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by Schormair, Barbara and Zhao, Chen and Bell, Steven and Bell, Robert K and Tilch, Erik and Salminen, Aaro V and Pütz, Benno and Dauvilliers, Yves and Stefani, Ambra and Högl, Birgit and Poewe, Werner and Kemlink, David and Sonka, Karel and Bachmann, Cornelius G and Paulus, Walter and Trenkwalder, Claudia and Oertel, Wolfgang H and Hornyak, Magdolna and Teder-Laving, Maris and Metspalu, Andres and Hadjigeorgiou, Georgios M and Polo, Olli and Fietze, Ingo and Ross, Owen A and Wszolek, Zbigniew and Butterworth, Adam S and Soranzo, Nicole and Ouwehand, Willem H and Roberts, David J and Danesh, John and Allen, Richard P and Earley, Christopher J and Ondo, William G and Xiong, Lan and Montplaisir, Jacques and Gan-Or, Ziv and Perola, Markus and Vodicka, Pavel and Dina, Christian and Franke, Andre and Tittmann, Lukas and Stewart, Alexandre F R and Shah, Svati H and Gieger, Christian and Peters, Annette and Rouleau, Guy A and Berger, Klaus and Oexle, Konrad and Di Angelantonio, Emanuele and Hinds, David A and Müller-Myhsok, Bertram and Winkelmann, Juliane and Balkau, B and Ducimetière, P and Eschwège, E and Rancière, F and Alhenc-Gelas, F and Gallois, Y and Girault, A and Fumeron, F and Marre, M and Roussel, R and Bonnet, F and Bonnefond, A and Cauchi, S and Froguel, P and Cogneau, J and Born, C and Caces, E and Cailleau, M and Lantieri, O and Moreau, JG and Rakotozafy, F and Tichet, J and Vol, S and Agee, Michelle and Alipanahi, Babak and Auton, Adam and Bryc, Katarzyna and Elson, Sarah L and Fontanillas, Pierre and Furlotte, Nicholas A and Hromatka, Bethann S and Huber, Karen E and Kleinman, Aaron and Litterman, Nadia K and McIntyre, Matthew H and Mountain, Joanna L and Northover, Carrie AM and Pitts, Steven J and Sathirapongsasuti, J Fah and Sazonova, Olga V and Shelton, Janie F and Shringarpure, Suyash and Tian, Chao and Tung, Joyce Y and Vacic, Vladimir and Wilson, Catherine H and Collaboration 23andMe Res Team and DESIR Study Grp and DESIR study group and 23andMe Research Team
The Lancet Neurology, ISSN 1474-4422, 11/2017, Volume 16, Issue 11, pp. 898 - 907
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2010, Volume 5, Issue 2, p. e9344
Background: Forsters resonance energy transfer (FRET) microscopy is widely used for the analysis of protein interactions in intact cells. However, FRET... 
DOWN-MODULATION | ACTIVATION | BINDS | MULTIDISCIPLINARY SCIENCES | VIRUS TYPE-1 NEF | VPU PROTEIN | RESONANCE ENERGY-TRANSFER | DEGRADATION | FLUORESCENT PROTEIN | HIV-1 VPU | EXPRESSION | Flow Cytometry - methods | Immunoprecipitation | Membrane Glycoproteins - metabolism | Humans | GPI-Linked Proteins | Gene Products, nef - genetics | Antigens, CD - genetics | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Antigens, CD - metabolism | Transfection | Gene Products, nef - metabolism | Cell Line | HIV-1 - metabolism | Jurkat Cells | Viral Regulatory and Accessory Proteins - genetics | Viral Proteins - genetics | Binding Sites - genetics | Viral Regulatory and Accessory Proteins - metabolism | Membrane Glycoproteins - genetics | Human Immunodeficiency Virus Proteins - metabolism | Microscopy, Confocal | Protein Interaction Mapping - methods | Animals | Protein Binding | Recombinant Fusion Proteins - genetics | Fluorescence Resonance Energy Transfer - methods | Human Immunodeficiency Virus Proteins - genetics | Luminescent Proteins - genetics | Simian Immunodeficiency Virus - metabolism | HeLa Cells | Mutation | Luminescent Proteins - metabolism | Proteins | Health aspects | Protein-protein interactions | Flow cytometry | Target recognition | Medical treatment | Cloning | Viruses | Assaying | Virology | Studies | Cytometry | Immunology | Nef protein | Microscopy | Human immunodeficiency virus--HIV | Cells (biology) | Proteomics | Fluorescence resonance energy transfer | Localization | Protein interaction | Energy transfer | HIV | Human immunodeficiency virus
Journal Article
Journal Article
Journal Article
Prostate, ISSN 0270-4137, 2009, Volume 69, Issue 15, pp. 1683 - 1693
BACKGROUND: According to the cancer stem cell hypothesis, tumor growth is sustained by a subpopulation of cancer stem/progenitor-like cells. Self-renewal and... 
self‐renewal | PSCA | prostaspheres | cancer stem/progenitor‐like cells | CD49f | Cancer stem/progenitor-like cells | Self-renewal | Prostaspheres | POPULATION | PROSPECTIVE IDENTIFICATION | self-renewal | TUMORS | MURINE | EPITHELIAL STEM-CELLS | EXPANSION | ENDOCRINOLOGY & METABOLISM | UROLOGY & NEPHROLOGY | cancer stem/progenitor-like cells | DIFFERENTIATION | CD133 | ANTIGEN | Immunohistochemistry | Prostatic Neoplasms - metabolism | Nestin | Proto-Oncogene Proteins c-met - biosynthesis | Antigens, CD - biosynthesis | Humans | Membrane Glycoproteins - biosynthesis | GPI-Linked Proteins | Octamer Transcription Factor-3 - biosynthesis | Cell Growth Processes - physiology | Intercellular Signaling Peptides and Proteins - biosynthesis | Male | Gene Expression Profiling | Proto-Oncogene Proteins - biosynthesis | Antigens, CD - genetics | Octamer Transcription Factor-3 - genetics | RNA, Messenger - biosynthesis | Prostatic Neoplasms - genetics | Neoplastic Stem Cells - metabolism | Serrate-Jagged Proteins | Intermediate Filament Proteins - genetics | Nerve Tissue Proteins - biosynthesis | Neoplastic Stem Cells - pathology | Retrospective Studies | Neoplasm Proteins - genetics | Jagged-1 Protein | Prostatic Neoplasms - pathology | Antigens, Neoplasm | Calcium-Binding Proteins - biosynthesis | Homeodomain Proteins - biosynthesis | Nanog Homeobox Protein | Keratin-14 - biosynthesis | Membrane Proteins - genetics | Neoplasm Proteins - biosynthesis | RNA, Messenger - genetics | Intercellular Signaling Peptides and Proteins - genetics | Intermediate Filament Proteins - biosynthesis | Proto-Oncogene Proteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Keratin-14 - genetics | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Membrane Glycoproteins - genetics | Proto-Oncogene Proteins c-met - genetics | Membrane Proteins - biosynthesis | Clone Cells - pathology | Calcium-Binding Proteins - genetics
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2012, Volume 287, Issue 1, pp. 58 - 67
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, p. e46307
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor beta superfamily that exert their effects via type I and type II serine... 
Bone Morphogenetic Protein 5 - chemistry | Bone Morphogenetic Protein 6 - chemistry | Bone Morphogenetic Protein 7 - chemistry | Hemochromatosis Protein | Bone Morphogenetic Protein 7 - genetics | Humans | Nerve Tissue Proteins - chemistry | Transfection | Bone Morphogenetic Protein 6 - genetics | Solutions | Growth Differentiation Factors - genetics | Genes, Reporter | Cell Line | Cell Adhesion Molecules, Neuronal - chemistry | Signal Transduction | Membrane Proteins - genetics | Bone Morphogenetic Protein 5 - genetics | Recombinant Proteins - chemistry | Histocompatibility Antigens Class I - genetics | Recombinant Proteins - genetics | Histocompatibility Antigens Class I - chemistry | Nerve Tissue Proteins - genetics | Cell Adhesion Molecules, Neuronal - genetics | GPI-Linked Proteins - chemistry | Membrane Proteins - chemistry | Protein Binding | Ligands | Kinetics | GPI-Linked Proteins - genetics | Growth Differentiation Factors - chemistry | Physiological aspects | Bone morphogenetic proteins | Genetic aspects | Research | Protein binding | Smad protein | Phosphorylation | Nephrology | Transforming growth factor-b | Homeostasis | Intracellular signalling | Iron | Biology | Kinases | Medical schools | Proteins | Signal transduction | Receptors | Rodents | Growth factors | Binding | Bone morphogenetic protein 6 | Bone morphogenetic protein 5 | Bone morphogenetic protein 4 | Bone morphogenetic protein 2 | Threonine | Research & development--R&D | Anemia | Affinity | Protein-serine/threonine kinase | Surface plasmon resonance | Mutation | Bone | Receptor mechanisms | Bone morphogenetic protein 9 | Bone morphogenetic protein 7 | Research & development | R&D
Journal Article
Nature, ISSN 0028-0836, 01/2008, Volume 451, Issue 7177, pp. 425 - 430
Journal Article
Neuron, ISSN 0896-6273, 08/2017, Volume 95, Issue 5, pp. 1056 - 1073.e5
Journal Article
PLoS Pathogens, ISSN 1553-7366, 07/2013, Volume 9, Issue 7, p. e1003483
Tetherin, an interferon-inducible membrane protein, inhibits the release of nascent enveloped viral particles from the surface of infected cells. However, the... 
INHIBITS HIV-1 | PROTEIN | IMMUNODEFICIENCY-VIRUS | PARTICLE RELEASE | DOWN-REGULATION | MICROBIOLOGY | RESTRICTION | BST-2/TETHERIN | INTERFERON-ALPHA | VIROLOGY | SURFACE | VPU | PARASITOLOGY | Humans | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism | Antiviral Agents - metabolism | Antigens, CD - genetics | Recombinant Fusion Proteins - metabolism | Antigens, CD - metabolism | HIV-1 - physiology | Glycosylphosphatidylinositols - chemistry | Antiviral Agents - chemistry | Proteolysis | HEK293 Cells | Antigens, CD - chemistry | Protein Interaction Domains and Motifs | Dimerization | Peptide Fragments - genetics | Virion - immunology | gag Gene Products, Human Immunodeficiency Virus - biosynthesis | Peptide Fragments - metabolism | Viral Regulatory and Accessory Proteins - genetics | Virion - physiology | Recombinant Fusion Proteins - chemistry | GPI-Linked Proteins - metabolism | Viral Regulatory and Accessory Proteins - metabolism | Human Immunodeficiency Virus Proteins - metabolism | HIV-1 - immunology | Peptide Fragments - chemistry | GPI-Linked Proteins - chemistry | Glycosylphosphatidylinositols - metabolism | Models, Biological | Virus Attachment | Human Immunodeficiency Virus Proteins - genetics | Protein Conformation | HeLa Cells | Mutation | GPI-Linked Proteins - genetics | Viral proteins | Physiological aspects | Virulence (Microbiology) | Research | HIV (Viruses) | Health aspects | Membrane proteins | Proteins | Viruses | Interferon | Experiments
Journal Article