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Neuron, ISSN 0896-6273, 02/2013, Volume 77, Issue 3, pp. 472 - 484
Major outputs of the neocortex are conveyed by corticothalamic axons (CTAs), which form reciprocal connections with thalamocortical axons, and... 
MUTANT MICE | CORTICAL AXONS | THALAMOCORTICAL AXONS | GROWTH | SEMAPHORIN 3E | CENTRAL-NERVOUS-SYSTEM | GUIDANCE | CHICK HINDLIMB | CAJAL-RETZIUS CELLS | NEUROSCIENCES | CEREBRAL-CORTEX | Thyroid Nuclear Factor 1 | Age Factors | Embryo, Mammalian | Leukocyte L1 Antigen Complex - metabolism | Gene Expression Regulation, Developmental - genetics | Axons - physiology | Cerebral Cortex - cytology | Neural Pathways - physiology | DNA-Binding Proteins - metabolism | POU Domain Factors - genetics | tau Proteins - genetics | Thalamus - physiology | Contactin 2 - metabolism | Repressor Proteins - metabolism | Glycoproteins - genetics | Tumor Suppressor Proteins - metabolism | Wnt3A Protein - genetics | Membrane Proteins - genetics | Mice, Inbred C57BL | Mice, Transgenic | Nuclear Proteins - metabolism | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Membrane Glycoproteins - genetics | Nerve Tissue Proteins - metabolism | S100 Calcium Binding Protein G - metabolism | Transcription Factors - metabolism | Animals | Calbindin 2 | Thalamus - cytology | Cerebral Cortex - physiology | Luminescent Proteins - genetics | Mice | Body Patterning - genetics | Luminescent Proteins - metabolism | Developmental biology | Neurons | Studies | Laboratories | Experiments | Repressor Proteins | Cerebral Cortex | Cellular Biology | Neural Pathways | tau Proteins | Life Sciences | Contactin 2 | Gene Expression Regulation, Developmental | Body Patterning | Thalamus | Membrane Glycoproteins | Luminescent Proteins | DNA-Binding Proteins | POU Domain Factors | Calcium-Binding Protein, Vitamin D-Dependent | Glycoproteins | Nerve Tissue Proteins | Nuclear Proteins | Membrane Proteins | Axons | Homeodomain Proteins | Leukocyte L1 Antigen Complex | Transcription Factors | Wnt3A Protein | Tumor Suppressor Proteins | reciprocal connections | handshake | waiting period | PlexinD1 | axon guidance | Sema3E | thalamocortical | corticothalamic
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 489, Issue 7415, pp. 313 - 317
Cornelia de Lange syndrome (CdLS) is a dominantly inherited congenital malformation disorder, caused by mutations in the cohesin-loading protein NIPBL1,2 for nearly 60... 
SISTER-CHROMATID COHESION | NIPPED-B | COMPLEX | NIPBL | HUMAN GENOME | RNA-SEQ | MULTIDISCIPLINARY SCIENCES | X-CHROMOSOME-INACTIVATION | S-PHASE | PROTEINS | BINDING | Chromatin - metabolism | Chondroitin Sulfate Proteoglycans - chemistry | Humans | Crystallography, X-Ray | Male | Phosphoproteins - metabolism | Cell Cycle Proteins - chemistry | Chromatin Immunoprecipitation | Repressor Proteins - deficiency | De Lange Syndrome - metabolism | Fibroblasts | Female | Transcription, Genetic | Acetylation | Binding Sites | Repressor Proteins - metabolism | De Lange Syndrome - genetics | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histone Deacetylases - genetics | Cell Cycle Proteins - metabolism | Chondroitin Sulfate Proteoglycans - metabolism | Histone Deacetylases - chemistry | Histone Deacetylases - deficiency | Mutant Proteins - genetics | Prophase | Models, Molecular | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Mutation - genetics | Proteins - genetics | Mutant Proteins - chemistry | Protein Conformation | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Anaphase | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Genetics | De Lange syndrome | Genetic aspects | Research | Mutation (Biology) | Proteins | Cell culture | Genes | Cell cycle | Mutation | Females | Chromosomes | Crystal structure | Chromatin | Repressor Proteins | Life Sciences | Phosphoproteins | Chromosomal Proteins, Non-Histone | Histone Deacetylases | De Lange Syndrome | Chondroitin Sulfate Proteoglycans | Nuclear Proteins | Mutant Proteins | Adaptor Proteins, Signal Transducing | Development Biology | Cell Cycle Proteins
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase
Journal Article
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 4774 - 10
The total number of acquired melanocytic nevi on the skin is strongly correlated with melanoma risk. Here we report a meta-analysis of 11 nevus GWAS from... 
CUTANEOUS MALIGNANT-MELANOMA | METAANALYSIS | SUN EXPOSURE | VARIANTS | MULTIDISCIPLINARY SCIENCES | GENETIC INFLUENCES | PREVALENCE | MELANOCYTIC NEVI | CANCER | TANNING RESPONSE | GENOME-WIDE ASSOCIATION | Cytochrome P-450 CYP1B1 - genetics | Humans | Stem Cell Factor - genetics | RNA-Binding Proteins | RNA - genetics | Telomere-Binding Proteins - genetics | Telomerase - genetics | Nevus, Pigmented - genetics | Group VI Phospholipases A2 - genetics | Melanoma - genetics | Genetic Pleiotropy - genetics | Nuclear Proteins - genetics | Microfilament Proteins - genetics | European Continental Ancestry Group - genetics | Genetic Predisposition to Disease | Genome-Wide Association Study | Guanine Nucleotide Exchange Factors - genetics | Histone Deacetylases - genetics | Interferon Regulatory Factors - genetics | Repressor Proteins - genetics | Nerve Tissue Proteins - genetics | Carrier Proteins - genetics | Skin Neoplasms - genetics | MicroRNAs - genetics | Polymorphism, Single Nucleotide | Receptors, G-Protein-Coupled - genetics | Bivariate analysis | Pathways | Interferon regulatory factor 4 | Genes | Melanoma | Nevus | Risk | Skin | Single-nucleotide polymorphism | Loci | PLA2G6 protein, human | risk assessment | cutaneous melanoma | Interferon Regulatory Factors | RNA | Medical and Health Sciences | KITLG protein, human | single nucleotide polymorphism | Repressor Proteins | carrier protein | repressor protein | Group VI Phospholipases A2 | Stn1 protein, human | pigmented nevus | G protein coupled receptor | genetic risk | genetic predisposition | skin tumor | PPARGC1B protein, human | telomerase RNA | Carrier Proteins | Basic Medicine | peroxisome proliferator activated receptor gamma coactivator 1beta | nerve protein | biology | gene | HDAC4 protein, human | Receptors, G-Protein-Coupled | Caucasian | melanoma | European Continental Ancestry Group | Genetic Pleiotropy | Nerve Tissue Proteins | histone deacetylase 4 | Guanine Nucleotide Exchange Factors | Nuclear Proteins | Clinical Medicine | Skin Neoplasms | Cytochrome P-450 CYP1B1 | interferon regulatory factor | DOCK8 protein, human | gene expression | cytochrome P450 1B1 | United States | meta analysis | Medicin och hälsovetenskap | Article | skin | pleiotropy | Klinisk medicin | nuclear protein | Medicinsk genetik | Medical Genetics | Netherlands | telomerase | genetics | human | stem cell factor | GPRC5A protein, human | phospholipase A2 group VI | telomere binding protein | meta-analysis | United Kingdom | Histone Deacetylases | interferon regulatory factor 4 | actin binding protein | SYNE2 protein, human | histone deacetylase | Telomere-Binding Proteins | gene locus | guanine nucleotide exchange factor | Microfilament Proteins | MicroRNAs | Nevus, Pigmented | genome-wide association study | Medicinska och farmaceutiska grundvetenskaper | microRNA | meta analysis (topic) | MIRN146 microRNA, human | cancer | Australia | Cancer and Oncology | CYP1B1 protein, human | interferon regulatory factor-4 | telomere homeostasis | Cancer och onkologi
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2009, Volume 4, Issue 5, pp. e5622 - e5622
Background: The INK4/ARF locus encodes three tumor suppressor genes (p15(Ink4b), Arf and p16(Ink4a)) and is frequently inactivated in a large number of human... 
INACTIVATION | MAMMALIAN TRITHORAX | DELAYED REPLICATION | METHYLATION | DOMAIN | GROUP GENE | MULTIDISCIPLINARY SCIENCES | METHYLTRANSFERASE ACTIVITY | MLL | CELLULAR SENESCENCE | HISTONE | NIH 3T3 Cells | Myeloid-Lymphoid Leukemia Protein - metabolism | Cellular Senescence | Repressor Proteins - metabolism | Fibroblasts - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Cycle Proteins - metabolism | Gene Silencing | Cyclin-Dependent Kinase Inhibitor p16 - genetics | Nuclear Proteins - metabolism | Polycomb-Group Proteins | Enhancer of Zeste Homolog 2 Protein | Polycomb Repressive Complex 2 | Animals | Cyclin-Dependent Kinase Inhibitor p16 - chemistry | Polycomb Repressive Complex 1 | Histone-Lysine N-Methyltransferase - metabolism | Embryo, Mammalian - cytology | Models, Biological | Cyclin-Dependent Kinase Inhibitor p16 - metabolism | Protein Binding | DNA Replication Timing | Fibroblasts - cytology | Mice | Histones - metabolism | Methylation | Proteins | Epigenetic inheritance | DNA replication | Senescence | Chromatin | Genes | INK4a protein | Genomes | Recruitment | Cell growth | Transcription activation | Cell cycle | Fibroblasts | Cyclin-dependent kinase inhibitors | Dissociation | Deoxyribonucleic acid--DNA | p16 Protein | INK4 protein | Embryo fibroblasts | Gene expression | Embryos | Loci | DNA biosynthesis | Polycomb group proteins | Replication origins | Pilot projects | Insects | Stem cells | Epigenetics | Tumor suppressor genes | Replication | Embryo, Mammalian | Histone-Lysine N-Methyltransferase | Repressor Proteins | Cell Aging | Nuclear Proteins | Cyclin-Dependent Kinase Inhibitor p16 | Life Sciences | Immunology | Histones | Myeloid-Lymphoid Leukemia Protein | Proto-Oncogene Proteins | Cell Cycle Proteins | Deoxyribonucleic acid | DNA
Journal Article
Nature (London), ISSN 1476-4687, 2004, Volume 431, Issue 7010, pp. 873 - 878
.... The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2... 
CORE | RECRUITMENT | TRANSCRIPTIONAL ACTIVATION | COMPLEX | LIGASE ACTIVITY | MULTIDISCIPLINARY SCIENCES | RAD6 | H3 LYSINE-27 METHYLATION | UBIQUITYLATION | RING FINGER PROTEINS | DROSOPHILA | Nuclear Proteins - isolation & purification | Nucleosomes - chemistry | Humans | Multiprotein Complexes | Ubiquitin - metabolism | Molecular Sequence Data | Drosophila melanogaster - genetics | Promoter Regions, Genetic - genetics | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Protein Subunits - isolation & purification | Repressor Proteins - isolation & purification | Response Elements - genetics | Nuclear Proteins - genetics | Proto-Oncogene Proteins - isolation & purification | Repressor Proteins - metabolism | Protein Subunits - genetics | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Cell Line | Catalytic Domain | Repressor Proteins - chemistry | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Nucleosomes - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Polycomb-Group Proteins | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - isolation & purification | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Homeodomain Proteins - genetics | Transcription Factors - metabolism | Polycomb Repressive Complex 2 | Animals | Polycomb Repressive Complex 1 | Transcription Factors - isolation & purification | Ubiquitin-Protein Ligases - isolation & purification | Protein Subunits - chemistry | Drosophila Proteins - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Proteins | Enzymes | Cell culture | Chromatin | Biochemistry
Journal Article
The Journal of cell biology, ISSN 0021-9525, 5/2010, Volume 189, Issue 5, pp. 795 - 811
.... So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope... 
Yeasts | Nuclear pore | Cell growth | Nuclear pore complex proteins | Mother cells | Cell nucleus | Nuclear membrane | Fluorescence | HeLa cells | Daughter cells | DE-NOVO | TRANSPORT | TUBULAR ENDOPLASMIC-RETICULUM | IN-VIVO | ENVELOPE | CELL-CYCLE | MESSENGER-RNA EXPORT | YEAST SACCHAROMYCES | SACCHAROMYCES-CEREVISIAE | INTEGRAL MEMBRANE-PROTEIN | CELL BIOLOGY | RNA-Binding Proteins - genetics | Cell Proliferation | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Phylogeny | RNA, Messenger - metabolism | Recombinant Fusion Proteins - metabolism | Nuclear Pore Complex Proteins - genetics | Saccharomyces cerevisiae - metabolism | Membrane Proteins - metabolism | Telophase - physiology | Active Transport, Cell Nucleus - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ribonuclease III - genetics | Ribonuclease III - metabolism | Membrane Proteins - genetics | Nuclear Pore Complex Proteins - metabolism | Nuclear Pore - genetics | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Pore - metabolism | Nucleocytoplasmic Transport Proteins - genetics | Sequence Homology, Amino Acid | Nucleocytoplasmic Transport Proteins - metabolism | Nuclear Pore - ultrastructure | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | RNA-Binding Proteins - metabolism | Protein Binding - physiology | Properties | Structure | Porins | Nucleocytoplasmic Transport Proteins | Nuclear Pore Complex Proteins | Repressor Proteins | RNA-Binding Proteins | Endoplasmic Reticulum | Cellular Biology | Recombinant Fusion Proteins | Membrane Proteins | Life Sciences | Ribonuclease III | Telophase | Saccharomyces cerevisiae Proteins | Protein Binding | Active Transport, Cell Nucleus | Nuclear Pore | RNA, Messenger | Saccharomyces cerevisiae
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2010, Volume 39, Issue 6, pp. 963 - 974
... a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive... 
NECDIN GENE | EMERGING ROLES | MELANOMA | KAP1 | CANCER/TESTIS ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MDM2 INTERACTION | HOMOLOGOUS RECOMBINATION | CANCER-IMMUNOTHERAPY | CELL-LINES | EXPRESSION | CELL BIOLOGY | Melanoma-Specific Antigens - chemistry | Protein Interaction Domains and Motifs - physiology | Humans | Crystallography, X-Ray | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | RING Finger Domains | Tripartite Motif-Containing Protein 28 | Ubiquitination | Cell Nucleus - metabolism | Transfection | Protein Structure, Quaternary | Antigens, Neoplasm - metabolism | Carrier Proteins - chemistry | Neoplasm Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Antigens, Neoplasm - genetics | Cell Line | Biocatalysis | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Recombinant Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Melanoma-Specific Antigens - metabolism | Cell Line, Tumor | Ubiquitin-Protein Ligases - genetics | Melanoma-Specific Antigens - genetics | Protein Binding - physiology | Ubiquitin | Antigens | Ligases | Crystals | Melanoma | Structure | Tumor proteins | Protein binding
Journal Article