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PLoS Pathogens, ISSN 1553-7366, 12/2015, Volume 11, Issue 12
  Reverse transcription is the central defining feature of HIV-1 replication. We previously reported that the cellular eukaryotic elongation factor 1 (eEF1)... 
Mutation | Plasmids | Human immunodeficiency virus--HIV | Genes
Journal Article
Immunity, ISSN 1074-7613, 10/2017, Volume 47, Issue 4, pp. 739 - 751.e5
Infection by helminth parasites is associated with amelioration of allergic reactivity, but mechanistic insights into this association are lacking. Products... 
immunomodulation | allergy | parasite | asthma | helminth | IL-33 | PRODUCTS | INFLAMMATION | DNA | CCP MODULES | TYPE-2 IMMUNITY | ASTHMA | LARGE-SCALE | CYTOKINE | INNATE LYMPHOID-CELLS | IMMUNOLOGY | Strongylida Infections - metabolism | Humans | Nematospiroides dubius - metabolism | Eosinophils - immunology | Interleukin-33 - immunology | Nematospiroides dubius - immunology | Receptors, Interleukin - metabolism | Lymphocytes - immunology | Allergens - immunology | Strongylida Infections - parasitology | Strongylida Infections - immunology | Helminth Proteins - metabolism | Amino Acid Sequence | Nematospiroides dubius - genetics | Receptors, Interleukin - immunology | Mice, Inbred C57BL | Helminth Proteins - genetics | Host-Parasite Interactions - immunology | Protein Binding - immunology | Blotting, Western | Mice, Knockout | Sequence Homology, Amino Acid | Alternaria - immunology | Immunity, Innate - immunology | Interleukin-33 - genetics | Animals | Helminth Proteins - immunology | Interleukin-33 - metabolism | Mice, Inbred BALB C | Interleukins | Allergens | Autoimmunity | Allergy | Medical research | Resveratrol | Medicine, Experimental | Research institutes | Allergic reaction | Cells | Food allergies | Fractionation | Candidates | Immune response | Disease | Cytokines | Leukocytes (eosinophilic) | Interleukin | Hypersensitivity | Tethering | Infections | Parasites | Immunity | Asthma | Macular degeneration | Proteins | Studies | Gangrene | Deoxyribonucleic acid--DNA | Viral infections | Predictive control | Apoptosis | Recombinant | Life Sciences | Immunology
Journal Article
Gut, ISSN 0017-5749, 05/2013, Volume 62, Issue 5, pp. 695 - 707
Objective Mutations in the nucleotide-binding oligomerisation domain-containing protein 2 (NOD2) gene remain the strongest genetic determinants for Crohn's... 
PATHWAYS | CELLS | INVASIVE ESCHERICHIA-COLI | DISEASE | ILEAL MUCOSA | LEUCINE-RICH REPEAT | AUTOPHAGY | GASTROENTEROLOGY & HEPATOLOGY | NF-KAPPA-B | EXPRESSION | BINDING | Crohn Disease - genetics | Disease Susceptibility | Epithelial Cells - metabolism | Frameshift Mutation | Immunoprecipitation | Colon - pathology | Vimentin - metabolism | Epithelial Cells - drug effects | Humans | Crohn Disease - metabolism | Nod2 Signaling Adaptor Protein - genetics | Colon - metabolism | Nod2 Signaling Adaptor Protein - metabolism | Withanolides - pharmacology | Crohn Disease - pathology | Vimentin - genetics | HEK293 Cells | Crohn Disease - physiopathology | Polymorphism, Single Nucleotide | Microscopy, Fluorescence | Physiological aspects | Development and progression | Genetic aspects | Crohn's disease | Research | NOD2 | Intermediate filament proteins | Plasma | Immunoglobulins | Yeast | Pathogenesis | Genes | Genomes | Autophagy | Crohns disease | Proteins | Studies | Tuberculosis | E coli | Plasmids | Biopsy | Mutation | Localization | autophagy | E.coli | vimentin | genetic association studies | inflammatory bowel disease | Crohn’s disease | Clinical Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Gastroenterologi | Internal Medicine | Invärtesmedicin | Klinisk medicin | Gastroenterology and Hepatology
Journal Article
Journal of Cell Science, ISSN 0021-9533, 02/2018, Volume 131, Issue 4, pp. jcs211748 - jcs211748
Retinitis pigmentosa 2 (RP2) is the causative gene for a form of X-linked retinal degeneration. RP2 was previously shown to have GTPase-activating protein... 
OSTF1 | Actin | Retinitis pigmentosa | RP2 | CELL MOTILITY | CRYSTAL-STRUCTURE | MYOSIN 1E | PLASMA-MEMBRANE | PROTEIN RP2 | CELL BIOLOGY | OSTEOCLAST-STIMULATING FACTOR | EVOLUTIONARY CONSERVATION | LINKED RETINITIS-PIGMENTOSA | PHOTORECEPTOR DEGENERATION | GENE-PRODUCT | Protein Binding - genetics | Retina - metabolism | Humans | Eye Proteins - chemistry | Cell Membrane - genetics | Protein Domains - genetics | Cell Movement - genetics | Actins - genetics | HEK293 Cells | Actins - chemistry | Cell Membrane - metabolism | Myosin Type I - chemistry | Eye Proteins - genetics | ADP-Ribosylation Factors - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein Structure, Tertiary | Cell Line | Myosin Type I - genetics | Membrane Proteins - genetics | Retinal Degeneration - genetics | Retinitis Pigmentosa - genetics | Retinitis Pigmentosa - metabolism | Binding Sites - genetics | Cilia - metabolism | Cilia - genetics | Proteins - genetics | ADP-Ribosylation Factors - chemistry | Membrane Proteins - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Protein Conformation | Molecular Docking Simulation | Proteins - chemistry | Retinal Degeneration - pathology | Retina - pathology | Retinitis Pigmentosa - pathology | Motility | Pathogenesis | Retina | C-Terminus | Proteins | Biomedical materials | GTPase-activating protein | N-Terminus | Retinal degeneration | Biocompatibility | Retinitis | Degeneration | Mutation | Binding sites | Cell migration | Guanosinetriphosphatase
Journal Article
Biology Direct, ISSN 1745-6150, 11/2013, Volume 8, Issue 1
Translation elongation factors eEF1A1 and eEF1A2 are 92% identical but exhibit non-overlapping expression patterns. While the two proteins are predicted to... 
Post-translational modification | Translation elongation factors | Research | Gene expression | Analysis | Ubiquitin | DNA binding proteins | Methylation | Acetates | Genetic translation
Journal Article
Journal Article