) is a lysosomal catabolic pathway that controls cellular homeostasis and survival. It has recently emerged as an attractive target for the treatment of a variety of degenerative diseases and cancer. The targeting of autophagy has, however, been hampered by the lack of specific small molecule inhibitors. Thus, we screened two small molecule kinase inhibitor libraries for inhibitors of rapamycin-induced autophagic flux. The three most potent inhibitors identified conferred profound inhibition of autophagic flux by inhibiting the formation of autophagosomes. Notably, the autophagy inhibitory effects of all three compounds were independent of their established kinase targets, i.e. ataxia telangiectasia mutated for KU55933, protein kinase C for Gö6976, and Janus kinase 3 for Jak3 inhibitor VI. Instead, we identified phosphatidylinositol 3-kinase (PtdIns3K) as a direct target of KU55933 and Gö6976. Importantly, and in contrast to the currently available inhibitors of autophagosome formation (e.g. 3-methyladenine), none of the three compounds inhibited the cell survival promoting class I phosphoinositide 3-kinase-Akt signaling at the concentrations required for effective autophagy inhibition. Accordingly, they proved to be valuable tools for investigations of autophagy-associated cell death and survival. Employing KU55399, we demonstrated that autophagy protects amino acid-starved cells against both apoptosis and necroptosis. Taken together, our data introduce new possibilities for the experimental study of autophagy and can form a basis for the development of clinically relevant autophagy inhibitors.
    MeSH term(s) Autophagy/drug effects ; Autophagy/genetics ; Carbazoles/pharmacology ; Cell Line, Tumor ; Enzyme Inhibitors/pharmacology ; Female ; Humans ; Morpholines/pharmacology ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoinositide-3 Kinase Inhibitors ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Pyrones/pharmacology ; Signal Transduction/drug effects ; Signal Transduction/genetics
    Chemical Substances 2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one ; Carbazoles ; Enzyme Inhibitors ; Morpholines ; Phosphoinositide-3 Kinase Inhibitors ; Pyrones ; Go 6976 (136194-77-9) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
    Language English
    Publishing date 2011-09-19
    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.M111.269134
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.

    Puustinen, Pietri / Keldsbo, Anne / Corcelle-Termeau, Elisabeth / Ngoei, Kevin / Sønder, Stine L / Farkas, Thomas / Kaae Andersen, Klaus / Oakhill, Jon S / Jäättelä, Marja

    Autophagy

    2020  Volume 16, Issue 10, Page(s) 1871–1888

    Abstract: Macroautophagy/autophagy is a central component of the cytoprotective cellular stress response. To enlighten stress-induced autophagy signaling, we screened a human kinome siRNA library for regulators of autophagic flux in MCF7 human breast carcinoma ... ...

    Abstract Macroautophagy/autophagy is a central component of the cytoprotective cellular stress response. To enlighten stress-induced autophagy signaling, we screened a human kinome siRNA library for regulators of autophagic flux in MCF7 human breast carcinoma cells and identified the catalytic subunit of DNA-dependent protein kinase PRKDC/DNA-PKcs as a positive regulator of basal and DNA damage-induced autophagy. Analysis of autophagy-regulating signaling cascades placed PRKDC upstream of the AMP-dependent protein kinase (AMPK) complex and ULK1 kinase. In normal culture conditions, PRKDC interacted with the AMPK complex and phosphorylated its nucleotide-sensing γ1 subunit PRKAG1/AMPKγ1 at Ser192 and Thr284, both events being significantly reduced upon the activation of the AMPK complex. Alanine substitutions of PRKDC phosphorylation sites in PRKAG1 reduced AMPK complex activation without affecting its nucleotide sensing capacity. Instead, the disturbance of PRKDC-mediated phosphorylation of PRKAG1 inhibited the lysosomal localization of the AMPK complex and its starvation-induced association with STK11 (serine/threonine kinase 11). Taken together, our data suggest that PRKDC-mediated phosphorylation of PRKAG1 primes AMPK complex to the lysosomal activation by STK11 in cancer cells thereby linking DNA damage response to autophagy and cellular metabolism.
    MeSH term(s) AMP-Activated Protein Kinases/metabolism ; Autophagy ; Binding Sites ; Cell Line, Tumor ; Cytosol/metabolism ; DNA Damage ; DNA-Activated Protein Kinase/metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Lysosomes/enzymology ; Lysosomes/metabolism ; MCF-7 Cells ; Phagocytosis ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering/metabolism ; Signal Transduction/genetics
    Chemical Substances RNA, Small Interfering ; STK11 protein, human (EC 2.7.1.-) ; DNA-Activated Protein Kinase (EC 2.7.11.1) ; PRKAG1 protein, human (EC 2.7.11.1) ; PRKDC protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
    Language English
    Publishing date 2020-01-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2019.1710430
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  6. Article ; Online: Identification of novel autophagy regulators by a luciferase-based assay for the kinetics of autophagic flux.

    Farkas, Thomas / Høyer-Hansen, Maria / Jäättelä, Marja

    Autophagy

    2009  Volume 5, Issue 7, Page(s) 1018–1025

    Abstract: Macroautophagy (hereafter referred to as autophagy) has recently emerged as an attractive target for the treatment of various degenerative diseases and cancer. The discovery of effective pharmaceutical regulators of autophagy has, however, been hindered ... ...

    Abstract Macroautophagy (hereafter referred to as autophagy) has recently emerged as an attractive target for the treatment of various degenerative diseases and cancer. The discovery of effective pharmaceutical regulators of autophagy has, however, been hindered by a lack of feasible assay systems for autophagic flux. Here, we present a luciferase-based reporter assay that measures autophagic flux in real time in living cells and demonstrate that this assay system is apt for the detection of dose- and stimulus-dependent differences in autophagy kinetics. Furthermore, by screening a small molecule kinase inhibitor library containing 80 compounds we identified 12 compounds as inducers of autophagic flux. Importantly, six inhibitors of the class I phosphoinositide 3-kinase -- protein kinase B -- mammalian target of rapamycin complex 1 axis, the central signaling pathway repressing autophagy, scored as autophagy inducers adequately validating the screen. We conclude that the assay system presented here allows easy and rapid monitoring of autophagy kinetics and is suitable for screening of small molecule libraries.
    MeSH term(s) Animals ; Anti-Bacterial Agents/metabolism ; Antineoplastic Agents, Phytogenic/metabolism ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Autophagy/physiology ; Beclin-1 ; Biological Assay/methods ; Cells, Cultured ; Enzyme Inhibitors/metabolism ; Etoposide/metabolism ; Fibroblasts/cytology ; Fibroblasts/physiology ; Genes, Reporter ; Humans ; Luciferases/genetics ; Luciferases/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; RNA, Small Interfering/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Sirolimus/metabolism
    Chemical Substances Anti-Bacterial Agents ; Antineoplastic Agents, Phytogenic ; Apoptosis Regulatory Proteins ; BECN1 protein, human ; Beclin-1 ; Enzyme Inhibitors ; LC3 protein, rat ; Membrane Proteins ; Microtubule-Associated Proteins ; RNA, Small Interfering ; Recombinant Fusion Proteins ; Etoposide (6PLQ3CP4P3) ; Luciferases (EC 1.13.12.-) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2009-10-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.5.7.9443
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  7. Article ; Online: Correction for Gyrd-Hansen et al., "Apoptosome-Independent Activation of the Lysosomal Cell Death Pathway by Caspase-9".

    Gyrd-Hansen, Mads / Farkas, Thomas / Fehrenbacher, Nicole / Bastholm, Lone / Høyer-Hansen, Maria / Elling, Folmer / Wallach, David / Flavell, Richard / Kroemer, Guido / Nylandsted, Jesper / Jäättelä, Marja

    Molecular and cellular biology

    2017  Volume 38, Issue 2

    Language English
    Publishing date 2017-12-29
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00563-17
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  8. Article ; Online: Sensitive detection of lysosomal membrane permeabilization by lysosomal galectin puncta assay.

    Aits, Sonja / Kricker, Jennifer / Liu, Bin / Ellegaard, Anne-Marie / Hämälistö, Saara / Tvingsholm, Siri / Corcelle-Termeau, Elisabeth / Høgh, Søren / Farkas, Thomas / Holm Jonassen, Anna / Gromova, Irina / Mortensen, Monika / Jäättelä, Marja

    Autophagy

    2015  Volume 11, Issue 8, Page(s) 1408–1424

    Abstract: Lysosomal membrane permeabilization (LMP) contributes to tissue involution, degenerative diseases, and cancer therapy. Its investigation has, however, been hindered by the lack of sensitive methods. Here, we characterize and validate the detection of ... ...

    Abstract Lysosomal membrane permeabilization (LMP) contributes to tissue involution, degenerative diseases, and cancer therapy. Its investigation has, however, been hindered by the lack of sensitive methods. Here, we characterize and validate the detection of galectin puncta at leaky lysosomes as a highly sensitive and easily manageable assay for LMP. LGALS1/galectin-1 and LGALS3/galectin-3 are best suited for this purpose due to their widespread expression, rapid translocation to leaky lysosomes and availability of high-affinity antibodies. Galectin staining marks individual leaky lysosomes early during lysosomal cell death and is useful when defining whether LMP is a primary or secondary cause of cell death. This sensitive method also reveals that cells can survive limited LMP and confirms a rapid formation of autophagic structures at the site of galectin puncta. Importantly, galectin staining detects individual leaky lysosomes also in paraffin-embedded tissues allowing us to demonstrate LMP in tumor xenografts in mice treated with cationic amphiphilic drugs and to identify a subpopulation of lysosomes that initiates LMP in involuting mouse mammary gland. The use of ectopic fluorescent galectins renders the galectin puncta assay suitable for automated screening and visualization of LMP in live cells and animals. Thus, the lysosomal galectin puncta assay opens up new possibilities to study LMP in cell death and its role in other cellular processes such as autophagy, senescence, aging, and inflammation.
    MeSH term(s) Animals ; Apoptosis ; Autophagy ; Blood Proteins ; Breast/pathology ; Caenorhabditis elegans/physiology ; Cell Death ; Cell Line, Tumor ; Cell Membrane Permeability ; Cell Survival ; Female ; Galectin 1/metabolism ; Galectin 3/metabolism ; Galectins/chemistry ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Humans ; Inflammation ; Intracellular Membranes/metabolism ; Lysosomes/metabolism ; MCF-7 Cells ; Mice ; Microscopy, Confocal ; Neoplasm Transplantation ; Protein Transport
    Chemical Substances Blood Proteins ; Galectin 1 ; Galectin 3 ; Galectins ; LGALS1 protein, human ; LGALS3 protein, human ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2015-06-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2015.1063871
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  9. Article ; Online: microRNA-101 is a potent inhibitor of autophagy.

    Frankel, Lisa B / Wen, Jiayu / Lees, Michael / Høyer-Hansen, Maria / Farkas, Thomas / Krogh, Anders / Jäättelä, Marja / Lund, Anders H

    The EMBO journal

    2011  Volume 30, Issue 22, Page(s) 4628–4641

    Abstract: Autophagy is an evolutionarily conserved mechanism of cellular self-digestion in which proteins and organelles are degraded through delivery to lysosomes. Defects in this process are implicated in numerous human diseases including cancer. To further ... ...

    Abstract Autophagy is an evolutionarily conserved mechanism of cellular self-digestion in which proteins and organelles are degraded through delivery to lysosomes. Defects in this process are implicated in numerous human diseases including cancer. To further elucidate regulatory mechanisms of autophagy, we performed a functional screen in search of microRNAs (miRNAs), which regulate the autophagic flux in breast cancer cells. In this study, we identified the tumour suppressive miRNA, miR-101, as a potent inhibitor of basal, etoposide- and rapamycin-induced autophagy. Through transcriptome profiling, we identified three novel miR-101 targets, STMN1, RAB5A and ATG4D. siRNA-mediated depletion of these genes phenocopied the effect of miR-101 overexpression, demonstrating their importance in autophagy regulation. Importantly, overexpression of STMN1 could partially rescue cells from miR-101-mediated inhibition of autophagy, indicating a functional importance for this target. Finally, we show that miR-101-mediated inhibition of autophagy can sensitize breast cancer cells to 4-hydroxytamoxifen (4-OHT)-mediated cell death. Collectively, these data establish a novel link between two highly important and rapidly growing research fields and present a new role for miR-101 as a key regulator of autophagy.
    MeSH term(s) Autophagy ; Autophagy-Related Proteins ; Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Cell Line, Tumor ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Etoposide/pharmacology ; Female ; Gene Expression Profiling ; Gene Expression Regulation ; Humans ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Oligonucleotide Array Sequence Analysis ; RNA Interference ; RNA, Small Interfering ; Sirolimus/pharmacology ; Stathmin/biosynthesis ; Stathmin/genetics ; Stathmin/metabolism ; Tamoxifen/analogs & derivatives ; Tamoxifen/pharmacology ; rab5 GTP-Binding Proteins/genetics ; rab5 GTP-Binding Proteins/metabolism
    Chemical Substances Autophagy-Related Proteins ; MIRN101 microRNA, human ; MicroRNAs ; RNA, Small Interfering ; STMN1 protein, human ; Stathmin ; Tamoxifen (094ZI81Y45) ; afimoxifene (17197F0KYM) ; Etoposide (6PLQ3CP4P3) ; ATG4D protein, human (EC 3.4.22.-) ; Cysteine Endopeptidases (EC 3.4.22.-) ; rab5 GTP-Binding Proteins (EC 3.6.5.2) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2011-09-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2011.331
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  10. Article ; Online: A comprehensive siRNA screen for kinases that suppress macroautophagy in optimal growth conditions.

    Szyniarowski, Piotr / Corcelle-Termeau, Elisabeth / Farkas, Thomas / Høyer-Hansen, Maria / Nylandsted, Jesper / Kallunki, Tuula / Jäättelä, Marja

    Autophagy

    2011  Volume 7, Issue 8, Page(s) 892–903

    Abstract: Macroautophagy is a catabolic process that maintains cellular homeostasis and protects cells against various external stresses including starvation. Except for the identification of the Akt-mTORC1 pathway as a major negative regulator, little is known ... ...

    Abstract Macroautophagy is a catabolic process that maintains cellular homeostasis and protects cells against various external stresses including starvation. Except for the identification of the Akt-mTORC1 pathway as a major negative regulator, little is known about signaling networks that control macroautophagy under optimal growth conditions. Therefore, we screened a human kinome siRNA library for siRNAs that increase the number of autophagosomes in normally growing MCF-7 human breast carcinoma cells, and identified 10 kinases as regulators of constitutive macroautophagy. Further analysis of these kinases with respect to the autophagic flux, kinase signaling and endolysosomal function identified WNK2 as a positive regulator of autophagosome maturation and nine others as macroautophagy inhibitors. The depletion of MK2, PACSIN1, DAPK2, CDKL3 and SCYL1 functioned upstream of Akt-mTORC1 pathway, whereas CSNK1A1, BUB1, PKLR and NEK4 suppressed autophagosome formation downstream or independent of mTORC1. Importantly, all identified kinases except for BUB1 regulated macroautophagy also in immortalized MCF-10A breast epithelial cells. The kinases identified here shed light to the complex regulation of macroautophagy and open new possibilities for its pharmacological manipulation.
    MeSH term(s) Autophagy ; Breast/pathology ; Cell Line, Tumor ; Cell Proliferation ; Endocytosis ; Epithelial Cells/metabolism ; Female ; Genetic Testing/methods ; Humans ; Lysosomes/metabolism ; Mechanistic Target of Rapamycin Complex 1 ; Microtubule-Associated Proteins/metabolism ; Multiprotein Complexes ; Phosphatidylinositol 3-Kinases ; Phosphotransferases/metabolism ; Protein Transport ; Proteins/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; RNA, Small Interfering/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases
    Chemical Substances MAP1LC3A protein, human ; Microtubule-Associated Proteins ; Multiprotein Complexes ; Proteins ; RNA, Small Interfering ; Phosphotransferases (EC 2.7.-) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
    Language English
    Publishing date 2011-08-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.7.8.15770
    Database MEDical Literature Analysis and Retrieval System OnLINE

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