| ¿µ¹® | medullary tumor | ÇÑ±Û | ¼öÁú¼º Á¾¾ç |
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| ¼³¸í | ¾ÏÀÇ º´¸®ÇÐÀûÀÎ ºÐ·ùÁß Çϳª. ¿©·¯ ±â°üÀÇ ¾Ï¿¡¼ ³ªÅ¸³ª´Âµ¥ ÁÖ·Î °©»ó»ù¾ÏÀ̳ª À¯¹æ¾Ï¿¡¼ º¸ÀδÙ. |
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| ¿µ¹® | malignant tumor | ÇÑ±Û | ¾Ç¼ºÁ¾¾ç |
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| ¼³¸í | Á¤»óÀûÀÎ Á¶Á÷ ¼¼Æ÷°¡ °¢Á¾ ¹°¸®Àû-ÈÇÐÀû-»ý¹°ÇÐÀûÀÎ ¹ß¾Ï ¹°ÁúÀÇ ÀÛ¿ë ¶Ç´Â ¿äÀο¡ ÀÇÇØ µ¹¿¬º¯À̸¦ ÀÏÀ¸ÄѼ Çü¼ºµÇ´Â Á¾¾ç. ¹«Á¦ÇÑÀÇ ¼¼Æ÷ºÐ¿·Î ¸Å¿ì ¿Õ¼ºÇÏ°Ô Áõ½ÄÇÏ¿© ÁÖÀ§Á¶Á÷À» ÆÄ±«-ħ½ÄÇÑ´Ù. ¶Ç ¾î¶² ÈÇй°ÁúÀ» ³»¾î ÁÖÀ§ÀÇ Á¶Á÷¼¼Æ÷¸¦ Ä§ÇØÇÒ »Ó¸¸ ¾Æ´Ï¶ó, Ç÷°ü ¹× ¸²ÇÁ°üÀ» µû¶ó ÀüÀÌÇÏ¿© Àü½ÅÀÇ Ä«ÄʽþƸ¦ÀÏÀ¸ÄÑ Á×À½À» ÃÊ·¡ÇÑ´Ù. »óÇǼºÀÎ °ÍÀ» ¾ÏÁ¾À̶ó Çϰí, ºñ»óÇǼºÀÎ °ÍÀ» À°Á¾À̶ó ÇÑ´Ù. |
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| ¿µ¹® | benign tumor | ÇÑ±Û | ¾ç¼ºÁ¾¾ç |
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| ¼³¸í | ¹ßÀ°¼Óµµ°¡ ¿Ï¸¸ÇÏ¿© ¼ºÀå¿¡ ÇѰ谡 ÀÖ°í, ÁÖÀ§¿ÍÀÇ °æ°è°¡ ¸íÈ®Çϸç, ´Ù¸¥ Á¶Á÷À¸·Î ÆÛÁöÁö ¾ÊÀ¸¸ç, ħÀ±À̳ª ÀüÀ̸¦ ÀÏÀ¸Å°Áö ¾Æ´ÏÇÏ´Â Á¾¾ç. ¼¶À¯Á¾À̳ª Áö¹æÁ¾ µûÀ§°¡ ÀüÇüÀûÀÎ ¿¹ÀÌ´Ù. ¾ç¼ºÁ¾¾çÀº Á¾¾çÀÌ Á¸ÀçÇÑ´Ù°í ÇØµµ 1Â÷ÀûÀ¸·Î ¼÷ÁÖÀÇ »ý¸íÀ» À§ÇùÇÏ´Â ÀÏÀº ¾ø´Ù. ¾ç¼ºÁ¾¾çÀÇ ¹ßÀ°Çü½ÄÀº ÁÖÀ§ÀÇ Á¶Á÷°£¿¡ ¿Õ·¡ÇÏ´Â ÀÏÀÌ ¾øÀÌ ÁÖÀ§ÀÇ Á¶Á÷À» ¹Ð¾î³»¸ç Áõ½ÄÇÑ´Ù. ¹ßÀ°¼Óµµ´Â ¿Ï¸¸Çϸç ÀüÀÌÇϰųª ÀýÁ¦ ÈÄ Àç¹ßÇÏ´Â ÀÏÀÌ ±ØÈ÷ µå¹°´Ù. Á¾¾ç¼ººÐÀº º¯ÀÌüÀ̱ä ÇÏÁö¸¸ ¼º¼÷ÇÑ Á¤»ó¼¼Æ÷¿Í °ÅÀÇ ´Ù¸¥ °ÍÀÌ ¾ø´Ù. Àü½Å¿¡ ´ëÇÑ ¿µÇâÀº ¾Ç¼ºÁ¾¾çÀÇ °æ¿ì ¾î´À Á¤µµ ¹ßÀ°ÇßÀ» ¶§ Àü½ÅÀÇ ¿µ¾ç»óŰ¡ ¼Õ»óµÇ¾î Ä«Äʽþư¡ µÇÁö¸¸ ¾ç¼ºÁ¾¾çÀÇ °æ¿ì ÀÌ·± ÀÏÀº °ÅÀÇ ¾ø´Ù. ¾ç¼ºÁ¾¾ç°ú ¾Ç¼ºÁ¾¾çÀÇ ¼º»óÀÇ Â÷ÀÌ¿¡ ¾ö¹ÐÇÑ °æ°è´Â ¾ø°í, °æ°è°æº¯À¸·Î º¸ÀÌ´Â Á¾¾çµµ ÀÖ´Ù. |
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| ¿µ¹® | Wilms' tumor | ÇÑ±Û | Àª¸§ÁîÁ¾¾ç |
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| ¼³¸í | ÄáÆÏ¿¡¼ ¹ß»ýÇÏ´Â ¾Ç¼ºÁ¾¾çÀ¸·Î ¼Ò¾Æ¿¡¼ ÀÚÁÖ ¹ß»ýÇÑ´Ù. ÈçÈ÷ ¼Ò¾Æ¿¡¼ º¹ºÎ³»Á¾¾çÀ» ¹ß°ß½Ã Áß¾Ó¼±À» ³Ñ¾î¼¸é ½Å°æ¸ð¼¼Æ÷Á¾À̰í, Áß¾Ó¼±À» ³ÑÁö ¾ÊÀ¸¸é Àª¸§ÁîÁ¾¾çÀ» ÀǽÉÇÒ ¸¸Å Áß¿äÇϰí ÈçÇÑ Á¾¾çÀÌ´Ù. ´ë°³ Áõ»óÀº ¾ø´Â ÆíÀ̸ç, ÁÖ·Î ¾Æ±âÀÇ ¸ñ¿åÀ» ½ÃÄÑÁÖ´Ù°¡ ¿ì¿¬È÷ ¹ß°ßµÈ º¹ºÎ³»Á¾±« ¶§¹®¿¡ º´¿øÀ» ã°Ô µÈ´Ù. Áø´Ü½Ã ÄÄÇ»ÅÍ´ÜÃþÃÔ¿µÀ¸·Î ÁÖÀ§ÀÇ ÀüÀ̰¡ ¾ø´ÂÁö¸¦ È®ÀÎÇØ¾ß Çϸç, ÀüÀ̰¡ ¾øÀ¸¸é Ç×¾ÏÈÇпä¹ý, ¹æ»ç¼±Ä¡·á¿ä¹ý, ±×¸®°í ¼ö¼ú¿ä¹ýÀÇ º´ÇÕ¿ä¹ý¿¡ ÀÇÇÑ Ä¡·áÈ¿°ú°¡ ³ô´Ù. |
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| ¿µ¹® | mucinous tumor | ÇÑ±Û | Á¡¾×Á¾¾ç |
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| ¼³¸í | Á¡¾×À¸·Î ±¸¼ºµÈ Á¾¾çÀ» ¸»Çϴµ¥ ÁÖ·Î ¿©¼ºÀÇ ³¼Ò¿¡¼ ¹ß»ýÇÏ´Â ³¶¼º(¹°ÁָӴϰ°Àº Á¾¾çÀ» ¸»ÇÔ) Á¾¾ç¿¡¼ ¸¹ÀÌ º¼ ¼ö ÀÖ´Ù. |
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| TP | temperature and pressure; temperature probe; temporal peak; temporoparietal; tension pneumothorax; t... |
|---|---|
| MAP | malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ... |
| MBP | major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl... |
| RP | radial pulse; radiopharmaceutical; rapid processing [of film]; Raynaud phenomenon; reactive protein;... |
| TCP | T-complex protein; therapeutic continuous penicillin; total circulating protein; transcutaneous pace... |
| suppressor mutation | <molecular biology> Mutation that alleviates the effect of a primary mutation at a different locus. May be through almost any mechanism that can give a primary mutation, but perhaps the most interesting class are the amber and ochre supressors, where the anticodon of the tRNA is altered so that it mis reads the termination codon and inserts an amino acid, preventing premature termination of the peptide chain. (18 Nov 1997) |
|---|---|
| suppressor-sensitive mutant | A conditionally lethal, host range, bacteriophage mutant that produces nonsense codons and can replicate only in a host bacterium able to translate the nonsense codon; the mutation's effects are lethal (i.e., prevent replication of the virus) in a bacterium without such a suppressor mechanism. (05 Mar 2000) |
| suppressor T-cell | <immunology> See T-cells. (18 Nov 1997) |
| suppressor tRNA | The tRNA associated with a suppressor mutation. (05 Mar 2000) |
| ochre suppressor | A gene that codes for an altered tRNA so that its anticodon can recognise the ochre codon and thus allows the continuation of protein synthesis. A suppressor of an ochre mutation is a tRNA that is charged with the amino acid corresponding to the original codon or a neutral substitute. Ochre suppressors will also suppress amber codons. (18 Nov 1997) |
| opal suppressor | <molecular biology> A gene that codes for an altered tRNA so that its anticodon can recognise the opal codon and thus allows the continuation of protein synthesis. A suppressor of an opal mutation is a tRNA that is charged with the amino acid corresponding to the original codon or a neutral substitute. Some eukaryote cells normally synthesise opal suppressor tRNAs. The function of these is not clear and they usually do not prevent normal termination of protein synthesis at an opal codon. (18 Nov 1997) |
| T-lymphocytes, suppressor-effector | Subpopulation of CD8+ T-lymphocytes which suppress antibody production or inhibit cellular immune responses. Suppressor-effector cells execute the message received from suppressor-inducer cells (T-lymphocytes, suppressor-inducer). (12 Dec 1998) |
| T-lymphocytes, suppressor-inducer | Subpopulation of CD4+ lymphocytes which induce CD8+ suppressor T-cells (T-lymphocytes, suppressor-effector) to suppress antibody production by B-cells. They also stimulate other cellular immune responses. (12 Dec 1998) |
| T suppressor cell | <haematology, immunology> Set of T lymphocytes (usually CD8) specifically involved in suppressing B-cell differentiation into antibody secreting cells. There may also be T suppresors of T-cell functions. (18 Nov 1997) |
| t-suppressor cell | A type of immune cells, also called t8 cells, these cells close down the immune response after it has destroyed invading organisms. T8 cells are sensitive to high concentrations of circulating lymphokine hormones and release their own lymphokines after an immune response has achieved its goal, signalling all other participants to cease their attack. Some memory B-cells remain to ward off a repeat attack by the invading organism. (12 Dec 1998) |
| tumour suppressor | <molecular biology, oncology> A gene that encodes a product that normally negatively regulates the cell cycle and that must be mutated or otherwise inactivated before a cell can proceed to rapid division. Examples: p53, RB retinoblastoma), WT 1 (Wilm's tumour), DCC (deleted in colonic carcinoma), NF 1 (neurofibrosarcoma) and APC adenomatous polyposis coli). (18 Nov 1997) |
| acetoacetyl-acyl carrier protein synthase | <enzyme> E coli enzyme, that catalyses condensation of malonyl-acyl carrier protein plus acetyl-acyl carrier protein; not inhibited by cerulenin Registry number: EC 2.3.1.- Synonym: acetoacetyl-acp synthase (26 Jun 1999) |
| acid soluble spore protein | <molecular biology> A DNA binding protein in the spores of some bacteria, thought to stabilise the DNA in an A configuration, so protecting it from cleavage by enzymes or UV light. (18 Nov 1997) |
| acute-phase protein | <haematology> These plasma proteins (in addition to fibrinogen) increase 25% or more in response to inflammation and injury are under direct control of interleukin-6 (IL-6) (hepatocyte-stimulating factor). Other proteins which increase are ceruloplasmin, C3 and C4 which increase 50% or more; alpha-1 acid glycoprotein, alpha-1 antitrypsin, haptoglobin and fibrinogen (the major determinant of viscosity 1 ) which increase two- to fourfold; C-reactive protein (CRP) and serum amyloid A which increase several hundred-fold. Despite long-held clinical opinion to the contrary, available data indicate that neither ESR nor measurement of specific acute-phase reactants are useful in excluding underlying infection or inflammation regardless of the pretest probability. These proteins are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. They can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumour markers. See also: amyloid, c-reactive protein, erythrocyte sedimentation rate, viscosity. (25 Jun 1999) |
| acyl-(acyl-carrier-protein)-phospholipid acyltransferase | <enzyme> Catalyses the formation of phosphatidylethanolamine from acyl-acyl carrier protein and 2-acyl-sn-glycero-3-phosphoethanolamine Registry number: EC 2.3.1.40 Synonym: 2-acyl-gpe acyltransferase, 2-acylglycerophosphoethanolamine acyltransferase (26 Jun 1999) |
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