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  • ¿µ¹®
    ÇѱÛ
  • cellular oncogene
    ¼¼Æ÷Á¾¾çÀ¯ÀüÀÚ
  • oncogene
    Á¾¾çÀ¯ÀüÀÚ
  • signaling oncogene
    ½ÅÈ£Á¾¾çÀ¯ÀüÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • oncogene
    Á¾¾çÀ¯ÀüÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • cellular oncogene
    ¼¼Æ÷Á¾¾çÀ¯ÀüÀÚ
  • oncogene
    Á¾¾çÀ¯ÀüÀÚ, Á¾¾ç¿ø
  • signaling oncogene
    ½ÅÈ£Á¾¾çÀ¯ÀüÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • G-proteins
    G-´Ü¹é(Ó±ÛÜ)
  • g proteins
    G ´Ü¹é
  • g-proteins
    G´Ü¹éÁú
  • guanosine triphosphate(gtp)-bindting proteins
    »ïÀλ걸¾Æ³ë½Å°áÇմܹéÁú
  • Erb-A oncogene
    Erb-A ¾ÏÀ¯ÀüÀÚ
  • Erb-B oncogene
    Erb-B ¾ÏÀ¯ÀüÀÚ
  • Fins oncogene
    Fins ¾ÏÀ¯ÀüÀÚ
  • proto-oncogene
    ¿øÁ¾¾çÀ¯ÀüÀÚ
  • proto-oncogene
    ¿øÇü¾ÏÀ¯ÀüÀÚ, ¿øÇü¼¼Æ÷Á¾¾çÀ¯ÀüÀÚ
  • proto-oncogene
    ¿ø¹ß¾ÏÀ¯ÀüÀÚ(ê«Û¡äßëºîîí­)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • g proteins
    G ´Ü¹é
  • g-proteins
    G´Ü¹éÁú
  • glycosyl phosphatidyl inositol-linked proteins
    Glycosyl phosphatidyl inositol-linked proteins
  • guanosine triphosphate(gtp)-bindting proteins
    »ïÀλ걸¾Æ³ë½Å°áÇմܹéÁú
  • stress proteins
    ½ºÆ®·¹½º´Ü¹éÁú(¡­Ó±ÛÜòõ)
  • cellular oncogene
    ¼¼Æ÷¾ÏÀ¯ÀüÀÚ
  • oncogene
    Á¾¾çÀ¯ÀüÀÚ
  • oncogene
    Á¾¾çÀ¯ÀüÀÚ(ðþåËë¶îîí­), Á¾¾ç¿ø(ðþåË¿ø)
  • proto-oncogene
    ¿øÇü¾ÏÀ¯ÀüÀÚ, ¿øÇü¼¼Æ÷Á¾¾çÀ¯ÀüÀÚ
  • proto-oncogene
    ¿øÁ¾¾çÀ¯ÀüÀÚ
  • proto-oncogene
    ¿ø¹ß¾ÏÀ¯ÀüÀÚ(ê«Û¡äßëºîîí­)
  • trk proto-oncogene
    trk¿øÇüÁ¾¾çÀ¯ÀüÀÚ
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    ¼¼Æ÷ ¾ÏÀ¯ÀüÀÚ(á¬øàäßë¶îîí­)
  • oncogene
    ¾ÏÀ¯ÀüÀÚ(äßë¶îîí­)
  • oncogene theory
    ¾ÏÀ¯ÀüÀÚÀÌ·Ð(äßë¶îîí­ìµÖå)
  • bundling proteins
    ±Ù¼Ó´Ü¹éÁú(ÐÉáÖÓ±ÛÜòõ)
  • capping proteins
    ĸÇü¼º(û¡à÷) ´Ü¹éÁú(Ó±ÛÜòõ)
  • extrinsic proteins
    ¿ÜÀÎ ´Ü¹éÁú (èâì×Ó±ÛÜòõ)
  • high-quality proteins
    °í±Þ ´Ü¹éÁú(ÍÔÐäÓ±ÛÜòõ)
  • integral proteins
    ÅëÇմܹéÁú(÷ÖùêÓ±ÛÜòõ)
  • labile proteins
    ºÒ¾ÈÁ¤´Ü¹éÁú(ÝÕäÌïÒÓ±ÛÜòõ)
  • microtubule-associated proteins
    ¹Ì¼Ò°ü ¿¬°ü´Ü¹éÁú(Ú°á³Î·æáμӱÛÜòõ)
  • nonbasic chromosomal proteins
    ºñ¿°±â¼º ¿°»öü´Ü¹éÁú(Þªç¤Ðñàõæøßäô÷Ó±ÛÜòõ)
  • nonhistone chromosomal proteins
    ºñ(Þª)È÷½ºÅæ ¿°»öü(æøßäô÷)´Ü¹éÁú(Ó±ÛÜòõ)
  • plasma proteins
    Ç÷Àå ´Ü¹éÁú(úìíìÓ±ÛÜòõ)
  • serum proteins
    Ç÷û ´Ü¹éÁú(úìôèÓ±ÛÜòõ)
  • split proteins
    ºÐ¸® ´Ü¹éÁú(ÝÂ×îÓ±ÛÜòõ)
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PBPs Penicillin-Binding Proteins
PVM pneumonia virus of mice; proteins, vitamins, and minerals
RPSP reference preparation for serum proteins
GnRH Gonadotropin Releasing Hormone  [HP 1898, 2034]
  = LHRH
  = Go...
AXL anexelekto [oncogene]; axillary lymphoscintigraphy
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G proteins GIP-binding proteins
G-proteins GTP)-binding regulatory proteins
G-proteins Guanine nucleotide-binding regulatory proteins
G proteins reglatory proteins
c-onc cellular oncogene
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cellular oncogene
    ¼¼Æ÷ ¾Ï À¯ÀüÀÚ
    ¼¼Æ÷ÀÇ ¿øÀο¡ ÀÇÇØ¼­ Á¾¾çÇü¼ºÀ» ÀÏÀ¸Å°´Â À¯ÀüÀÚ.
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
oncogene proteins v-erba Transforming proteins encoded by erba oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erba, the thyroid hormone receptor (receptors, thyroid hormone) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. V-erba acts as a dominant repressor of c-erba, inducing transformation by disinhibiting proliferation.
(12 Dec 1998)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
proto-oncogene proteins Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
(12 Dec 1998)
proto-oncogene proteins c-abl Membrane proteins encoded by the c-abl genes. They exhibit tyrosine kinase activity and play a role in normal haematopoiesis especially of the myeloid lineage. Oncogenic transformation of c-abl arises when specific n-terminal amino acids are deleted, releasing the kinase from negative regulation.
(12 Dec 1998)
proto-oncogene proteins c-bcl-2 Membrane proteins encoded by the bcl-2 genes and serving as a potent inhibitor of cell death by apoptosis. The proteins are found on mitochondrial, microsomal, and nuclear membrane sites within many cell types. Overexpression of bcl-2 proteins, due to a translocation of the gene, is associated with follicular lymphoma.
(12 Dec 1998)
proto-oncogene proteins c-erbb-2 Cellular proteins in the epidermal growth factor receptor family encoded by the c-erbb genes. These proteins are overexpressed in a significant portion of adenocarcinomas found at various sites, especially in the breast. Gene amplification appears to be the predominant method leading to overexpression.
(12 Dec 1998)
proto-oncogene proteins c-fos Cellular DNA-binding proteins encoded by the c-fos genes (genes, fos). They are involved in growth-related transcriptional control. C-fos combines with c-jun (proto-oncogene proteins c-jun) to form a c-fos/c-jun heterodimer (transcription factor ap-1) that binds to the tre (tpa-responsive element) in promoters of certain genes.
(12 Dec 1998)
proto-oncogene proteins c-jun Cellular DNA-binding proteins encoded by the c-jun genes (genes, jun). They are involved in growth-related transcriptional control. There appear to be three distinct functions: dimerization (with c-fos), DNA-binding, and transcriptional activation. Oncogenic transformation can take place by constitutive expression of c-jun.
(12 Dec 1998)
proto-oncogene proteins c-kit Tyrosine kinase membrane receptors which are the natural ligands for mast cell growth factor (steel factor). This interaction is crucial for the development of haematopoietic, gonadal, and pigment stem cells.
(12 Dec 1998)
proto-oncogene proteins c-met <enzyme> A transmembrane tyrosine kinase that is the receptor for hepatocyte growth factor (scatter factor). It consists of an extracellular alpha chain which is disulfide linked to the transmembrane beta chain. The cytoplasmic portion contains the catalytic domain and critical sites for the regulation of kinase activity.
Registry number: EC 2.7.11.-
(12 Dec 1998)
proto-oncogene proteins c-mos Cellular proteins encoded by the c-mos genes (genes, mos). They function in the cell cycle to maintain maturation-promoting factor in the active state and have protein-serine/threonine kinase activity. Oncogenic transformation can take place when c-mos proteins are expressed at the wrong time.
(12 Dec 1998)
proto-oncogene proteins c-myc Cellular DNA-binding proteins encoded by the c-myc genes. They are normally involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Elevated and deregulated (constitutive) expression of c-myc proteins can cause tumourigenesis.
(12 Dec 1998)
proto-oncogene proteins c-raf <enzyme> A class of serine-threonine kinases involved in cellular signal transduction. Included in this class are the proto-oncogene proteins mil and raf. Raf is a component of a signal transduction pathway leading to increased gene expression through the c-jun DNA binding site, ap1.
Registry number: EC 2.7.10.-
(12 Dec 1998)
oncogene proteins Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (oncogene proteins, fusion).
(12 Dec 1998)
oncogene proteins, fusion The translation products of the fusion between an oncogene and another gene. The latter may be of viral or cellular origin.
(12 Dec 1998)
oncogene proteins v-abl Transforming proteins encoded by the abl oncogenes. Oncogenic transformation of c-abl to v-abl occurs by insertional activation that results in deletions of specific n-terminal amino acids.
(12 Dec 1998)
oncogene proteins v-erbb Transforming proteins encoded by erbb oncogenes from the avian erythroblastosis virus. The protein is a truncated form of the egf receptor (receptors, epidermal growth factor-urogastrone) whose kinase domain is constitutively activated by deletion of the ligand-binding domain.
(12 Dec 1998)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Oncogene Proteins v-erbA - »õâ Transforming proteins encoded by erbA oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erbA, the thyroid hormone receptor (RECEPTORS, THYROID HORMONE) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. v-erbA acts as a dominant repressor of c-erbA, inducing transformation by disinhibiting proliferation.
    Synonyms : Oncogene Products v-erbA, Oncogene Products v erbA, Oncogene Proteins v erbA, v erbA Proteins
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