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"Complement System Proteins"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • primary signalling system
    ÀÏÂ÷½Åȣü°è
  • projective system
    Åõ»çü°è
  • real time system
    ½Ç½Ã°£Ã¼°è
  • registration system
    ½Å°íÁ¦µµ, µî·ÏÁ¦µµ
  • remote afterloading system
    ¿ø°ÝÁ¶ÀÛÈÄÀåÁø¹ý
  • reproductive system
    »ý½Ä°èÅë
  • respiratory system
    È£Èí°èÅë
  • reticuloendothelial system
    ±×¹°³»ÇǰèÅë, ¼¼¸Á³»ÇǰèÅë
  • Rh blood group system
    ¾Ë¿¡ÃëÇ÷¾×Çü±º
  • self-system
    ÀÚ±âü°è
  • system
    °èÅë, ÀåÄ¡, Á¦µµ
  • scavenging system
    ¸¶Ãë°¡½ºÁ¦°Åü°è
  • skeletal system
    »À´ë°èÅë
  • social security system
    »çȸº¸ÀåÁ¦µµ
  • somatosensory system
    ¸ö°¨°¢°èÅë
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • primitive duct system
    ¿ø½Ã°ü°èÅë
  • projective system
    Åõ»çü°è
  • real time system
    ½Ç½Ã°£ ü°è
  • reciprocal system
    »ó¹Ý°è(ßÓÚãͧ).
  • recirculating system
    Àç¼øÈ¯(¹æ)½Ä .
  • redox system
    »êȭȯ¿ø°è(ß«ûùü»êªÍ§).
  • registration system
    ½Å°íÁ¦µµ(Ëà˭̡̬).
  • remote afterloading system,RALS
    ¿ø°ÝÁ¶ÀÛÈÄÀåÁø¹ý
  • renal collecting system
    ½ÅÁýÇÕ°ü°èÅë(ãìó¢ùêηͧ÷Ö).
  • renal collecting system
    ½ÅÁýÇÕ°ü°èÅë
  • renal depressor system
    ½Å°­¾Ð°è.
  • renal pressor system
    ½Å½Â¾Ð°è(¡­ã°äâͧ).
  • renin angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅٽŰè(¡­Í§).
  • renin-angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅÙ½Åü°è
  • renin-angiotensin system
    ·¹´Ñ-¾ÈÁö¿ÀÅٽŰè(¡­Ìõ)
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  • ¿µ¹®
    ÇѱÛ
  • collecting system
    ÁýÇÕ°è
  • combined system disease
    º¹ÇÕ°èÅëÁúȯ.
  • community sewage disposal system
    Áö¿ª»çȸÇϼö󸮰èÅë(̤ËçË×̷̰Ëà̧Ëö˭̬).
  • community water system
    Áö¿ª»çȸ±Þ¼ö½Ã¼³(ÊÙË»ËàËàËÛ).
  • complete rebreathing system
    ¿ÏÀüÀçÈ£Èí½Ä(¹ý), Æó¼â½Ä(¹ý).
  • conduction system
    ÈïºÐÀüµµ°è(ýéÝÇîîÓôͧ).
  • conduction system of heart
    ½ÉÀåÀüµµ°èÅë
  • conductive system
    Àüµµ°è(îîÓôͧ), ÀüÀ½°è.
  • cortically originating extrapyamidal system =COEPS
    °ÑÁú±â¿øÇǶó¹Ô¹Ù±ù·Î°èÅë, ÇÇÁú¹ßÃßü¿Ü·Î°è(¡­Û¡õÞô÷èâÖØÍ§).
  • cortically originating extrapyamidal system =COEPS
    ÇÇÁú±â¿øÇǶó¹Ô¹Ù±ù·Î°èÅë, ÇÇÁú¹ßÃßü¿Ü·Î°è(¡­Û¡õÞô÷èâÖØÍ§).
  • corticothalamic system
    ÇÇÁú½Ã»ó°è(ù«òõãÊßÉͧ)
  • countercurrent exchanger system
    ¿ª·ù±³È¯°è(æ½êüÎßüµÍ§).
  • countercurrent multiplier system
    ¿ª·ùÁõÆø°è(¡­ñòøëͧ),´ëÇâ·ùÁõÆø°è.
  • countercurrent system
    ¿ª·ù°è(æ½êüͧ), ´ëÇâ·ù°è.
  • crystal system
    (°á)Á¤°è(Ì¿ïÜͧ).
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C2a activated second component of complement
C3 third cervical nerve; third cervical vertebra; third component of complement
C3a activated third component of complement
C4 fourth cervical nerve; fourth cervical vertebra; fourth component of complement
C4a activated fourth component of complement
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ACP Alternative complement pathway
C Complement
C' 3 Complement
C3 Complement 3
CCP Complement Control Protein
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    ¼³¸í
  • sensory modulatory system
    °¨°¢ Á¶Àý°è
  • serotonergic endogenous analgesic system
    ¼¼·ÎÅä´Ñ ³»¿ø¼º ÁøÅë°è
  • shift system
    ±³´ëÁ¦ ±Ù¹«
    8½Ã°£ ÀÌ»óÀÇ ³ëµ¿À» ÇÊ¿ä·Î ÇÏ´Â Á÷Àå¿¡¼­ Á¶·Î ³ª´©¾î ÀÏÇÏ´Â Á¦µµ.
  • sodium transport system
    ³ªÆ®·ý ¿î¹Ý°è
  • stomatognathic system
    ±¸°­¾Ç°è, ±¸°­ ÇϾǰè, ¾Ç±¸°­°è
    Ä¡¾Æ, ¾Ç°ñ, ÃøµÎÇϾǰüÀý, ÀúÀÛ±Ù »çÀÌÀÇ ±â´ÉÀû ¹× ÇØºÎÇÐÀû °ü°è.
  • superficial musculoaponeurotic system
    Ç¥Ãþ ±Ù°Ç¸· ü°è
  • supraopticohypophyseal system
    ½Ã°¢ ±³Â÷ À§³úÇÏ ¼öü°è, ½Ã°¢·ÎÀ§ ³úÇÏ ¼öü·Î
  • sympathetic nerve system
    ±³°¨ ½Å°æ°è
  • sympathetic nervous system activity
    ±³°¨½Å°æ°è Ȱ¼º
  • sympatheticoadrenomedullary system
    ±³°¨½Å°æ ºÎ½Å ¼ÓÁú°è
  • system
    °èÅë, ü°è, ±â°ü°è, °è, Àü½Å
  • system lupus erythematosus
    Àü½Å¼º È«¹Ý¼º ³¶Ã¢
  • TNM-system
    TNM °è
  • to and fro absorbent system
    ¿Õº¹ Èí¼ö¹ý
  • trigonal system
    »ï°¢Çü°è
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heat-shock proteins 70 <cell biology, protein> A class of molecular chaperones found in both prokaryotes and in several compartments of eukaryotic cells. There is evidence that these proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
(12 Dec 1998)
heat-shock proteins 90 <cell biology, protein> A class of molecular chaperones whose members act in the mechanism of signal transduction by steroid receptors.
(12 Dec 1998)
salivary proteins Proteins found in saliva and the salivary glands. These proteins show some enzymatic activity, but their composition varies in different individuals.
(12 Dec 1998)
helminth proteins Proteins found in any species of helminth.
(12 Dec 1998)
scaffold proteins Proteins that remain when chromosomes are digested with DNase. Many antigenic species have been identified.
(18 Nov 1997)
proteins Nitrogenous organic compounds, containing more than about 100 amino acid residues, molecular weight 8,000-200,000, in vegetable and animal matter. Proteins yield amino acids on hydrolysis and are foods assimilated as amino acids and reconstructed in the protoplasm.
(12 Dec 1998)
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)
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