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eukaryotic initiation factor-4g - metabolism (278) 278
animals (253) 253
biochemistry & molecular biology (243) 243
humans (234) 234
index medicus (200) 200
protein biosynthesis (170) 170
eukaryotic initiation factor-4g (154) 154
translation initiation (128) 128
phosphorylation (121) 121
eukaryotic initiation factor-4g - genetics (119) 119
peptide initiation factors - metabolism (119) 119
protein binding (119) 119
messenger-rna (116) 116
rna, messenger - metabolism (102) 102
eukaryotic initiation factor-4e - metabolism (96) 96
molecular sequence data (92) 92
cell biology (88) 88
amino acid sequence (75) 75
rna, messenger - genetics (74) 74
phosphoproteins - metabolism (71) 71
binding sites (68) 68
mice (68) 68
male (65) 65
eif4g (64) 64
protein-synthesis (63) 63
cell line (60) 60
article (59) 59
hela cells (57) 57
protein synthesis (57) 57
rats (56) 56
proteins (54) 54
ribosomes - metabolism (54) 54
translation (54) 54
eukaryotic initiation factor-4g - chemistry (52) 52
eukaryotic initiation factor-4e (51) 51
viruses (51) 51
base sequence (50) 50
carrier proteins - metabolism (50) 50
poly-binding protein (48) 48
rna (48) 48
in-vitro (47) 47
peptide chain initiation, translational (47) 47
peptide initiation factors - genetics (47) 47
saccharomyces-cerevisiae (47) 47
genetic translation (45) 45
protein biosynthesis - physiology (44) 44
factor 4g eif4g (43) 43
gene-expression (43) 43
protein structure, tertiary (43) 43
physiology (42) 42
mutation (41) 41
rna-binding proteins - metabolism (41) 41
gene expression (40) 40
rna caps - metabolism (40) 40
binding-protein (39) 39
messenger-rna translation (38) 38
protein biosynthesis - drug effects (38) 38
environment and public health (37) 37
in-vivo (37) 37
models, molecular (36) 36
research (36) 36
yeast (36) 36
apoptosis (35) 35
eif4e (35) 35
initiation (35) 35
molecular biology (34) 34
research article (34) 34
endocrinology & metabolism (33) 33
rats, sprague-dawley (33) 33
eukaryotic initiation factor-4e - genetics (31) 31
tor serine-threonine kinases (31) 31
eukaryotic initiation factor-4a - metabolism (30) 30
peptide fragments - metabolism (30) 30
virology (30) 30
complex (29) 29
kinetics (29) 29
physiological aspects (29) 29
cap-dependent translation (28) 28
female (28) 28
insulin (28) 28
muscle, skeletal - metabolism (28) 28
protein kinases - metabolism (28) 28
binding (27) 27
cells (27) 27
cells, cultured (27) 27
eukaryotic initiation factor-4g - physiology (27) 27
eukaryotic translation (27) 27
expression (27) 27
initiation-factor 4g (27) 27
mammalian target (27) 27
rabbits (27) 27
saccharomyces cerevisiae - metabolism (27) 27
signal transduction (27) 27
biophysics (26) 26
cell line, tumor (26) 26
messenger rna (26) 26
phosphorylation - drug effects (26) 26
recombinant proteins - metabolism (26) 26
sirolimus - pharmacology (26) 26
blotting, western (25) 25
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1. Full Text Angiogenin-Induced tRNA Fragments Inhibit Translation Initiation
by Ivanov, Pavel and Emara, Mohamed M and Villen, Judit and Gygi, Steven P and Anderson, Paul
Molecular Cell, ISSN 1097-2765, 2011, Volume 43, Issue 4, pp. 613 - 623
Angiogenin is a stress-activated ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs). Transfection... 
ENCEPHALOMYOCARDITIS VIRUS | OXIDATIVE STRESS | MESSENGER-RNA | IRES | BIOCHEMISTRY & MOLECULAR BIOLOGY | EIF4G | INTERNAL INITIATION | CLEAVAGE | BINDING | ASSOCIATION | RIBOSOMAL ENTRY SITE | CELL BIOLOGY | Cell Line | Ribonuclease, Pancreatic - physiology | RNA, Transfer - physiology | Y-Box-Binding Protein 1 - metabolism | Humans | Y-Box-Binding Protein 1 - physiology | Stress, Physiological | Peptide Chain Initiation, Translational | Eukaryotic Initiation Factor-4G - metabolism | RNA, Transfer - chemistry | Eukaryotic Initiation Factor-4G - physiology | Angiogenin
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2. Full Text Essential role for eIF4GI overexpression in the pathogenesis of inflammatory breast cancer
by Goldberg, Judith and Silvera, Deborah and Schneider, Robert J and Zolfaghari, Ladan and Hochman, Tsivia and Arju, Rezina and Levine, Paul H and Darvishian, Farbod and Formenti, Silvia C
Nature Cell Biology, ISSN 1465-7392, 07/2009, Volume 11, Issue 7, pp. 903 - 908
Inflammatory breast cancer (IBC) is the most lethal form of primary breast cancer. IBC lethality derives from generation of tumour emboli, which are... 
LUNG | INITIATION-FACTOR EIF-4E | ANGIOGENESIS | E-CADHERIN EXPRESSION | RHOC-GTPASE | PHENOTYPE | TRANSLATION INITIATION | PROLIFERATION | CARCINOMA | MAMMARY EPITHELIAL-CELLS | CELL BIOLOGY | Immunohistochemistry | Cell Adhesion Molecules - genetics | Cadherins - metabolism | Humans | Immunoblotting | Eukaryotic Initiation Factor-4G - metabolism | Phosphoproteins - metabolism | Breast Neoplasms - metabolism | Catenins | Female | Biological Transport - genetics | Cadherins - genetics | Eukaryotic Initiation Factor-4G - physiology | Gene Expression Regulation, Neoplastic - physiology | Gene Expression Regulation, Neoplastic - genetics | Cell Line | Phosphoproteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Cell Adhesion Molecules - metabolism | Microscopy, Confocal | Animals | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Mice, Nude | Cell Line, Tumor | Biological Transport - physiology | Eukaryotic Initiation Factor-4G - genetics | Mice | Control | Development and progression | Genetic aspects | Breast cancer | Metastasis | Research | Gene expression | Risk factors
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3. Full Text Intra-axonal synthesis of eukaryotic translation initiation factors regulates local protein synthesis and axon growth in rat sympathetic neurons
by Kar, Amar N and Macgibeny, Margaret A and Gervasi, Noreen M and Gioio, Anthony E and Kaplan, Barry B
Journal of Neuroscience, ISSN 0270-6474, 04/2013, Volume 33, Issue 17, pp. 7165 - 7174
Axonal protein synthesis is a complex process involving selective mRNA localization and translational regulation. In this study, using in situ hybridization... 
LOCALIZATION | PHOSPHORYLATION | CONE COLLAPSE | DISTAL AXONS | DISTINCT | ACTIN MESSENGER-RNA | BETA-ACTIN | IDENTIFICATION | FACILITATION | NEUROSCIENCES | APLYSIA | Eukaryotic Initiation Factor-2B - biosynthesis | Cells, Cultured | Protein Biosynthesis - physiology | Axons - metabolism | Rats | Adrenergic Fibers - physiology | Male | Axons - physiology | Rats, Sprague-Dawley | Superior Cervical Ganglion - metabolism | Down-Regulation - physiology | Superior Cervical Ganglion - physiology | Eukaryotic Initiation Factor-4G - biosynthesis | Eukaryotic Initiation Factor-4G - antagonists & inhibitors | Animals | Eukaryotic Initiation Factor-2B - physiology | Female | Adrenergic Fibers - metabolism | Eukaryotic Initiation Factor-4G - physiology | Eukaryotic Initiation Factor-2B - antagonists & inhibitors
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4. Full Text Duplex Unwinding and ATPase Activities of the DEAD-Box Helicase eIF4A Are Coupled by eIF4G and eIF4B
by Özeş, Ali R and Feoktistova, Kateryna and Avanzino, Brian C and Fraser, Christopher S
Journal of Molecular Biology, ISSN 0022-2836, 2011, Volume 412, Issue 4, pp. 674 - 687
Eukaryotic initiation factor (eIF) 4A is a DEAD-box helicase that stimulates translation initiation by unwinding mRNA secondary structure. The accessory... 
translation | protein synthesis | ribosome | initiation | RECRUITMENT | COMPLEX | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CORE DOMAIN | KINETIC CHARACTERIZATION | PROTEIN EIF4A | MESSENGER-RNA STRUCTURE | BINDING | Eukaryotic Initiation Factors - chemistry | Eukaryotic Initiation Factors - metabolism | Protein Structure, Tertiary | Humans | Base Composition - physiology | Adenosine Triphosphatases - metabolism | Models, Molecular | Eukaryotic Initiation Factor-4G - metabolism | Nucleic Acid Heteroduplexes - metabolism | Nucleic Acid Heteroduplexes - chemistry | Hydrolysis | DNA Helicases - metabolism | Eukaryotic Initiation Factors - physiology | Models, Biological | Base Pairing - physiology | Eukaryotic Initiation Factor-4A - chemistry | Eukaryotic Initiation Factor-4G - chemistry | DEAD-box RNA Helicases - metabolism | Eukaryotic Initiation Factor-4A - metabolism | Adenosine Triphosphatases - physiology | DEAD-box RNA Helicases - chemistry | Enzyme Activation - physiology | Eukaryotic Initiation Factor-4G - physiology | DNA Helicases - physiology | Proteins | Protein biosynthesis | RNA | Adenosine triphosphatase | Translation | Ribosome | Protein synthesis | Initiation
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5. Full Text Scd6 Targets eIF4G to Repress Translation: RGG Motif Proteins as a Class of eIF4G-Binding Proteins
by Rajyaguru, Purusharth and She, Meipei and Parker, Roy
Molecular Cell, ISSN 1097-2765, 01/2012, Volume 45, Issue 2, pp. 244 - 254
The formation of mRNPs controls the interaction of the translation and degradation machinery with individual mRNAs. The yeast Scd6 protein and its orthologs... 
YEAST | MESSENGER-RNA TRANSLATION | P-BODY FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | BINDING-PROTEIN | BODIES | INITIATION-FACTOR 4E | COMPONENT | SACCHAROMYCES-CEREVISIAE | STRESS GRANULES | CELL BIOLOGY | Fungal Proteins - physiology | Protein Biosynthesis | Eukaryotic Initiation Factor-4E - physiology | Eukaryotic Initiation Factor-4E - metabolism | Models, Genetic | Eukaryotic Initiation Factor-4G - metabolism | Fungal Proteins - genetics | RNA, Messenger - metabolism | Eukaryotic Initiation Factor-4G - physiology | Amino Acid Motifs | Fungal Proteins - metabolism | Caenorhabditis elegans | Messenger RNA | Chemical properties | Binding proteins | Genetic translation | Protein binding
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6. Full Text MiRNA repression of translation in vitro takes place during 43S ribosomal scanning
by Ricci, Emiliano P and Limousin, Taran and Soto-Rifo, Ricardo and Rubilar, Paulina S and Decimo, Didier and Ohlmann, Théophile
Nucleic Acids Research, ISSN 0305-1048, 01/2013, Volume 41, Issue 1, pp. 586 - 598
microRNAs (miRNAs) regulate gene expression at multiple levels by repressing translation, stimulating deadenylation and inducing the premature decay of target... 
POLY(A)-DEPENDENT TRANSLATION | INITIATION | LET-7 MICRORNA | HUMAN-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | POLY(A)-BINDING PROTEIN | BINDING-PROTEIN | HIV-1 PROTEASE | MAMMALIAN MESSENGER-RNAS | PROTEIN-SYNTHESIS | HEPATITIS-C | Poly(A)-Binding Proteins - physiology | Protein Biosynthesis | Gene Expression Regulation | Hepacivirus - genetics | MicroRNAs - metabolism | Peptide Chain Initiation, Translational | RNA Stability | RNA, Messenger - metabolism | Peptides - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | 5' Untranslated Regions | Proteasome Endopeptidase Complex - metabolism | Ribosome Subunits, Small, Eukaryotic - metabolism | Eukaryotic Initiation Factor-4G - physiology | Peptides | Ribosome Subunits, Small, Eukaryotic | Proteasome Endopeptidase Complex | Life Sciences | Eukaryotic Initiation Factor-4G | MicroRNAs | Ribosome Subunits, Large, Eukaryotic | RNA, Messenger | Hepacivirus | Poly(A)-Binding Proteins | RNA
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7. Full Text Mutation of Eif4g3, encoding a eukaryotic translation initiation factor, causes male infertility and meiotic arrest of mouse spermatocytes
by Sun, Fengyun and Palmer, Kristina and Handel, Mary Ann
Development, ISSN 0950-1991, 05/2010, Volume 137, Issue 10, pp. 1699 - 1707
The ENU-induced repro8 mutation was identified in a screen to uncover genes that control mouse gametogenesis. repro8 causes male-limited infertility, with... 
Meiosis | Mouse | Spermatogenesis | Translation initiation | CYCLIN A1 | HSP70-2 | TRANSCRIPTION FACTOR-1 | MALE GERM-CELLS | SPERMATOGENIC CELLS | DEVELOPMENTAL BIOLOGY | MAMMALIAN MEIOSIS | HEAT-SHOCK-PROTEIN | MESSENGER-RNA | EXPRESSION | BINDING | Cell Division - genetics | Cell Proliferation | Spermatocytes - metabolism | Spermatogenesis - genetics | Mice, Inbred C57BL | HSP70 Heat-Shock Proteins - genetics | Male | Mice, Transgenic | Eukaryotic Initiation Factor-4G - metabolism | Mice, Inbred C3H | HSP70 Heat-Shock Proteins - metabolism | Meiosis - genetics | Spermatocytes - physiology | Mutation, Missense - physiology | Phenotype | Spermatogenesis - physiology | Animals | Infertility, Male - genetics | Gene Expression Regulation, Developmental | Eukaryotic Initiation Factor-4G - genetics | Mice | Mice, Congenic | Eukaryotic Initiation Factor-4G - physiology
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8. Full Text Requirement of mammalian target of rapamycin complex 1 downstream effectors in cued fear memory reconsolidation and its persistence
by Huynh, Thu N and Santini, Emanuela and Klann, Eric
Journal of Neuroscience, ISSN 0270-6474, 2014, Volume 34, Issue 27, pp. 9034 - 9039
Memory retrieval, often termed reconsolidation, can render previously consolidated memories susceptible to manipulation that can lead to alterations in memory... 
Reconsolidation | Long-term memory | MTORC1 | Translation | Consolidation | Fear conditioning | fear conditioning | TRANSLATION INITIATION | MECHANISMS | consolidation | reconsolidation | long-term memory | NEUROSCIENCES | MTOR | HIPPOCAMPUS | SYNAPTIC PROTEIN-DEGRADATION | INHIBITION | REACTIVATION | translation | S6 KINASE | mTORC1 | AMYGDALA | Ribosomal Protein S6 Kinases, 90-kDa - deficiency | Male | Fear - physiology | Mechanistic Target of Rapamycin Complex 1 | Eukaryotic Initiation Factor-4G - antagonists & inhibitors | Nitro Compounds - pharmacology | TOR Serine-Threonine Kinases - physiology | Ribosomal Protein S6 Kinases, 90-kDa - physiology | Eukaryotic Initiation Factor-4G - physiology | Cues | Conditioning, Classical - drug effects | Acoustic Stimulation | Mice, Inbred C57BL | Eukaryotic Initiation Factor-4E - physiology | Hydrazones | Memory, Long-Term - drug effects | Imidazoles - pharmacology | Avoidance Learning - physiology | Mental Recall - drug effects | Memory, Long-Term - physiology | Conditioning, Classical - physiology | Eukaryotic Initiation Factor-4E - antagonists & inhibitors | Piperazines - pharmacology | Sirolimus - pharmacology | Mice, Knockout | Multiprotein Complexes - physiology | Animals | Mental Recall - physiology | Avoidance Learning - drug effects | Mice | Thiazoles - pharmacology | Electroshock | Brief Communications
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9. Full Text Functional overlap between eIF4G isoforms in Saccharomyces cerevisiae
by Clarkson, Bryan K and Gilbert, Wendy V and Doudna, Jennifer A
PLoS ONE, ISSN 1932-6203, 02/2010, Volume 5, Issue 2, p. e9114
Initiation factor eIF4G is a key regulator of eukaryotic protein synthesis, recognizing proteins bound at both ends of an mRNA to help recruit messages to the... 
YEAST TRANSCRIPTOME | MESSENGER-RNA | HELICASE ACTIVITY | BIOLOGY | INITIATION-FACTOR 4G | DEPENDENT TRANSLATION | RIBOSOMAL-RNA SYNTHESIS | EUKARYOTIC TRANSLATION | PROTEIN-SYNTHESIS | CYTOPLASMIC PROCESSING BODIES | CAP-INDEPENDENT TRANSLATION | Sequence Deletion | Protein Biosynthesis | Oligonucleotide Array Sequence Analysis | Saccharomyces cerevisiae - genetics | Molecular Sequence Data | Gene Expression Profiling | Eukaryotic Initiation Factor-4G - metabolism | Eukaryotic Initiation Factor-4F - metabolism | Saccharomyces cerevisiae - metabolism | Protein Isoforms - metabolism | Base Sequence | Eukaryotic Initiation Factor-4G - physiology | Cell Division - genetics | Gene Expression Regulation, Fungal | Saccharomyces cerevisiae - physiology | Eukaryotic Initiation Factor-4F - physiology | Eukaryotic Initiation Factor-4F - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Isoforms - physiology | Cell Division - physiology | Saccharomyces cerevisiae Proteins - metabolism | Polyribosomes - metabolism | Eukaryotic Initiation Factor-4G - genetics | Saccharomyces cerevisiae Proteins - physiology | Mutation | Protein Isoforms - genetics | Proteins | DNA microarrays | RNA | Analysis | Genomics | Protein biosynthesis | Genetic translation | Protein binding | Poly(A) | Translation | Yeast | Messages | Translation initiation | Genomes | Biology | mRNA | Saccharomyces | Experiments | Eukaryotes | Clonal deletion | Protein synthesis | Isoforms | Phylogenetics | Deletion | Books | Localization | Bioinformatics | Bayesian analysis | Saccharomyces cerevisiae | Initiation factor eIF-4G
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10. Full Text Targets and mechanisms for the regulation of translation in malignant transformation
by Clemens, Michael J
Oncogene, ISSN 0950-9232, 04/2004, Volume 23, Issue 18, pp. 3180 - 3188
There is increasing evidence that deregulation of gene expression at the level of mRNA translation can contribute to cell transformation and the malignant... 
eIF4E-binding proteins | TNF family | PKR | eIF2 | Oncogenic viruses | p53 | TRANSCRIPTIONAL ACTIVATION | INDUCED APOPTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | EIF2-ALPHA PHOSPHORYLATION | DEPENDENT PROTEIN-KINASE | INITIATION-FACTOR 4E | CELL BIOLOGY | TUMOR-NECROSIS-FACTOR | CAP-BINDING PROTEIN | HEPATITIS-C VIRUS | MESSENGER-RNA | ONCOLOGY | GENETICS & HEREDITY | oncogenic viruses | EPSTEIN-BARR-VIRUS | Carrier Proteins - physiology | Protein Biosynthesis | Humans | Eukaryotic Initiation Factor-4E - physiology | Eukaryotic Initiation Factor-2 - physiology | Tumor Suppressor Protein p53 - physiology | Adaptor Proteins, Signal Transducing | Animals | eIF-2 Kinase - physiology | Cell Transformation, Neoplastic - genetics | Phosphoproteins - physiology | Eukaryotic Initiation Factor-4G - physiology | Apoptosis
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11. Full Text TOR Deficiency in C. elegans Causes Developmental Arrest and Intestinal Atrophy by Inhibition of mRNA Translation
by Long, Xiaomeng and Spycher, Carmen and Han, Z.Stanley and Rose, Ann M and Müller, Fritz and Avruch, Joseph
Current Biology, ISSN 0960-9822, 09/2002, Volume 12, Issue 17, pp. 1448 - 1461
Background: TOR is a phosphatidylinositol kinase (PIK)-related kinase that controls cell growth and proliferation in response to nutritional cues. We describe... 
RAPAMYCIN | CATALYTIC SUBUNIT | CAENORHABDITIS-ELEGANS | SIGNALING PATHWAY | PHOSPHATIDYLINOSITOL 3-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | PROTEIN PHOSPHATASE 2A | CELL-GROWTH | S6 KINASE | AGE-1 PI3 KINASE | Eukaryotic Initiation Factor-4G - deficiency | Protein Biosynthesis | Species Specificity | Ribosomal Protein S6 Kinases, 70-kDa - physiology | Genetic Complementation Test | Atrophy | Genes, Lethal | Eukaryotic Initiation Factor-2 - deficiency | RNA Interference | Adaptation, Physiological - genetics | Gene Expression Regulation, Developmental | Eukaryotic Initiation Factor-4G - physiology | Ribosomal Protein S6 Kinases, 70-kDa - deficiency | Gene Targeting | Starvation | Intestines - pathology | Caenorhabditis elegans - growth & development | Caenorhabditis elegans - genetics | Phosphotransferases (Alcohol Group Acceptor) - isolation & purification | RNA, Messenger - genetics | Intestines - growth & development | Ribosomal Protein S6 Kinases, 70-kDa - genetics | Phosphotransferases (Alcohol Group Acceptor) - genetics | Caenorhabditis elegans Proteins - isolation & purification | Eukaryotic Initiation Factor-2 - physiology | Sirolimus - pharmacology | Sequence Homology, Amino Acid | Phenotype | Animals | Larva | Alleles | Caenorhabditis elegans Proteins - physiology | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans Proteins - pharmacology | Phosphotransferases (Alcohol Group Acceptor) - pharmacology
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12. Full Text PABP interacting protein 2A (PAIP2A) regulates specific key proteins during spermiogenesis in the mouse
by Delbes, Geraldine and Yanagiya, Akiko and Sonenberg, Nahum and Robaire, Bernard
Biology of Reproduction, ISSN 0006-3363, 03/2012, Volume 86, Issue 3, p. 95
During spermiogenesis, expression of the specific proteins needed for proper differentiation of male germ cells is under translational control. We have shown... 
Proteomics | Elongated spermatids | Gene expression | Tail structure | PAIP2A | Spemiogenesis | Translational control | POLY(A) BINDING-PROTEIN | proteomics | MALE GERM-CELLS | SPERMATOGENIC CELLS | tail structure | translational control | RAT TESTIS | TRANSFERASE YO SUBUNIT | T-COMPLEX GENE | MESSENGER-RNAS | IMMUNOCYTOCHEMICAL LOCALIZATION | REPRODUCTIVE BIOLOGY | TRANSLATIONAL REPRESSION | spemiogenesis | elongated spermatids | gene expression | FIBROUS SHEATH | Carrier Proteins - physiology | Flagella - physiology | Hexokinase - physiology | Spermatogenesis - genetics | Male | Gene Expression Profiling | Fertility - physiology | Mice, Knockout | A Kinase Anchor Proteins - genetics | A Kinase Anchor Proteins - physiology | Carrier Proteins - genetics | Tumor Suppressor Proteins - physiology | Fertility - genetics | Spermatogenesis - physiology | Animals | Sperm Motility - physiology | Tumor Suppressor Proteins - genetics | Models, Animal | Eukaryotic Initiation Factor-4G - genetics | Mice | Hexokinase - genetics | Eukaryotic Initiation Factor-4G - physiology
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13. Full Text Characterization of the Role of eIF4G in Stimulating Cap- and IRES-Dependent Translation in Aplysia Neurons
by Dyer, John and Sossin, Wayne S
PLoS ONE, ISSN 1932-6203, 09/2013, Volume 8, Issue 9, p. e74085
The rate-limiting step(s) of translation in the nervous system have not been clearly identified. We have been examining this question in the cell body of the... 
INITIATION | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | KINASE | SITES | EUKARYOTES | MECHANISMS | HELICASE | CANCER | PLASTICITY | Aplysia | Protein Biosynthesis | Animals | 5' Untranslated Regions | Open Reading Frames | Cells, Cultured | Cloning, Molecular | RNA Caps | Ribosomes - metabolism | Eukaryotic Initiation Factor-4G - genetics | Sensory Receptor Cells - metabolism | Eukaryotic Initiation Factor-4G - physiology | RNA | Neurons | Genetic translation | Protein-protein interactions | Internal ribosome entry site | Translation | Phosphorylation | Synaptic strength | Methionine | Fluorescence | Amino acids | Nervous system | mRNA | Neurosurgery | Kinases | Gene expression | Constraining | Proteins | Signal transduction | Coding | Sensory neurons | Cell body | Initiation factor eIF-4G | Elongation | Binding sites
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14. Full Text Translational control of meiotic cell cycle progression and spermatid differentiation in male germ cells by a novel eIF4G homolog
by Catherine C. Baker and Margaret T. Fuller
Development, ISSN 0950-1991, 08/2007, Volume 134, Issue 15, pp. 2863 - 2869
Translational control is crucial for proper timing of developmental events that take place in the absence of transcription, as in meiotic activation in... 
SPERMATOGENESIS | TRANSFORMATION | DOMAIN | meiosis | PROTEIN | eIF4G | cell cycle | DROSOPHILA-MELANOGASTER | Drosophila | TRANSCRIPTION | spermatocyte | DEVELOPMENTAL BIOLOGY | translational control | DON-JUAN | ELEMENT | MESSENGER-RNA | ASSOCIATION | Cell Cycle - genetics | Protein Biosynthesis | Animals, Genetically Modified | Cells, Cultured | Male | Testis - growth & development | Sequence Homology, Amino Acid | Cell Differentiation - genetics | Meiosis - genetics | Drosophila Proteins - physiology | Fertility - genetics | Animals | Gene Expression Regulation, Developmental | Spermatids - cytology | Eukaryotic Initiation Factor-4G - genetics | Spermatozoa - cytology | Drosophila Proteins - genetics | Eukaryotic Initiation Factor-4G - physiology | Drosophila - genetics | Meiosis | Spermatocyte | Translational control | Cell cycle
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15. Full Text Structural Basis for Inhibition of Translation by the Tumor Suppressor Pdcd4
by Nicole LaRonde-LeBlanc and Arti N. Santhanam and Alyson R. Baker and Alexander Wlodawer and Nancy H. Colburn
Molecular and Cellular Biology, ISSN 0270-7306, 01/2007, Volume 27, Issue 1, pp. 147 - 156
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
EIF4A | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | INITIATION-FACTOR 4G | VHS DOMAIN | MESSENGER-RNA DECAY | TRANSFORMATION SUPPRESSOR | BINDING | TUMORIGENESIS | EXPRESSION | CARCINOMA | CELL BIOLOGY | Protein Structure, Tertiary | Amino Acid Sequence | Phosphorylation | Protein Biosynthesis | Mutagenesis, Site-Directed | RNA-Binding Proteins - physiology | Apoptosis Regulatory Proteins - chemistry | RNA-Binding Proteins - chemistry | Gene Expression Regulation | Models, Molecular | Molecular Sequence Data | Eukaryotic Initiation Factor-4A - physiology | Sequence Homology, Amino Acid | Two-Hybrid System Techniques | Protein Binding | Apoptosis Regulatory Proteins - physiology | Protein Conformation | Eukaryotic Initiation Factor-4G - physiology
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