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  • ¿µ¹®
    ÇѱÛ
  • protein sensitization
    ´Ü¹éÁú¹Î°¨È­
  • protein-losing enteropathy
    ´Ü¹éÁú¼Ò½ÇÀ庴(Áõ)
  • purified protein derivative
    Á¤Á¦´Ü¹éÁúÀ¯µµÃ¼
  • reserve protein
    ÀúÀå´Ü¹éÁú
  • specific protein
    ƯÀ̴ܹéÁú
  • split-timed urine protein
    ½Ã°£´ëº°¿ä´Ü¹éÁ¤·®
  • stage-specific protein
    ¹ßÀ°´Ü°èƯÀ̴ܹéÁú
  • stress protein
    ½ºÆ®·¹½º´Ü¹éÁú
  • structural protein
    ±¸Á¶´Ü¹éÁú
  • vehicle protein
    ¿î¹Ý´Ü¹éÁú
  • Z-protein
    Z´Ü¹éÁú
  • antihemophilic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÎÀÚ, Ç׎½ÄÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • vehicle protein
    ¿î¹Ý´Ü¹éÁú
  • stable plasma protein solution
    ¾ÈÁ¤Ç÷Àå´Ü¹é¿ë¾×
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • activation factor
    Ȱ¼ºÀÎÀÚ
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ, ÇãÆÄ²Ê¸®Èñ¼®ÀÎÀÚ
  • amplification factor
    ÁõÆøÀÎÀÚ
  • antihemophlic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÛ¿ëÀÎÀÚ
  • antirachitic factor
    Ç×±¸·íº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ³ªÆ®·ýÀÌ´¢ÀÎÀÚ
  • colonizing factor antigen
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø
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  • ¿µ¹®
    ÇѱÛ
  • protein A
    ´Ü¹éÁú A (Æ÷µµ±¸±ÕÀÇ)
  • protein C
    C ´Ü¹é
  • protein score
    ´Ü¹é°¡(ËÀËÑ˧) ½ÄǰÀÇ .
  • protein sensitization
    ´Ü¹é°¨ÀÛ(¡­ÊïíÂ).
  • protein separation
    ´Ü¹éºÐ¸®
  • protein sparing effect
    ´Ü¹éÁúÀý¾àÈ¿°ú(Ó±ÛÜòõï½å³üùÍý).
  • protein synthesis
    ´Ü¹éÁúÇÕ¼º.
  • protein therapy
    ´Ü¹é(Áú)¿ä¹ý(¡­èþÛö).
  • protein,actin-binding
    ¾×ƾ-°áÇÕ(´Ü¹é)
  • protein,al
    AL(´Ü¹é)
  • protein,bence jones
    º¥½º-Á¸½º(´Ü¹é)
  • protein-calorie deficiency
    ´Ü¹é(Áú)¿­·®°áÇÌ(Ó±ÛÜ(òõ)æðÕáÌÀù¹)
  • protein-calorie malnutrition
    ´Ü¹é(Áú)¿­·®¿µ¾ç½ÇÁ¶(Áõ)(Ó±ÛÜ(òõ)æðÕáç½å×ã÷ðà(ñø))
  • protein-energy malnutrition
    ´Ü¹é(Áú)¿¡³ÊÁö¿µ¾ç½ÇÁ¶(Áõ)(¡­ç½å×ã÷ðà(ñø))
  • protein-losing
    ´Ü¹é»ó½Ç¼º.
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  • ¿µ¹®
    ÇѱÛ
  • bacterial cell protein
    ±Õü´Ü¹é(Áú).
  • bactericidal permeability increasing protein(bpip)
    Bactericidal permeability increasing protein
  • bence-jones protein
    º¥½º-Á¸½º ´Ü¹é(¡­Ó±ÛÜ)
  • blood protein
    Ç÷¾×´Ü¹é(¡­Ó±ÛÜ).
  • body protein
    ü´Ü¹é(Áú)(ô÷Ó±ÛÜòõ).
  • c-Jun protein
    ¾¾-ÁØ ´Ü¹é(Ó±ÛÜ)
  • calcium-binding protein
    Ä®½· °áÇմܹé(Ì¿ùêÓ±ÛÜ)
  • cap binding protein
    ĸ°áÇմܹéÁú
  • carrier protein
    ¿î¹Ý´Ü¹éÁú
  • carrier protein
    ¿î¹Ý´Ü¹é(¡­Ó±ÛÜ)
  • catabolite activating protein
    ÀÌÈ­»ê¹° Ȱ¼ºÈ­´Ü¹éÁú
  • cellular retinol-binding protein
    ¼¼Æ÷³» ·¹Æ¼³î °áÇմܹé
  • chromatographic protein separation
    Å©·Î¸¶Åä±×·¡Çǹý ´Ü¹éºÐ¸®
  • coat protein
    ¿ÜÇǴܹéÁú
  • competitive protein binding radioassay
    °æÇÕÀû ´Ü¹é°áÇÕ¹æ»çºÐ¼®(¹ý)(¡­Ó±ÛÜ Ì¿ùêÛ¯ÞÒÝÂà°Ûö).
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  • ¿µ¹®
    ÇѱÛ
  • factor XIII
    ÀÎÀÚ(ì×í­) XIII
  • factor XIV
    ÀÎÀÚ(ì×í­) XIV
  • factor F
    ÀÎÀÚ(ì×í­) F
  • factor G
    ÀÎÀÚ(ì×í­) G
  • factor IF
    ÀÎÀÚ(ì×í­) IF
  • factor R
    ÀÎÀÚ(ì×í­) R
  • factor T
    ÀÎÀÚ(ì×í­) T
  • factor theory
    ÀÎÀÚ ÀÌ·Ð(ì×í­×âÖå)
  • factor X
    ÀÎÀÚ(ì×í­) X
  • factor Y
    ÀÎÀÚ(ì×í­) Y
  • fertility factor
    ¼öÁ¤ ÀÎÀÚ (áôïñì×í­)
  • F factor
    F ÀÎÀÚ(ì×í­)
  • F' factor
    F' ÀÎÀÚ(ì×í­)
  • fibrin-stabilizing factor
    ¼¶À¯¼Ò ¾ÈÁ¤È­ÀÎÀÚ(àéë«áÈäÌïÒûùì×í­)
  • Fitzgerald factor
    ÇÍÁ¦¶öµå ÀÎÀÚ(ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 6
Inv, inv inversion; involuntary
Inv/Ev inversion/eversion
inv(p+q-) pericentric inversion
inv(p-q+) pericentric inversion
IR drop of voltage across a resistor produced by a current; ileal resection; immune response; immunizat...
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FS Field stimulation
FES Functional Electric Stimulation
F.E.S. Functional Electrical Stimulation
FNS Functional Neuromuscular Stimulation
FMS Functional magnetic stimulation
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • blood factor
    Ç÷¾× ÀÎÀÚ
  • bone factor
    °ñ ÀÎÀÚ
    Ȱ¼ºÀ̳ª ÀÚÁï¿¡ ´ëÇÑ Ä¡Á¶°ñÀÇ »ó´ë ¹ÝÀÀ.
  • Castle factor
    ij½½ ÀÎÀÚ
    ½ÄǰÀ̳ª À§¾× ¼Ó¿¡ ÀÖ´Â Ç׺óÇ÷ ÀÎÀÚ. À̰ÍÀÌ °áÇÌµÇ¸é ¾Ç¼º ºóÇ÷ÀÌ µÈ´Ù. À§¾×¿¡ ÇÔÀ¯µÈ ij½½³» ÀÎÀÚ¿Í ½Äǰ¿¡ ÇÔÀ¯µÈ ij½½¿Ü ÀÎÀÚ°¡ ÀÖ´Ù. ³»ÀÎÀÚ°¡ °áÇÌµÇ¸é ½Äǰ ³»ÀÇ ¿ÜÀÎÀÚ°¡ Èí¼öµÇÁö ¾Ê°í ¾Ç¼º ºóÇ÷ÀÌ ÀϾ´Ù. À§ ¾Ï µîÀ¸·Î À§¸¦ ÀüºÎ Àß¶ó¹ö¸®¸é ºóÇ÷ÀÌ ÀϾ´Â °ÍÀº ³»ÀÎÀÚ°¡ ¾ø¾îÁö±â ¶§¹®ÀÌ´Ù. ³»ÀÎÀÚ´Â ºÐÀÚ·® ¾à 10¸¸ÀÎ ´Ü¹éÁú·Î À§º®ÀÇ ¹æ ¼¼Æ÷¿¡¼­ ºÐºñµÈ´Ù. ¿ÜÀÎÀڷμ­´Â ºñŸ¹Î D°¡ °ü°èÇÑ´Ù. 1927³â ¹Ì±¹ÀÇ W.B. ij½½ÀÌ Ã³À½À¸·Î ÀÌ·¯ÇÑ ±¸Á¶¸¦ Á¦Ã¢ÇÏ¿´´Ù.
  • Castles extrinsic factor
    ij½½ ¿ÜÀÎÀÚ
  • cavity-gas calibration factor
    °­-±âü ±³Á¤ °è¼ö
  • certainty factor
    È®½Ç ¿äÀÎ
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤ °è¼ö, »óÀÚ ÃøÁ¤ °è¼ö
  • circumstance factor
    »óȲ ÀÎÀÚ
  • clotting factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • clumping factor
    ÀÀ±« ÀÎÀÚ
  • coagulase-reacting factor
    Ç÷Àå ÀÀ°í È¿¼Ò ¹ÝÀÀ ÀÎÀÚ
  • coagulation factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°í ÀÎÀÚ ¾ïÁ¦Á¦
  • colicin factor
    Äݸ®½Å ÀÎÀÚ
  • colony stimulating factor
    ±ºÃ¼ ÀÚ±Ø ¿ä¼Ò, Áý¶ô ÀÚ±Ø ÀÎÀÚ
    ¹ß´Þ ´Ü°èÀÇ Àü±¸Àû ¼¼Æ÷°¡ Áý¶ôÀ» Çü¼ºÇÏ´Â °úÁ¤¿¡´Â À̰ÍÀÇ ÀÛ¿ëÀÌ ÇÊ¿äÇÏ´Ù´Â °ÍÀÌ ÀνĵǾú´Ù. ÀÌ ÀÎÀÚ´Â ¼¶À¯¾Æ¼¼Æ÷, ³»ÇǼ¼Æ÷, ´ë½Ä¼¼Æ÷ µî¿¡¼­ »ý»êµÇ¸ç ¼º¼÷ÇÑ ¸é¿ª°è ¼¼Æ÷ÀÇ ÀÛ¿ë¿¡µµ ¿µÇâÀ» ³¢Ä£´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 6
macrophage colony-stimulating factor <growth factor> A glycoprotein growth factor that causes the committed cell line to proliferate and mature into macrophages.
A cytokine synthesised by mesenchymal cells that stimulates pluripotent stem cells of bone marrow into differentiating towards the production of monocytes (mononuclear phagocytes).
The compound stimulates the survival, proliferation, and differentiation of haematopoietic cells of the monocyte-macrophage series. It is a disulfide-bonded glycoprotein dimer with a mw of 70 kD and binds to a single class of high affinity receptor which is identical to the product of the c-fms proto-oncogene.
See: colony-stimulating factors.
Chemical name: Colony-stimulating factor 1
Acronym: M-CSF
(12 Dec 1998)
macrophage inhibition factor <cytokine> A group of lymphokines (including a 14 kD glycoprotein) produced by activated T lymphocytes that reduces macrophage mobility and probably increases macrophage macrophage adhesion.
(18 Nov 1997)
radiation weighting factor In radiation protection, a factor weighting the absorbed dose of radiation of a specific type and energy for its effect on tissue.
See: equivalent dose.
(05 Mar 2000)
maise factor <molecular biology, plant biology> A naturally occurring cytokinin, originally isolated from maize seeds. Its riboside is also a cytokinin.
(18 Nov 1997)
vascular endothelial growth factor A growth factor that is responsible for the growth of blood vessels.
(12 Dec 1998)
mammotropic factor <protein> Pituitary lactogenic hormone (23 kD) Synthesised on endoplasmic reticulum bound ribosomes as preprolactin that has an N terminal signal peptide that is cleaved from the mature form. The conversion of preprolactin to prolactin has been much used as an assay for membrane insertion.
(18 Nov 1997)
receptors, atrial natriuretic factor Cell surface proteins that bind atrial natriuretic factor with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, colony-stimulating factor Cell surface receptors for colony-stimulating factors, local mediators, and hormones that regulate the survival, proliferation, and differentiation of haemopoietic cells.
(12 Dec 1998)
receptors, epidermal growth factor-urogastrone Glycoproteins of about 170 kD that have protein kinase activity and span the plasma membranes of growing cells, including tumours. They are activated by the binding of epidermal growth factor-urogastrone which then initiates DNA and protein synthesis. They are not found on mitotically quiescent cells except in the stomach where they control the synthesis and release of digestive enzymes and gastric acid. Transforming growth factor alpha also binds to and activates these receptors.
(12 Dec 1998)
receptors, fibroblast growth factor Specific molecular sites or structures on cell membranes that react with fibroblast growth factors (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity.
(12 Dec 1998)
receptors, granulocyte-colony-stimulating factor Receptors that bind and internalise granulocyte-colony-stimulating factor. Their mw is believed to be 150 kD. These receptors are found mainly on a subset of myelomonocytic cells.
(12 Dec 1998)
receptors, granulocyte-macrophage colony-stimulating factor Receptors that bind and internalise the granulocyte-macrophage stimulating factor. Their mw is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor.
(12 Dec 1998)
receptors, growth factor Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
(12 Dec 1998)
receptors, insulin-like-growth factor I Specific proteins on or in cells to which insulin-like growth factor I (somatomedin c) binds and thereby modifies the function of the cells. These receptors contain transmembrane and cytosolic domains, bind igf-I preferentially, and have high-affinity sites for igf-II. The alpha-subunit has a mw of 130 kD and the beta subunit possesses tyrosine kinase activity.
(12 Dec 1998)
receptors, insulin-like-growth-factor II Specific proteins on or in cells to which insulin-like growth factor II and mannose-6-phosphate bind and thereby modify the function of the cells. These receptors have a mw of 250 kD and possess no tyrosine kinase activity.
(12 Dec 1998)
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