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"coronary risk factor"¿¡ ´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
  • myocardial depressant factor
    ½É(Àå)±Ù(À°)¾ïÁ¦ÀÎÀÚ
  • macrophage aggregating factor
    Å«Æ÷½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ, ´ë½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ
  • macrophage arming factor
    Å«Æ÷½Ä¼¼Æ÷¹«ÀåÀÎÀÚ, ´ë½Ä¼¼Æ÷¹«ÀåÀÎÀÚ
  • macrophage chemotactic factor
    Å«Æ÷½Ä¼¼Æ÷È­Çнò¸²ÀÎÀÚ, ´ë½Ä¼¼Æ÷È­Çнò¸²ÀÎÀÚ
  • macrophage colony-stimulating factor
    Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ, ´ë½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • macrophage migration inhibitory factor
    Å«Æ÷½Ä¼¼Æ÷À̵¿ÀúÁöÀÎÀÚ, ´ë½Ä¼¼Æ÷À̵¿ÀúÁöÀÎÀÚ
  • macrophage-activating factor
    Å«Æ÷½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ, ´ë½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ
  • macrophage-derived growth factor
    Å«Æ÷½Ä¼¼Æ÷À¯·¡¼ºÀåÀÎÀÚ, ´ë½Ä¼¼Æ÷À¯·¡¼ºÀåÀÎÀÚ
  • nerve growth factor
    ½Å°æ¼ºÀåÀÎÀÚ
  • neutron kerma factor
    Áß¼ºÀÚÄ¿¸¶°è¼ö
  • neutrophil chemotactic factor
    Áß¼º±¸È­ÇÐÁÖ¼ºÀÎÀÚ, È£Áß±¸½ò¸²ÀÎÀÚ
  • occupancy factor
    °ÅÁÖ°è¼ö
  • obliquity factor
    ±â¿ï±â°è¼ö
  • output factor
    Ãâ·ÂÀÎÀÚ
  • oxygen gain factor
    »ê¼ÒÀ̵æ°è¼ö
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  • ¿µ¹®
    ÇѱÛ
  • neutrophil chemotactic factor
    È£Áß±¸ÁÖ¼ºÀÎÀÚ, È£Áß±¸½ò¸²ÀÎÀÚ
  • obliquity factor
    ±â¿ï±â°è¼ö
  • occupancy factor
    °ÅÁÖ°è¼ö
  • output factor
    Ãâ·ÂÀÎÀÚ
  • oxygen gain factor
    »ê¼ÒÀ̵æ°è¼ö
  • phantom scatter factor
    ÆÒÅè»ê¶õ°è¼ö
  • plasma coagulation factor
    Ç÷ÀåÀÀ°íÀÎÀÚ
  • plasma thromboplastin factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ
  • platelet activating factor
    Ç÷¼ÒÆÇȰ¼ºÀÎÀÚ
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡¼ºÀåÀÎÀÚ, Ç÷¼ÒÆÇ±â¿ø¼ºÀåÀÎÀÚ
  • precipitation factor
    ÃËÁø¿äÀÎ
  • predisposing factor
    ¼±Çà¿äÀÎ
  • prognostic factor
    ¿¹ÈÄÀÎÀÚ
  • prolactin inhibitory factor
    ÇÁ·Î¶ôƾºÐºñ¾ïÁ¦ÀÎÀÚ
  • prolactin releasing factor
    ÇÁ·Î¶ôƾºÐºñÀ¯¹ßÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
  • ¿µ¹®
    ÇѱÛ
  • platelet-derived growth factor(pdgf)
    ÆÇ-À¯µµ¼ºÀåÀÎÀÚ(úìá³÷ù-ë¯Óôà÷íþì×í­)
  • power factor
    Ãâ·Â·ü(õóæ³ëÒ), ¿ª·ü(æ³ëÒ).
  • predisposing factor
    ¼ÒÀμº ¿äÀÎ, ¼±Çà¿äÀÎ.
  • prognostic factor
    ¿¹ÈÄÀÎÀÚ
  • prolactin inhibiting factor
    ÇÁ·Ñ¶ôƾ(ºÐºñ)¾ïÁ¦ÀÎÀÚ.
  • prolactin inhibiting factor
    ÇÁ·Î¶ôƾ¾ïÁ¦ÀÎÀÚ
  • prolactin-inhibitory factor(PIF)
    ÇÁ·Î¶ôƾ ºÐºñ ¾ïÁ¦ ÀÎÀÚ
  • prolactin-releasing factor(PRF)
    ÇÁ·Î¶ôƾ ºÐºñ À¯¹ß ÀÎÀÚ
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ(Ó±ÛÜùêà÷ì×í­).
  • psychogenic factor
    ½ÉÀμº ¿ä¼Ò(¡­é©áÈ).
  • psychological factor
    ½É¸®Àû ¿äÀÎ
  • psychosocial factor
    ½É¸®»çȸÀû ¿äÀÎ
  • quality factor
    Á¤¼ºÀÎÀÚ(ïÒàõì×í­).
  • quality factor
    ¼±Áú°è¼ö
  • radiation weighting factor
    ¹æ»ç¼±°¡Áß°è¼ö
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  • ¿µ¹®
    ÇѱÛ
  • atomic factor
    ¿øÀÚÀÎÀÚ(¡­ì×í­).
  • atrial natriuretic factor
    ½É¹æ¼º ³ªÆ®·ýÀÌ´¢ÀÎÀÚ
  • atrial natriuretic factor
    Atrial natriuretic factor
  • attenuation factor
    °¨¾à ¿ä¼Ò, °¨¼è ¿äÀÎ
  • autocrine motility factor
    Autocrine motility factor
  • back scatter factor
    ÈĹæ»ê¶õ°è¼ö
  • beam scattering factor
    ºö»ê¶õÀÎÀÚ
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • blood factor
    Ç÷¾×ÀÎÀÚ(?ËöËö).
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ(ËÑËâËöËö).
  • cavaliere blood factor
    Ä«¹ß¸®¿¡ Ç÷¾×ÀÎÀÚ.
  • cavity-gas calibration factor
    °­-±âü ±³Á¤°è¼ö, ºó±¸¸Û-
  • cell loss factor
    ¼¼Æ÷¼Ò½Ç°è¼ö
  • certainty factor
    È®½Ç¿äÀÎ
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  • ¿µ¹®
    ÇѱÛ
  • pyruvate oxidation factor
    ÆÄÀÌ·çºê»ê(ß«) »êÈ­ÀÎÀÚ(ß«ûùì×í­)
  • rat antispectacle eye factor
    Áã Ç׾ȱ¸ µ¹ÃâÁõ ÀÎÀÚ(ù÷äÑϹÔÍõóñøì×í­)
  • recruitment factor
    º¸ÃæÀÎÀÚ(ÜÍõöì×í­)
  • regulatory factor
    Á¶Àý ÀÎÀÚ(ðàï½ì×í­)
  • Reid factor
    ¶óÀ̵å ÀÎÀÚ(ì×í­)
  • relaxing factor
    ÀÌ¿Ï ÀÎÀÚ(ì¬èÐì×í­)
  • release factor
    À¯¸® ÀÎÀÚ(ë´×îì×í­)
  • resistance factor
    ÀúÇ× ÀÎÀÚ(ì×í­)
  • resistance-transfer factor
    ÀúÇ×ÀüÀÌ ÀÎÀÚ(ï®ì¹ì×í­)
  • R factor
    R ÀÎÀÚ(ì×í­)
  • Rhesus factor
    ·¹¼­½º ÀÎÀÚ(ì×í­)
  • rheumatoid factor
    ·ù¸¶ÅäÀ̵å ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
  • rho factor
    rho ÀÎÀÚ
  • ribosome dissociating factor
    ¶óÀ̺¸¼Ø ÇØ¸®ÀÎÀÚ(ú°×îì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 10
CDSRF chronic disease and sociodemographic risk factors
CSPINE corticosteroid use, seropositive RA, peripheral joint destruction, involvement of cervical nerves, n...
DRC damage risk criterion; dendritic reticulum cell; diagnostic reporting console; digitorenocerebral [s...
HARP homeless and at-risk population
HRA health record analyst; health risk appraisal; heart rate audiometry; hereditary renal adysplasia; hi...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 10
CCU Coronary Care Unit
CHD Coronary Heart Disease
CPP Coronary Perfusion Pressure
CA Coronary angiography
CAG Coronary angiography
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • predisposing factor
    ¼ÒÀÎ, Áúº´ ¼ÒÁú
    ÁúȯÀ̳ª Àå¾Ö¸¦ À¯¹ß½Ãų À§Ç輺À» Áõ°¡½ÃŰ´Â ¿ä¼Ò.
  • psychogenic factor
    Á¤½ÅÀû ¿ä¼Ò, ½ÉÀμº ¿ä¼Ò
  • psychosocial factor
    »çȸ Á¤½ÅÀû ¿äÀÎ
  • quality factor
    Á¤¼º ÀÎÀÚ, Ư¼º ¿ä¼Ò, Áú ¿ä¼Ò
  • release factor
    ¹æÃâ ÀÎÀÚ
  • releasing factor
    À¯¸® ÃËÁø ÀÎÀÚ, ¹æÃâ ÀÎÀÚ
  • resistance factor
    ³»¼º ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
  • rheumsid factor
    ·ù¸¶Æ¼½º¾ç ÀÎÀÚ
  • safety factor
    ¾ÈÀü·ü
    ½Å°æ ¼¶À¯³ª ±Ù¼¶À¯ÀÇ ÈïºÐ Á¤µµ¿¡ À־ ÀÌ¹Ì ÈïºÐÇÑ °÷¿¡¼­, ¾ÆÁ÷ ÈïºÐÇϰí ÀÖÁö ¾ÊÀº ºÎºÐÀ¸·Î Àü·ù°¡ È帧À¸·Î½á ÈïºÐÀÌ ÀüµµÇϴµ¥, ÀÌ Àü·ù°¡ ½ÇÁ¦·Î ÈïºÐ½Ã۴µ¥ ÇÊ¿äÇÑ Àü·ù°ª.
  • self-associated rheumatoid factor complex

    self-care (ÀÚ°¡ Ä¡·á

  • sex factor
    ¼º ÀÎÀÚ
  • situational factor
    »óȲ ¿äÀÎ
  • socioeconomic factor
    »çȸ °æÁ¦Àû ¿äÀÎ
  • somatic factor
    ü¼º ¿äÀÎ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
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)
receptors, macrophage colony-stimulating factor Glycoproteins of mw 165 kD which are encoded by the c-fms proto-oncogene. The binding of csf-1 to its receptors activates an intrinsic tyrosine kinase activity resulting in autophosphorylation of the receptors on tyrosine, rapid receptor down-regulation, and phosphorylation of as yet unidentified physiologic substrates that initiate a mitogenic response.
(12 Dec 1998)
receptors, nerve growth factor Cell surface receptors that bind nerve growth factor (ngf) and trigger intracellular changes influencing the behaviour of cells. Nerve growth factor receptors mediate the effects of nerve growth factor on the survival and growth of neurons.
(12 Dec 1998)
receptors, platelet-derived growth factor Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain.
(12 Dec 1998)
receptors, transforming growth factor beta Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone).
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ±¸ºÐ/º¸Çè±Þ¿©
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    ÇÑÀÚ
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