| D009363 |
Neoplasm Proteins |
Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. |
Proteins, Neoplasm |
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| D006258 |
Head and Neck Neoplasms |
Soft tissue tumors or cancer arising from the mucosal surfaces of the LIP; oral cavity; PHARYNX; LARYNX; and cervical esophagus. Other sites included are the NOSE and PARANASAL SINUSES; SALIVARY GLANDS; THYROID GLAND and PARATHYROID GLANDS; and MELANOMA and non-melanoma skin cancers of the head and neck. (from Holland et al., Cancer Medicine, 4th ed, p1651) |
Cancer of Head and Neck,Head Cancer,Head Neoplasm,Head and Neck Cancer,Head and Neck Neoplasm,Neck Cancer,Neck Neoplasm,Neck Neoplasms,Neoplasms, Upper Aerodigestive Tract,UADT Neoplasm,Upper Aerodigestive Tract Neoplasm,Upper Aerodigestive Tract Neoplasms,Cancer of Head,Cancer of Neck,Cancer of the Head,Cancer of the Head and Neck,Cancer of the Neck,Head Neoplasms,Head, Neck Neoplasms,Neoplasms, Head,Neoplasms, Head and Neck,Neoplasms, Neck,UADT Neoplasms,Cancer, Head,Cancer, Neck,Cancers, Head,Cancers, Neck,Head Cancers,Neck Cancers,Neoplasm, Head,Neoplasm, Neck,Neoplasm, UADT,Neoplasms, UADT |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000077195 |
Squamous Cell Carcinoma of Head and Neck |
The most common type of head and neck carcinoma that originates from cells on the surface of the NASAL CAVITY; MOUTH; PARANASAL SINUSES, SALIVARY GLANDS, and LARYNX. Mutations in TNFRSF10B, PTEN, and ING1 genes are associated with this cancer. |
HNSCC,Head And Neck Squamous Cell Carcinomas,Hypopharyngeal Squamous Cell Carcinoma,Laryngeal Squamous Cell Carcinoma,Oral Cavity Squamous Cell Carcinoma,Oral Squamous Cell Carcinoma,Oral Squamous Cell Carcinomas,Oral Tongue Squamous Cell Carcinoma,Oropharyngeal Squamous Cell Carcinoma,Squamous Cell Carcinoma of Larynx,Squamous Cell Carcinoma of the Larynx,Squamous Cell Carcinoma of the Mouth,Squamous Cell Carcinoma of the Nasal Cavity,Carcinoma, Squamous Cell of Head and Neck,Head and Neck Squamous Cell Carcinoma,Squamous Cell Carcinoma of the Head and Neck,Squamous Cell Carcinoma, Head And Neck |
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| D001343 |
Autophagy |
The segregation and degradation of various cytoplasmic constituents via engulfment by MULTIVESICULAR BODIES; VACUOLES; or AUTOPHAGOSOMES and their digestion by LYSOSOMES. It plays an important role in BIOLOGICAL METAMORPHOSIS and in the removal of bone by OSTEOCLASTS. Defective autophagy is associated with various diseases, including NEURODEGENERATIVE DISEASES and cancer. |
Autophagocytosis,ER-Phagy,Lipophagy,Nucleophagy,Reticulophagy,Ribophagy,Autophagy, Cellular,Cellular Autophagy,ER Phagy |
|
| D051907 |
Lysosomal Membrane Proteins |
Ubiquitously expressed integral membrane glycoproteins found in the LYSOSOME. |
LAMP Lysosomal-Associated Membrane Protein,LAMP Lysosomal-Associated Membrane Proteins,Lysosomal Integral Membrane Protein,Lysosomal Membrane Glycoprotein,Lysosomal Membrane Protein,Lysosomal-Associated Membrane Protein,Lysosome-Associated Membrane Glycoprotein,Lysosome-Associated Membrane Glycoproteins,Lysosome-Associated Membrane Protein,Lysosomal Integral Membrane Proteins,Lysosomal Membrane Glycoproteins,Lysosomal-Associated Membrane Proteins,Lysosome-Associated Membrane Proteins,LAMP Lysosomal Associated Membrane Protein,LAMP Lysosomal Associated Membrane Proteins,Lysosomal Associated Membrane Protein,Lysosomal Associated Membrane Proteins,Lysosome Associated Membrane Glycoprotein,Lysosome Associated Membrane Glycoproteins,Lysosome Associated Membrane Protein,Lysosome Associated Membrane Proteins,Membrane Glycoprotein, Lysosomal,Membrane Glycoprotein, Lysosome-Associated,Membrane Glycoproteins, Lysosomal,Membrane Glycoproteins, Lysosome-Associated,Membrane Protein, Lysosomal,Membrane Protein, Lysosomal-Associated,Membrane Protein, Lysosome-Associated,Membrane Proteins, Lysosomal,Membrane Proteins, Lysosomal-Associated,Membrane Proteins, Lysosome-Associated |
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| D059666 |
Lysosomal-Associated Membrane Protein 3 |
A lysosomal-associated membrane glycoprotein that is expressed at high levels in mature DENDRITIC CELLS. |
Antigens, CD208,CD208 Antigens,DC-LAMP Protein,LAMP-3 Protein,DC LAMP Protein,LAMP 3 Protein,Lysosomal Associated Membrane Protein 3 |
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| D035683 |
MicroRNAs |
Small double-stranded, non-protein coding RNAs, 21-25 nucleotides in length generated from single-stranded microRNA gene transcripts by the same RIBONUCLEASE III, Dicer, that produces small interfering RNAs (RNA, SMALL INTERFERING). They become part of the RNA-INDUCED SILENCING COMPLEX and repress the translation (TRANSLATION, GENETIC) of target RNA by binding to homologous 3'UTR region as an imperfect match. The small temporal RNAs (stRNAs), let-7 and lin-4, from C. elegans, are the first 2 miRNAs discovered, and are from a class of miRNAs involved in developmental timing. |
RNA, Small Temporal,Small Temporal RNA,miRNA,stRNA,Micro RNA,MicroRNA,Primary MicroRNA,Primary miRNA,miRNAs,pre-miRNA,pri-miRNA,MicroRNA, Primary,RNA, Micro,Temporal RNA, Small,miRNA, Primary,pre miRNA,pri miRNA |
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