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Nature (London), ISSN 1476-4687, 2017, Volume 546, Issue 7659, pp. 504 - 509
ABCG2 is a constitutively expressed ATP-binding cassette (ABC) transporter that protects many tissues against xenobiotic molecules. Its activity affects the... 
BINDING CASSETTE TRANSPORTER | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | RESISTANCE-ASSOCIATED PROTEIN | MONOCLONAL-ANTIBODY | IDENTIFICATION | CANCER | EXPRESSION | RECONSTITUTION | P-GLYCOPROTEIN | ATPASE SUBUNIT | Immunoglobulin Fab Fragments - ultrastructure | Antibodies - chemistry | Humans | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - metabolism | Cholesterol - chemistry | Biological Transport | Antibodies - immunology | Protein Domains | Adenosine Triphosphatases - ultrastructure | Binding Sites | Amino Acid Sequence | Neoplasm Proteins - ultrastructure | Adenosine Triphosphatases - metabolism | Antibodies - ultrastructure | Models, Molecular | Neoplasm Proteins - chemistry | Cholesterol - metabolism | Cryoelectron Microscopy | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - antagonists & inhibitors | Immunoglobulin Fab Fragments - chemistry | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - chemistry | Polymorphism, Single Nucleotide - genetics | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - ultrastructure | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Immunoglobulin Fab Fragments - immunology | Physiological aspects | Binding proteins | Observations | Drug interactions
Journal Article
Molecular cell, ISSN 1097-2765, 2008, Volume 29, Issue 2, pp. 169 - 179
The ATPase RIG-I senses viral RNAs that contain 5′-triphosphates in the cytoplasm. It initiates a signaling cascade that activates innate immune response by... 
RNA | MOLIMMUNO | RESPONSES | HELICASE LGP2 | VIRUS | ACID | REPLICATION | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIVIRAL INNATE IMMUNITY | HOST | IDENTIFICATION | ADAPTER PROTEIN | CELL BIOLOGY | RNA Caps - immunology | RNA Helicases - metabolism | Zinc - metabolism | Humans | rab GTP-Binding Proteins - genetics | Structure-Activity Relationship | RNA Helicases - chemistry | Interferons - immunology | RNA Caps - metabolism | Zinc - chemistry | Adenosine Triphosphatases - immunology | Interferon-Induced Helicase, IFIH1 | RNA, Viral - genetics | Immunity, Innate - physiology | RNA Caps - chemistry | Zinc - immunology | RNA Helicases - genetics | RNA, Viral - metabolism | Interferons - genetics | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Dimerization | RNA Caps - genetics | rab GTP-Binding Proteins - metabolism | Cell Line | DEAD Box Protein 58 | Adenosine Triphosphatases - metabolism | Protein Structure, Tertiary - genetics | Binding Sites - genetics | Substrate Specificity - genetics | Polyphosphates - metabolism | DEAD-box RNA Helicases - genetics | Animals | RNA, Viral - chemistry | Polyphosphates - immunology | rab GTP-Binding Proteins - immunology | DEAD-box RNA Helicases - immunology | Interferons - metabolism | Adenosine Triphosphatases - chemistry | RNA, Viral - immunology | rab GTP-Binding Proteins - chemistry | Adenosine Triphosphatases - genetics | Structural Homology, Protein | RNA Helicases - immunology | Polyphosphates - chemistry | Sensors | G proteins | Biological response modifiers | Adenosine triphosphatase | Index Medicus
Journal Article
Oncogene, ISSN 1476-5594, 2010, Volume 29, Issue 37, pp. 5171 - 5181
Cancer cells frequently express genes normally active in male germ cells. ATAD2 is one of them encoding a conserved factor harbouring an AAA type ATPase domain... 
proteasome | H4 K5ac | histone | chromatin | epigenetics | COACTIVATOR | PROTEIN | ATPASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANCCA | CELL BIOLOGY | ONCOLOGY | ROLES | GENETICS & HEREDITY | GENE-EXPRESSION | BOUNDARY | HISTONE CODE | Testis - metabolism | Prognosis | Humans | Lung Neoplasms - metabolism | Molecular Sequence Data | Male | Lung Neoplasms - physiopathology | Breast Neoplasms - physiopathology | Breast Neoplasms - metabolism | DNA-Binding Proteins - metabolism | Female | Acetylation | Lung Neoplasms - genetics | Amino Acid Sequence | ATPases Associated with Diverse Cellular Activities | DNA-Binding Proteins - physiology | Adenosine Triphosphatases - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Sequence Homology, Amino Acid | Breast Neoplasms - genetics | Cell Line, Tumor | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Adenosine Triphosphatases - physiology | Testis | Lung cancer | Physiological aspects | Breast cancer | Genetic aspects | Research | Adenosine triphosphatase | Proteins | Chromatin | Cellular biology | Medical prognosis | Epigenetics | Gene expression | Biochemistry, Molecular Biology | Breast Neoplasms | Lung Neoplasms | Life Sciences | Human health and pathology | Adenosine Triphosphatases | Genetics | DNA-Binding Proteins | Cancer
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 6/2013, Volume 110, Issue 24, pp. 9710 - 9715
ABCB10 is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria. In mammals ABCB10 is essential for... 
ATP binding cassette transporters | Proteins | Crystals | Adenosine triphosphatases | Lipids | Nucleotides | Exporters | Binding sites | Monomers | Crystal structure | X-ray crystallography | Nucleotide complex | Abc mitochondrial erythroid | Cardiolipin | Human membrane protein structure | COMPLEX | nucleotide complex | MECHANISM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOCHONDRIA | HYDROLYSIS | cardiolipin | ABC mitochondrial erythroid | P-GLYCOPROTEIN | MITOFERRIN-1 | RESISTANCE | human membrane protein structure | PROTEINS | REVEALS | Humans | Molecular Conformation | Molecular Sequence Data | Crystallography, X-Ray | Nucleotides - chemistry | ATP-Binding Cassette Transporters - chemistry | Sf9 Cells | ATP-Binding Cassette Transporters - genetics | Adenosine Triphosphate - metabolism | ATP-Binding Cassette Transporters - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Adenosine Triphosphatases - metabolism | Models, Molecular | Binding Sites - genetics | Phosphatidylcholines - chemistry | Nucleotides - metabolism | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Mutation | Adenosine Triphosphate - chemistry | Phosphatidylethanolamines - chemistry | Biological transport, Active | Physiological aspects | Research | Binding proteins | Structure | Health aspects | Adenosine triphosphate | Biological Sciences
Journal Article
Journal Article
Nature (London), ISSN 1476-4687, 2014, Volume 508, Issue 7497, pp. 550 - 553
Journal Article
Journal Article
Journal Article
Nature structural & molecular biology, ISSN 1545-9993, 08/2011, Volume 18, Issue 8, pp. 894 - 901
Journal Article
Cancer cell, ISSN 1535-6108, 2015, Volume 28, Issue 5, pp. 653 - 665
Journal Article