| D008565 |
Membrane Proteins |
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. |
Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell |
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| D011499 |
Protein Processing, Post-Translational |
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. |
Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational |
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| D006031 |
Glycosylation |
The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). |
Protein Glycosylation,Glycosylation, Protein |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000070584 |
Tripartite Motif Proteins |
A protein family defined by the presence of three ZINC FINGER domains, one of which is a RING FINGER DOMAIN, a coiled-coil region, and a highly variable C-terminal region. They function in many cellular processes including APOPTOSIS and CELL CYCLE regulation. |
RBCC Protein,TRIM Protein,Tripartite Motif Protein,RBCC Protein Family,RBCC Proteins,TRIM Protein Family,TRIM Proteins,Family, RBCC Protein,Family, TRIM Protein,Motif Protein, Tripartite,Motif Proteins, Tripartite,Protein Family, RBCC,Protein Family, TRIM,Protein, RBCC,Protein, TRIM,Protein, Tripartite Motif,Proteins, RBCC,Proteins, TRIM,Proteins, Tripartite Motif |
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| D000076106 |
SAM Domain and HD Domain-Containing Protein 1 |
A host restriction triphosphorylhydrolase and dNTPase that contains an N-terminal STERILE ALPHA MOTIF and central, conserved ASPARTATE and HISTIDINE (HD) domain. It acts on single-stranded RNA, yielding deoxynucleosides and triphosphate, and functions in anti-viral defense through its dNTPase activity, reducing cellular dNTP levels below what is required for retroviral reverse transcription in DENDRITIC CELLS and MYELOID CELLS. It also has RIBONUCLEASE activity which blocks early replication of retroviruses such as HIV-1. Mutations in the SAMHD1 gene are associated with type 5 Aicardi-Goutieres syndrome (AGS5) and type 2 chilblain LUPUS (CHBL2). |
SAMHD1 Deoxynucleoside Triphosphate Triphosphohydrolase,SAMHD1 Protein,SAMHD1 dNTPase,SAM Domain and HD Domain Containing Protein 1 |
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| D000090103 |
Antiviral Restriction Factors |
A broad category of endogenous host cellular factors upregulated in response to pathogens (i.e., INTERFERON-stimulated genes) and recruited to interfere with VIRAL REPLICATION and/or trigger host antiviral CELLULAR IMMUNE RESPONSE. |
Antiviral Effectors,Cellular Restriction Factors,Host Cell Restriction Factors,Restriction Factors, Antiviral |
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| D014764 |
Viral Proteins |
Proteins found in any species of virus. |
Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral |
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| D014777 |
Virus Diseases |
A general term for diseases caused by viruses. |
Viral Diseases,Viral Infections,Virus Infections,Disease, Viral,Disease, Virus,Diseases, Viral,Diseases, Virus,Infection, Viral,Infection, Virus,Infections, Viral,Infections, Virus,Viral Disease,Viral Infection,Virus Disease,Virus Infection |
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| D014779 |
Virus Replication |
The process of intracellular viral multiplication, consisting of the synthesis of PROTEINS; NUCLEIC ACIDS; and sometimes LIPIDS, and their assembly into a new infectious particle. |
Viral Replication,Replication, Viral,Replication, Virus,Replications, Viral,Replications, Virus,Viral Replications,Virus Replications |
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