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Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2018, Volume 25, Issue 7, pp. 616 - 622
Journal Article
Neuron, ISSN 0896-6273, 04/2017, Volume 94, Issue 1, pp. 48 - 57.e4
Journal Article
Molecular Cell, ISSN 1097-2765, 05/2017, Volume 66, Issue 4, pp. 488 - 502.e7
Ubiquitin-binding domain (UBD) proteins regulate numerous cellular processes, but their specificities toward ubiquitin chain types in cells remain... 
proteasome | autophagy | proteasome inhibitor | ubiquitin-binding domain | endocytosis | mass spectrometry | UBD protein | ubiquitin | MVB sorting | UBIQUITYLATED PROTEINS | SINGLE UBIQUITIN | RECOGNITION | RAD23 | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEGRADATION | POLYUBIQUITIN CHAIN | QUANTITATIVE-ANALYSIS | BINDING | DOMAINS | CELL BIOLOGY | Saccharomyces cerevisiae - genetics | Ubiquitins - genetics | Valosin Containing Protein | Ubiquitin - metabolism | Endosomal Sorting Complexes Required for Transport - genetics | Saccharomyces cerevisiae - drug effects | DNA-Binding Proteins - metabolism | Endocytosis | Proteasome Endopeptidase Complex - drug effects | Ubiquitination - drug effects | Time Factors | Proteolysis | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Ubiquitins - metabolism | Proteasome Inhibitors - pharmacology | Membrane Proteins - genetics | Cell Cycle Proteins - metabolism | Endosomal Sorting Complexes Required for Transport - metabolism | Adenosine Triphosphatases - metabolism | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - genetics | Nucleocytoplasmic Transport Proteins - genetics | Proteasome Endopeptidase Complex - genetics | Carrier Proteins - genetics | Carrier Proteins - metabolism | Nucleocytoplasmic Transport Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Adenosine Triphosphatases - genetics | Proteasome Endopeptidase Complex - metabolism | Ubiquitin | Physiological aspects | Analysis | Protein binding | Mass spectrometry
Journal Article
Journal Article
Cancer Research, ISSN 0008-5472, 04/2014, Volume 74, Issue 8, pp. 2193 - 2203
The immunoreceptor NKG2D originally identified in natural killer (NK) cells recognizes ligands that are upregulated on tumor cells. Expression of NKG2D ligands... 
TRANSCRIPTION FACTORS | B-CELLS | DAMAGE RESPONSE | SIGNALING PATHWAYS | NATURAL-KILLER | INTERFERON | IMMUNE-SYSTEM | ONCOLOGY | IN-VIVO | C-MYC | INNATE | Immunologic Surveillance | Up-Regulation | Phosphorylation | Nucleocytoplasmic Transport Proteins - biosynthesis | DNA, Neoplasm - metabolism | NK Cell Lectin-Like Receptor Subfamily K - immunology | Interferon Regulatory Factor-3 - genetics | Lymphoma - metabolism | Transfection | DNA Damage - physiology | NK Cell Lectin-Like Receptor Subfamily K - metabolism | DNA Damage - genetics | Killer Cells, Natural - immunology | Membrane Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | Interferon Regulatory Factor-3 - immunology | Nucleocytoplasmic Transport Proteins - immunology | Membrane Proteins - genetics | Nuclear Matrix-Associated Proteins - immunology | Mice, Inbred C57BL | Lymphoma - immunology | Protein-Serine-Threonine Kinases - genetics | Lymphoma - genetics | Nuclear Matrix-Associated Proteins - metabolism | Membrane Proteins - immunology | Mice, Transgenic | NK Cell Lectin-Like Receptor Subfamily K - genetics | Nucleocytoplasmic Transport Proteins - genetics | Animals | Nucleocytoplasmic Transport Proteins - metabolism | Nuclear Matrix-Associated Proteins - genetics | Cell Line, Tumor | Interferon Regulatory Factor-3 - metabolism | Ligands | Protein-Serine-Threonine Kinases - immunology | Mice | Killer Cells, Natural - metabolism | Nuclear Matrix-Associated Proteins - biosynthesis | DNA Damage - radiation effects
Journal Article
Nature Genetics, ISSN 1061-4036, 02/2009, Volume 41, Issue 2, pp. 234 - 239
Vitamin B(12) (cobalamin) is essential in animals for metabolism of branched chain amino acids and odd chain fatty acids, and for remethylation of homocysteine... 
Vitamin B 12 Deficiency - etiology | Transcobalamins - genetics | Humans | Male | Methylmalonic Acid - metabolism | Proteins - isolation & purification | Tissue Distribution | Membrane Transport Proteins - deficiency | Membrane Transport Proteins - genetics | Transcobalamins - isolation & purification | Female | Membrane Transport Proteins - metabolism | Vitamin B 12 Deficiency - metabolism | Child | Methylmalonic Acid - urine | Chromosome Deletion | Lysosome-Associated Membrane Glycoproteins - metabolism | Nucleocytoplasmic Transport Proteins - physiology | Chromosome Mapping | Chromosomes, Human, Pair 6 | Nucleocytoplasmic Transport Proteins - genetics | Polymorphism, Genetic | Proteins - genetics | Nucleocytoplasmic Transport Proteins - metabolism | Proteins - metabolism | Transcobalamins - metabolism | Vitamin B 12 Deficiency - genetics | Hyperhomocysteinemia - genetics | HeLa Cells | Hyperhomocysteinemia - complications | Vitamin B 12 - metabolism | Medical research | Heart surgery | Genes | Vitamin B | Genetics | Medical screening | Chromosomes | Nucleocytoplasmic Transport Proteins | Biochemistry, Molecular Biology | Vitamin B 12 Deficiency | Proteins | Life Sciences | Membrane Transport Proteins | Transcobalamins | Vitamin B 12 | Hyperhomocysteinemia | Methylmalonic Acid | Lysosome-Associated Membrane Glycoproteins | Hela Cells
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2319 - 19
The nuclear pore complex (NPC) controls the passage of macromolecules between the nucleus and cytoplasm, but how the NPC directly participates in... 
GLE1 | INNER RING | REPEAT EXPANSION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | CONSERVED MECHANISM | CYTOPLASMIC FIBRILS | BOX PROTEIN RAT8P/DBP5P | DBP5 | HELICASE DDX19 | NUCLEOPORIN NUP214 | Fungal Proteins - chemistry | Saccharomyces cerevisiae - genetics | Humans | Nuclear Pore Complex Proteins - chemistry | RNA, Messenger - metabolism | Nuclear Pore Complex Proteins - genetics | Saccharomyces cerevisiae - metabolism | Phytic Acid - metabolism | Nucleocytoplasmic Transport Proteins - chemistry | Active Transport, Cell Nucleus | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Recombinant Proteins - metabolism | RNA Transport | Nuclear Pore Complex Proteins - metabolism | RNA, Messenger - genetics | Models, Molecular | Nuclear Pore - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Pore - metabolism | Chaetomium - genetics | Nucleocytoplasmic Transport Proteins - genetics | Chaetomium - metabolism | DEAD-box RNA Helicases - genetics | Nucleocytoplasmic Transport Proteins - metabolism | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | RNA, Messenger - chemistry | Nuclear Pore - chemistry | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Binding | Macromolecules | Homology | Activation | mRNA | Functional analysis | Ribonucleic acid--RNA | Thermal stability | Exports | DNA helicase | Nucleoporins | Mutation | Adenosine triphosphatase | Cytoplasm | Crystal structure | Structure-function relationships
Journal Article
Journal Article