X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (1830) 1830
Publication (419) 419
Book Chapter (8) 8
Conference Proceeding (6) 6
Book Review (5) 5
Dissertation (2) 2
Reference (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (1266) 1266
index medicus (942) 942
animals (902) 902
elav proteins (754) 754
rna-binding proteins - metabolism (518) 518
rna, messenger - metabolism (484) 484
biochemistry & molecular biology (469) 469
elav-like protein 1 (456) 456
female (409) 409
male (408) 408
mice (404) 404
elav proteins - metabolism (393) 393
expression (353) 353
cell biology (347) 347
hur (345) 345
rna-binding proteins - genetics (341) 341
messenger-rna (314) 314
protein binding (299) 299
neurosciences (297) 297
rna, messenger - genetics (295) 295
proteins (258) 258
antigens, surface - metabolism (249) 249
gene-expression (245) 245
elav proteins - genetics (233) 233
middle aged (225) 225
cell line, tumor (220) 220
molecular sequence data (220) 220
gene expression (217) 217
base sequence (215) 215
rats (201) 201
cancer (200) 200
rna-binding protein (200) 200
oncology (195) 195
rna (194) 194
aged (189) 189
gene expression regulation (186) 186
article (185) 185
3' untranslated regions (180) 180
elav-like protein 1 - metabolism (177) 177
cell line (176) 176
rna stability (169) 169
neurons (167) 167
messenger rna (165) 165
elav (164) 164
posttranscriptional regulation (161) 161
neurons - metabolism (157) 157
clinical neurology (151) 151
cells, cultured (143) 143
phosphorylation (143) 143
antigens, surface - genetics (142) 142
research (141) 141
rna-binding proteins - immunology (140) 140
elav proteins - immunology (137) 137
immunohistochemistry (136) 136
3'-untranslated region (132) 132
elav-like protein 1 - genetics (131) 131
nerve tissue proteins - metabolism (131) 131
analysis (128) 128
rna-binding proteins (128) 128
binding proteins (126) 126
binding sites (126) 126
binding protein hur (125) 125
cytoplasm - metabolism (125) 125
translation (124) 124
elav-like protein 4 (123) 123
apoptosis (121) 121
au-rich elements (121) 121
hur protein (121) 121
nerve tissue proteins - genetics (120) 120
hela cells (118) 118
nerve tissue proteins - immunology (117) 117
mrna stability (116) 116
messenger-rna stability (115) 115
cells (114) 114
stability (114) 114
au-rich element (110) 110
blotting, western (110) 110
gene expression regulation, neoplastic (109) 109
transfection (107) 107
adult (106) 106
cell proliferation (106) 106
research article (105) 105
stabilization (103) 103
antigens, surface (102) 102
in-vivo (102) 102
multidisciplinary sciences (99) 99
gene (98) 98
genetic aspects (96) 96
antibodies (95) 95
physiological aspects (94) 94
signal transduction (94) 94
nervous-system (93) 93
rna interference (93) 93
cell nucleus - metabolism (92) 92
developmental biology (92) 92
immunology (92) 92
reverse transcriptase polymerase chain reaction (92) 92
time factors (91) 91
3' untranslated regions - genetics (90) 90
amino acid sequence (89) 89
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1788) 1788
Japanese (32) 32
French (13) 13
Chinese (5) 5
Spanish (4) 4
German (2) 2
Korean (2) 2
Dutch (1) 1
Italian (1) 1
Russian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


PLoS Computational Biology, ISSN 1553-734X, 2006, Volume 2, Issue 8, pp. 0890 - 0901
Recent proteome-wide screening approaches have provided a wealth of information about interacting proteins in various organisms. To test for a potential... 
UNSTRUCTURED PROTEINS | DATABASE | RECOGNITION | PROTEOME | BIOCHEMICAL RESEARCH METHODS | MATHEMATICAL & COMPUTATIONAL BIOLOGY | INTERACTION MAP | PREDICTIONS | INTERACTION NETWORKS | GENE ONTOLOGY | SACCHAROMYCES-CEREVISIAE | BINDING | Caenorhabditis elegans - chemistry | ELAV-Like Protein 2 | Drosophila Proteins - classification | Saccharomyces cerevisiae - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Ligases - genetics | Amino Acids - chemistry | Caenorhabditis elegans Proteins - metabolism | ELAV Proteins - classification | Ligases - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Saccharomyces cerevisiae - metabolism | Ligases - classification | Carrier Proteins - chemistry | ELAV Proteins - chemistry | Carrier Proteins - classification | Protein Structure, Tertiary | Saccharomyces cerevisiae Proteins - classification | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - genetics | Computational Biology | ELAV Proteins - metabolism | Ligases - metabolism | Models, Molecular | Drosophila Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Carrier Proteins - genetics | Caenorhabditis elegans Proteins - classification | Animals | Carrier Proteins - metabolism | Drosophila melanogaster - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Drosophila Proteins - genetics | Caenorhabditis elegans Proteins - genetics | ELAV Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Eukaryotes | Genetic aspects | Brewer's yeast | Analysis | Drosophila | Proteins | Confidence intervals | Genetics | Hypotheses | Organisms | Network hubs | Caenorhabditis | Bioinformatics - Computational Biology | Saccharomyces | Homo (Human) | Molecular Biology - Structural Biology
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 2004, Volume 32, Issue 4, pp. 1279 - 1288
Journal Article
MOLECULAR AND CELLULAR BIOLOGY, ISSN 0270-7306, 08/2009, Volume 29, Issue 16, pp. 4341 - 4351
Activation of p38 mitogen-activated protein kinase (MAPK) plays an important role in the G(2)/M cell cycle arrest induced by DNA damage, but little is known... 
UV-IRRADIATION | CELLS | PHOSPHORYLATION | DIFFERENTIAL ACTIVATION | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | P21(WAF1/CIP1) EXPRESSION | S-PHASE | ATAXIA-TELANGIECTASIA | P53 | CELL BIOLOGY | ELAV-Like Protein 1 | Gamma Rays | RNA, Small Interfering - genetics | RNA-Binding Proteins - genetics | Phosphorylation | Humans | RNA, Messenger - metabolism | ELAV Proteins | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | Cell Line - physiology | Cyclin-Dependent Kinase Inhibitor p21 - genetics | Tumor Suppressor Proteins - genetics | Antigens, Surface - metabolism | Cell Cycle Proteins - genetics | Cyclin-Dependent Kinase Inhibitor p21 - metabolism | p38 Mitogen-Activated Protein Kinases - metabolism | Protein-Serine-Threonine Kinases - metabolism | Tumor Suppressor Proteins - metabolism | RNA, Messenger - genetics | Antigens, Surface - genetics | Cell Cycle Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Tumor Suppressor Protein p53 - metabolism | p38 Mitogen-Activated Protein Kinases - genetics | Ataxia Telangiectasia Mutated Proteins | DNA-Binding Proteins - genetics | G1 Phase - physiology | RNA Stability | Cell Line - radiation effects | Animals | S Phase - physiology | Mice | DNA Damage | Enzyme Activation | RNA-Binding Proteins - metabolism | RNA, Small Interfering - metabolism
Journal Article
Journal of Neurochemistry, ISSN 0022-3042, 11/2009, Volume 111, Issue 4, pp. 1051 - 1061
Transactive response DNA‐binding protein 43 (TDP‐43) forms abnormal ubiquitinated and phosphorylated inclusions in brain tissues from patients with amyotrophic... 
stress granules | Transactive response DNA‐binding protein 43 | RNA‐binding protein | amyotrophic lateral sclerosis | Amyotrophic lateral sclerosis | RNA-binding protein | Transactive response DNA-binding protein 43 | Stress granules | GENE-MUTATIONS | INCLUSIONS | FUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | BINDING PROTEIN | NEUROSCIENCES | PROCESSING BODIES | MESSENGER-RNA | DISEASE | EXPRESSION | Arsenites - pharmacology | ELAV-Like Protein 1 | RNA, Small Interfering - genetics | Spinal Cord - metabolism | Emetine - pharmacology | Hybrid Cells | Oxidative Stress - physiology | Protein Transport - drug effects | ELAV Proteins | DNA-Binding Proteins - metabolism | Transfection - methods | Teratogens - pharmacology | Spinal Cord - pathology | Antigens, Surface - metabolism | Protein Synthesis Inhibitors - pharmacology | Motor Neurons - drug effects | Hot Temperature - adverse effects | Oxidative Stress - genetics | Ribonucleoproteins - metabolism | DNA-Binding Proteins - genetics | Motor Neurons - metabolism | Amyotrophic Lateral Sclerosis - pathology | Animals | Mice | Oxidative Stress - drug effects | RNA-Binding Proteins - metabolism | Protein Structure, Tertiary - drug effects | RNA, Small Interfering - metabolism | Neurosciences | Messenger RNA | Snow | Neurons | Analysis | Genetically modified organisms | Protein biosynthesis | Binding proteins | Proteins | Brain | Biochemistry | Index Medicus
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 06/2013, Volume 12, Issue 6, pp. 2869 - 2884
RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No... 
heterogeneous nuclear ribonucleoproteins | protein-protein interactions RALY | biotinylation | RNA-binding proteins | proteomics | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | EXON JUNCTION COMPLEX | HNRNP PROTEINS | MAMMALIAN-CELLS | MASS-SPECTROMETRY | MESSENGER-RNA | GLYCINE-RICH DOMAIN | NONSENSE-MEDIATED DECAY | FRAGILE-X-SYNDROME | ELAV-Like Protein 1 | RNA-Binding Proteins - genetics | Protein Biosynthesis | Humans | Molecular Sequence Data | Heterogeneous-Nuclear Ribonucleoprotein Group C - metabolism | Recombinant Fusion Proteins - metabolism | Carbon-Nitrogen Ligases - genetics | Protein Interaction Maps | Biotin - chemistry | HEK293 Cells | Biological Assay | Carbon-Nitrogen Ligases - chemistry | Poly(A)-Binding Protein I - genetics | ELAV Proteins - chemistry | Poly(A)-Binding Protein I - chemistry | Repressor Proteins - metabolism | Streptavidin - chemistry | Amino Acid Sequence | Repressor Proteins - chemistry | Carbon-Nitrogen Ligases - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group C - genetics | RNA-Binding Proteins - chemistry | ELAV Proteins - metabolism | Gene Expression Regulation | Poly(A)-Binding Protein I - metabolism | Nuclear Matrix-Associated Proteins - metabolism | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Proteome - analysis | Recombinant Fusion Proteins - chemistry | Protein Interaction Mapping | Heterogeneous-Nuclear Ribonucleoprotein Group C - chemistry | Nuclear Matrix-Associated Proteins - genetics | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | HeLa Cells | Escherichia coli Proteins - chemistry | Nuclear Matrix-Associated Proteins - chemistry | ELAV Proteins - genetics | RNA-Binding Proteins - metabolism
Journal Article
Cell Cycle, ISSN 1538-4101, 06/2007, Volume 6, Issue 11, pp. 1288 - 1292
The RNA-binding protein HuR can stabilize and/or regulate the translation of target mRNAs, thereby affecting the cellular responses to immune, proliferative,... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | Bcl-2 | Mcl-1 | mRNA turnover | ProTα | mRNA-binding protein | ELAV | SIRT1 | Translational control | PROTHYMOSIN-ALPHA | FACTOR MESSENGER-RNA | translational control | FOXO TRANSCRIPTION FACTORS | ELAV-LIKE PROTEIN | STABILITY FACTOR | RNA-BINDING PROTEIN | CELL BIOLOGY | CYTOCHROME-C | GENE-EXPRESSION | ProT alpha | TNF-ALPHA | AU-RICH ELEMENT | ELAV-Like Protein 1 | RNA, Small Interfering - genetics | Thymosin - genetics | Humans | Apoptosis - genetics | Thymosin - analogs & derivatives | Gene Expression Profiling | RNA, Messenger - metabolism | ELAV Proteins | Antigens, Surface - physiology | Transfection | Sirtuin 1 | Apoptosis Regulatory Proteins - genetics | Thymosin - biosynthesis | Thymosin - metabolism | Neoplasm Proteins - genetics | RNA Interference - physiology | Sirtuins - genetics | Apoptosis Regulatory Proteins - biosynthesis | Protein Precursors - genetics | RNA-Binding Proteins - physiology | Cell Survival | Neoplasm Proteins - biosynthesis | Sirtuins - physiology | Gene Expression Regulation - physiology | RNA, Small Interfering - physiology | Genes, bcl-2 | Proto-Oncogene Proteins c-bcl-2 - biosynthesis | Protein Precursors - metabolism | Sirtuins - biosynthesis | Protein Precursors - biosynthesis | Myeloid Cell Leukemia Sequence 1 Protein | Protein Binding | Apoptosis - physiology | HeLa Cells | Proto-Oncogene Proteins c-bcl-2 - genetics
Journal Article
Nature Cell Biology, ISSN 1465-7392, 03/2010, Volume 12, Issue 3, pp. 278 - 285
The Notch signalling pathway has a crucial function in determining cell fates in multiple tissues within metazoan organisms(1). On binding to ligands, the... 
COACTIVATOR | PROTEIN | DROSOPHILA MASTERMIND | PHOSPHORYLATION | PATHWAY | HOMOLOG | DIFFERENTIATION | NLK | RECEPTORS | EXPRESSION | CELL BIOLOGY | Phosphorylation - physiology | Xenopus | RNA, Small Interfering - genetics | ELAV-Like Protein 3 | Transcription Factor HES-1 | Protein Interaction Domains and Motifs - physiology | Receptors, Notch - metabolism | Homeodomain Proteins - metabolism | Humans | Embryo, Nonmammalian - metabolism | Receptors, Notch - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Transfection | Basic Helix-Loop-Helix Transcription Factors - metabolism | Nuclear Proteins - genetics | Immunoglobulin J Recombination Signal Sequence-Binding Protein - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Basic Helix-Loop-Helix Transcription Factors - genetics | Zebrafish Proteins - metabolism | ELAV Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Gene Expression Regulation - physiology | Nuclear Proteins - metabolism | Zebrafish | DNA - metabolism | Receptor, Notch1 - metabolism | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Animals | Oligonucleotides, Antisense - genetics | Amino Acid Substitution - physiology | Models, Biological | Neurogenesis - physiology | Cell Line, Tumor | Mitogen-Activated Protein Kinases - genetics | Signal Transduction - physiology | Mice | Zebrafish Proteins - genetics | Receptor, Notch1 - genetics | Mitogen-Activated Protein Kinases - metabolism | Protein Binding - physiology | Physiological aspects | Cellular signal transduction | Genetic aspects | Research | Genetic transcription | Protein kinases
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 25, pp. 10337 - 10342
Spinal muscular atrophy (SMA), caused by the deletion of the SMN1 gene, is the leading genetic cause of infant mortality. SMN protein is present at high levels... 
Axons | Motor neurons | Growth cones | Neuroscience | Messenger RNA | RNA | Neurons | Antibodies | Gene expression regulation | SMN complex proteins | Neuritin | Local protein synthesis | Embryonic lethal abnormal vision drosophila-like 4 (ELAV-L4) | LOCALIZATION | RIBONUCLEOPROTEIN | MULTIDISCIPLINARY SCIENCES | ACTIVITY-DEPENDENT EXPRESSION | IDENTIFICATION | neuritin | GROWTH CONES | TRANSPORT | DETERMINING GENE-PRODUCT | SPINAL MUSCULAR-ATROPHY | IN-VIVO | ASSOCIATION | embryonic lethal abnormal vision Drosophila-like 4 (ELAV-L4) | local protein synthesis | ELAV-Like Protein 4 | Humans | RNA, Messenger - metabolism | Zebrafish - embryology | Recombinant Fusion Proteins - metabolism | Embryo, Mammalian - anatomy & histology | Motor Neurons - cytology | Survival of Motor Neuron 1 Protein - genetics | Neuropeptides - genetics | Animals, Genetically Modified | RNA, Messenger - genetics | Cells, Cultured | ELAV Proteins - metabolism | Axons - metabolism | Neuropeptides - metabolism | Survival of Motor Neuron 1 Protein - metabolism | Nerve Tissue Proteins - genetics | GPI-Linked Proteins - metabolism | Motor Neurons - metabolism | Nerve Tissue Proteins - metabolism | Embryo, Mammalian - physiology | Animals | Axons - pathology | Recombinant Fusion Proteins - genetics | Zebrafish - physiology | Mice | ELAV Proteins - genetics | GPI-Linked Proteins - genetics | Gene mutations | Physiological aspects | Genetic aspects | Research | Health aspects | Risk factors | Spinal muscular atrophy | Biological Sciences
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 02/2017, Volume 16, Issue 2, pp. 999 - 1013
Journal Article
Journal of Cell Science, ISSN 0021-9533, 2017, Volume 130, Issue 21, pp. 3650 - 3662
HuD protein (also known as ELAVL4) has been shown to stabilize mRNAs with AU-rich elements (ARE) in their 3' untranslated regions (UTRs), including Gap43,... 
MRNA transport | Nrn1 | RNA-binding protein | HuD | Axon,mRNAlocalization | COMPLEX | PROTEIN HUD | TRANSCRIPTOME | DISTINCT | mRNA transport | Axon | TRANSLATIONAL CONTROL | CELL BIOLOGY | mRNA localization | NEURITE OUTGROWTH | GAP-43 GENE-EXPRESSION | GROWTH | NEURONS | PC12 CELLS | Male | GAP-43 Protein - genetics | Neurons - ultrastructure | Gene Expression Regulation, Developmental | Base Sequence | Axons - ultrastructure | Hippocampus - ultrastructure | Membrane Proteins - metabolism | Neurons - metabolism | Neuropeptides - genetics | 3' Untranslated Regions | Binding, Competitive | Response Elements | Signal Transduction | ELAV-Like Protein 4 - genetics | GAP-43 Protein - metabolism | Membrane Proteins - genetics | Axons - metabolism | Rats | Neuropeptides - metabolism | Ganglia, Spinal - ultrastructure | Nerve Tissue Proteins - genetics | Rats, Sprague-Dawley | GPI-Linked Proteins - metabolism | Nerve Tissue Proteins - metabolism | ELAV-Like Protein 4 - metabolism | Hippocampus - metabolism | Animals | Protein Binding | Primary Cell Culture | GPI-Linked Proteins - genetics | Ganglia, Spinal - metabolism | Stoichiometry | Neurons | mRNA | Ribonucleic acid--RNA | Embryos | Gene sequencing | HuD protein | Proteins | Dorsal root ganglia | 3' Untranslated regions | Affinity | Localization | Protein interaction | Hippocampus
Journal Article
BBA - Molecular Cell Research, ISSN 0167-4889, 03/2017, Volume 1864, Issue 3, pp. 562 - 571
Posttranslational modifications of certain stress granule (SG) proteins are closely related to the assembly of SGs, a type of cytoplasmic foci structure. Our... 
Phosphorylation | Tudor-SN | C-Jun N-terminal kinase | Stress granules | Stress | COACTIVATOR | PROTEIN | P100 | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | TRANSLATION | CELL BIOLOGY | PHASE | COMPONENT | ARABIDOPSIS | G3BP | AGGREGATION | Arsenites - pharmacology | Oxidative Stress | Humans | JNK Mitogen-Activated Protein Kinases - metabolism | RNA, Messenger - metabolism | Threonine - metabolism | Poly-ADP-Ribose Binding Proteins | RNA Helicases | Receptor, Angiotensin, Type 1 - genetics | ELAV-Like Protein 1 - metabolism | Cytoplasmic Granules - metabolism | JNK Mitogen-Activated Protein Kinases - genetics | Phosphorylation - drug effects | Nuclear Proteins - genetics | RNA Recognition Motif Proteins | JNK Mitogen-Activated Protein Kinases - antagonists & inhibitors | Cytoplasmic Granules - drug effects | RNA, Messenger - genetics | ELAV-Like Protein 1 - genetics | Nuclear Proteins - metabolism | Sodium Compounds - pharmacology | Anthracenes - pharmacology | Carrier Proteins - genetics | DNA Helicases | Carrier Proteins - metabolism | Cytoplasmic Granules - ultrastructure | Receptor, Angiotensin, Type 1 - metabolism | Protein Binding | Protein Kinase Inhibitors - pharmacology | Protein Processing, Post-Translational | HeLa Cells | Mutation | Proteins | Physiological aspects | Protein binding | Arsenic compounds | Analysis
Journal Article