¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"amyloid bodies"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid angiopathy
    ¾Æ¹Ð·ÎÀ̵åÇ÷°üº´(Áõ)
  • amyloid kidney
    ¾Æ¹Ð·ÎÀ̵åÄáÆÏ, ¾Æ¹Ð·ÎÀ̵å½ÅÀå
  • amyloid nephrosis
    ¾Æ¹Ð·ÎÀ̵åÄáÆÏÁõ, ¾Æ¹Ð·ÎÀ̵å½ÅÀåÁõ
  • amyloid plaque
    ¾Æ¹Ð·ÎÀ̵åÆÇ
  • familial amyloid neuropathy
    °¡Á·¼º¾Æ¹Ð·ÎÀ̵å½Å°æº´(Áõ)
  • Aschoff bodies
    ¾Æ¼îÇÁ¼Òü
  • Cabot ring bodies
    Ä«º¸Æ®°í¸®¼Òü
  • Cowdry type A inclusion bodies
    Ä«¿ìµå¸®AÇüÆ÷ÇÔü, Ä«¿ìµå¸®AÇüºÀÀÔü
  • Cowdry type B inclusion bodies
    Ä«¿ìµå¸®BÇüÆ÷ÇÔü, Ä«¿ìµå¸®BÇüºÀÀÔü
  • Call-Exner bodies
    Ä®-¿¢½º³Ê¼Òü
  • Guarnieri¡¯s bodies
    °ú¸£´Ï¿¡¸®Æ÷ÇÔü, °ú¸£´Ï¿¡¸®ºÀÀÔü
  • Heinz bodies
    ÇÏÀÎÃ÷¼Òü
  • Howell-Jolly bodies
    ÇÏ¿ù-Á¹¸®¼Òü
  • Mallory bodies
    ¸È·Î¸®¼Òü
  • Negri bodies
    ³×±×¸®¼Òü
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid kidney
    ¾Æ¹Ð·ÎÀ̵åÄáÆÏ, ¾Æ¹Ð·ÎÀ̵å½ÅÀå
  • amyloid nephrosis
    ¾Æ¹Ð·ÎÀ̵åÄáÆÏÁõ
  • amyloid plaque
    ¾Æ¹Ð·ÎÀ̵åÆÇ
  • amyloid angiopathy
    ¾Æ¹Ð·ÎÀ̵åÇ÷°üº´Áõ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid bodies<³ª> corpora amylacea
    ¾Æ¹Ð·ÎÀ̵å¼Òü(¡­á³ô÷).
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Ketone bodies
    ÄÉÅæÃ¼(¡­ô÷)
  • Negri bodies
    ³×±×¸®¼Òü ±¤°ßº´ºÀÀÔ¼Òü .
  • Nissls bodies
    ´Ï½½¼Òü.
  • guarneri bodies
    Guarneri ¼Òü
  • quadrigeminal bodies
    »ç±¸Ã¼(ÞÌÎøô÷).
  • quadrigeminal bodies
    ȍ
  • removal of foreign bodies in root canal
    ±Ù°ü³»À̹°Á¦°Å¹ý(ÐÆÎ·Ò®ì¶Úªð¶ËÛ Ûö).
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å.
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å
  • amyloid angiopathy
    À¯ÀüºÐÇ÷°üº´Áõ(ëºîþÝÏ úìηܻñø)
  • amyloid degeneration
    ¾Æ¹Ð·ÎÀ̵庯¼º(¡­Ü¨àõ).
  • amyloid disease
    ¾Æ¹Ð·ÎÀ̵庴(¡­Ü»).
  • amyloid kidney
    ¾Æ¹Ð·ÎÀÌµå ½Å
  • amyloid nephrosis
    ¾Æ¹Ð·ÎÀ̵å½ÅÁõ(¡­ãìñø).
  • amyloid precurssor protein
    ¾Æ¹Ð·ÎÀ̵å Àü±¸ ´Ü¹éÁú
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid bodies<³ª> corpora amylacea
    ¾Æ¹Ð·ÎÀ̵å¼Òü(¡­á³ô÷).
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å.
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å
  • amyloid angiopathy
    À¯ÀüºÐÇ÷°üº´Áõ(ëºîþÝÏ úìηܻñø)
  • amyloid degeneration
    ¾Æ¹Ð·ÎÀ̵庯¼º(¡­Ü¨àõ).
  • amyloid disease
    ¾Æ¹Ð·ÎÀ̵庴(¡­Ü»).
  • amyloid kidney
    ¾Æ¹Ð·ÎÀÌµå ½Å
  • amyloid nephrosis
    ¾Æ¹Ð·ÎÀ̵å½ÅÁõ(¡­ãìñø).
  • amyloid precurssor protein
    ¾Æ¹Ð·ÎÀ̵å Àü±¸ ´Ü¹éÁú
  • amyloid tumor
    ¾Æ¹Ð·ÎÀ̵åÁ¾¾ç.
  • familial amyloid elastosis
    °¡Á·¼º À¯ÀüºÐ ź·Â¼¶À¯Áõ
  • familial amyloid polyneuropathy
    °¡Á·¼º ¾Æ¹Ð·ÎÀÌµå ´Ù¹ß½Å°æº´Áõ
  • laryngeal amyloid
    Èĵξƹ̷ÎÀ̵å
  • papular amyloid elastosis
    ±¸Áø¼º À¯ÀüºÐ ź·Â ¼¶À¯Áõ
  • civatte bodies
    ½Ã¹ÙƮü(¡­ô÷)
  • cystoid bodies
    ¼¼Æ÷¾ç¼Òü
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å
  • herring bodies
    Ç층ü(ô÷)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid infiltration
    ¾Æ¹Ð·ÎÀ̵åħÀ±
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
APP acute phase protein; alum-precipitated pyridine; aminopyrazolopyrimidine; amyloid peptide precursor;...
ASAB Anti-Sperm Anti-Bodies
HJ Howell-Jolly [bodies]
P/I/X patients, indicators, external bodies
UFB urinary fat bodies
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
AB Asbestos bodies
ABs Asbestos bodies
CBs Carotid bodies
CBs Coiled bodies
DLB Dementia with Lewy Bodies
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • amyloid degeneration
    ¾Æ¹Ð·ÎÀÌµå º¯¼º
  • amyloid infiltration
    ¾Æ¹Ð·ÎÀ̵å ħÀ±
  • familial amyloid polyneuropathy
    °¡Á·¼º ¾Æ¹Ð·ÎÀÌµå ´Ù¹ß ½Å°æº´Áõ
  • serum amyloid protein A
    Ç÷û ¾Æ¹Ð·ÎÀ̵å ÇÁ·Îƾ A
  • bodies of Arantius
    ¾Æ¶õƼ¿ì½º °áÀý
    ´ëµ¿¸ÆÆÇÀÇ °áÀý.
  • Cabot's ring bodies
    Ä«º¸Æ® ȯ»óü
    ÁßÁõ ºóÇ÷ ȯÀÚÀÇ ÀûÇ÷±¸¿¡¼­ º¼ ¼ö Àִ ȯ»ó ¶Ç´Â 8ÀÚÇüÀÇ ¼±À̸ç, Wright-Leishman ¿°»öü¿¡¼­ Àû»öÀ¸·Î, ¿°È­ ¸ÞƿŸÀÌ¿À´ÑÀÇ ¿¡¿À»êÈ­¹° ¿°»ö¿¡¼­ û»öÀ¸·Î ¿°»öµÈ´Ù.
  • Doehle bodies
    Doehle ¼Òü
  • fibrin bodies of pleura
    È丷 ¼¶À¯ ¼Òü
    È丷°­ ±âÀúºÎ±Ù¿¡ ÀÖ´Â °¡µ¿¼º ¶Ç´Â Á¡Âø¼º, ±¸»ó, µ¿Áú¼º, ±×¸®°í ÇѰ谡 ¸íÈ®ÇÑ À¯¹éü·Î¼­, È丷 »ïÃâ¾×, ±âÈä ¶Ç´Â Ç÷±âÈäÁõ¿¡¼­ ÀÌÂ÷ÀûÀ¸·Î ¹ß»ýÇÑ´Ù.
  • Herring bodies
    Ç층 ¼Òü
    Çϼöü ½Å°æºÎ¿¡ Á¸ÀçÇÏ´Â ÃÊÀÚÁú ¶Ç´Â ±³ÁúÀÇ µ¢¾î¸®.
  • inclusion bodies
    ºÀÀÔü, ºÀÀÔ ¼Òü
    ¼¼Æ÷ÀÇ ¼¼Æ÷Áú ³»Áö ÇÙÁú ³»¿¡ ³ªÅ¸³ª´Â ±¸Çü ¶Ç´Â ³­ÇüÀÇ ºÒ±ÔÄ¢ÇÑ ¼ÒüÀ̸ç, ±¤°ßº´, µÎâ, ÇãÇǽº¿Í °°Àº ¿©°ú¼º ¹ÙÀÌ·¯½º¿¡ ÀÇÇÑ °¨¿°Áõ¿¡¼­ º¼ ¼ö ÀÖ´Ù.
  • Leishman-Donovan bodies
    ·¹½´¸¸-µµ³ë¹Ýü
    Ä®¶ó-¾ÆÀÚ¸£ º´¿¡ °É¸° ȯÀÚÀÇ Æ¯È÷ ºñÀå°ú °£ÀÇ ¼¼¸Á ³»ÇÇ ¼¼Æ÷ ³»¿¡¼­ °üÂûµÇ´Â ±¸Çü ¶Ç´Â ³­ÇüÀÇ ¼Òü·Î¼­, ÀÌ º´À» ÀÏÀ¸Å°´Â ±â»ýÃæÀÎ ¿ø»ýµ¿¹°ÀÇ ¹«Æí¸ð ¼¼Æ÷ ³»¿¡ ÀÖ´Ù. ¶ÇÇÑ ÇǺμº ·¹½´¸¶´Ï¾ÆÁõ¿¡¼­ ´ë½Ä ¼¼Æ÷³»¿¡¼­µµ °üÂûµÈ´Ù. L. tro
  • Mooser bodies
    ¹«¿ì¼­ ¼Òü
    ¹ßÁøÆ¼Çª½ºÀÇ ¾î¶² Çü¿¡ À־ Ãʸ· »óÇÇ ¼¼Æ÷ÀÇ »ïÃâ¾×¿¡¼­ °üÂûµÇ´Â ¸®ÄÉÄ¡¾Æ ¸ð¾çÀÇ ¼Òü.
  • Nissl bodies
    ´Ï½½ ¼Òü
    »ö¼Ò ģȭü, ŸÀ̱׷ÎÀÌµå ¹°Áú, Ç¥¹® ¹°Áú. ¿°±â¼º ¿°·á·Î ¿°»öµÇ°í, ³»ÇüÁú ¼¼¸Á°ú ¶óÀ̺¸¼ØÀ¸·Î ±¸¼ºµÈ ½Å°æ ¼¼Æ÷³»ÀÇ Ä¿´Ù¶õ °ú¸³.
  • purine bodies test
    Ǫ¸°Ã¼ ½ÃÇè
  • rice bodies
    ¹Ì¸³Ã¼
    °üÀý°ÇÀ̳ª ¼öȰ¾× ³¶Á¾¾× ¼Ó¿¡ Çü¼ºµÇ´Â ¹Ì¸³»óÀÇ ¼Òü.
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
amyloid bodies of the prostate An obsolete term for small masses of colloid material often present in the tubules of the gland.
See: corpus amylaceum.
(05 Mar 2000)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
amyloid Glycoprotein deposited extracellularly in tissues in amyloidosis. The glycoprotein may either derive from light chain of immunoglobulin (AIO (amyloid of immune origin): 5-18 kD glycoprotein, product of a single clone of plasma cells, the N terminal part of lambda or kappa light chain) or, in what used to be referred to as AUO, amyloid of unknown origin, from serum amyloid A (SAA), one of the acute phase proteins that increases many fold in inflammation. The polypeptides are organised as a _ pleated sheet making the material rather inert and insoluble. Minor protein components are also found. Should be distinguished from _ amyloid deposited in the brain and that is derived from amyloid precursor protein (see amyloidogenic glycoprotein.
(18 Nov 1997)
amyloid A-degrading serine protease <enzyme> Reduced in amyloidosis associated with rheumatoid arthritis
Registry number: EC 3.4.21.-
Synonym: amyloid a-degrading activity, aad-protease
(26 Jun 1999)
amyloid angiopathy Deposition of acellular hyaline material in small arteries and arterioles of the leptomeninges and cerebral cortex in the elderly with resulting predilection for recurrent lobar intraparenchymal haematomas.
(05 Mar 2000)
amyloid beta-protein A 4 kD protein, 39-43 amino acids long, expressed by a gene located on chromosome 21. It is the major protein subunit of the vascular and plaque amyloid filaments in individuals with alzheimer's disease and in aged individuals with trisomy 21 (down syndrome). The protein is found predominantly in the nervous system, but there have been reports of its presence in non-neural tissue.
(12 Dec 1998)
amyloid beta-protein precursor A precursor to the amyloid-beta protein (beta/a4). Alterations in the expression of the amyloid beta-protein precursor (abpp) gene, located on chromosome 21, plays a role in the development of the neuropathology common to both alzheimer disease and down syndrome. Abpp is associated with the extensive extracellular matrix secreted by neuronal cells. Upon cleavage, this precursor produces three proteins of varying amino acid lengths: 695, 751, and 770. The beta/a4 (695 amino acids) or beta-amyloid protein is the principal component of the extracellular amyloid in senile plaques found in alzheimer disease, down syndrome and, to a limited extent, in normal aging.
(12 Dec 1998)
amyloid corpuscle One of a number of small ovoid or rounded, sometimes laminated, bodies resembling a grain of starch and found in nervous tissue, in the prostate, and in pulmonary alveoli; of little pathological significance, and apparently derived from degenerated cells or proteinaceous secretions.
Synonym: amniotic corpuscle, amylaceous corpuscle, amyloid corpuscle, colloid corpuscle.
(05 Mar 2000)
amyloid degeneration Infiltration of amyloid between cells and fibres of tissues and organs.
Synonym: waxy degeneration.
(05 Mar 2000)
amyloid kidney A kidney in which amyloidosis has occurred, usually in association with some chronic illness such as multiple myeloma, tuberculosis, osteomyelitis, or other chronic suppurative inflammation; such kidney's are moderately enlarged and grossly manifest a waxy appearance, with amyloid deposited beneath the endothelium in the glomerular loops and in the arterioles, apparently beginning as foci of thickening of the basement membranes.
Synonym: waxy kidney.
(05 Mar 2000)
amyloid nephrosis The nephrotic syndrome due to deposition of amyloid in the kidney.
See: renal amyloidosis.
(05 Mar 2000)
amyloid neuropathies Disorders of the peripheral nervous system associated with deposition of amyloid. Amyloid neuropathies may result from non-hereditary or hereditary amyloidosis. Several different forms of familial amyloid neuropathies have been described, most of which have specific mutations in the prealbumin gene.
(12 Dec 1998)
amyloid p component Amyloid p component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin) structure. It acts as an acute phase protein in the mouse, modulates immunologic responses in man, inhibits elastase, and has been suggested as an indicator of liver disease.
(12 Dec 1998)
amyloid precursor protein <protein> Individuals with Alzheimer's disease are characterised by extensive accumulation of amyloid in the brain, referred to as senile plaques. These consist of a core of amyloid fibrils surrounded by dystrophic neurites. The principal component of the amyloid fibrils is B/A4, a peptide derived from the larger APP. The specific role of amyloid protein is unclear but it is thought that amyloid deposits may cause neurons to degenerate. Amyloid deposits also occur in brains of older Down's Syndrome patients.
(04 May 1997)
amyloid protein Glycoprotein deposited extracellularly in tissues in amyloidosis. The glycoprotein may either derive from light chain of immunoglobulin (AIO (amyloid of immune origin): 5-18 kD glycoprotein, product of a single clone of plasma cells, the N terminal part of lambda or kappa light chain) or, in what used to be referred to as AUO, amyloid of unknown origin, from serum amyloid A (SAA), one of the acute phase proteins that increases many fold in inflammation. The polypeptides are organised as a _ pleated sheet making the material rather inert and insoluble. Minor protein components are also found. Should be distinguished from _ amyloid deposited in the brain and that is derived from amyloid precursor protein (see amyloidogenic glycoprotein.
(18 Nov 1997)
amyloid protein aa A nonimmunoglobulin amyloid isolated from amyloid fibrils deposited in amyloidosis secondary to chronic inflammatory diseases such as rheumatoid arthritis. Antisera to amyloid protein aa have been used to detect a related serum protein saa.
(12 Dec 1998)
amyloid protein saa A serum protein believed to be a circulating precursor to amyloid protein aa. It is present in low concentrations in normal sera, but found in much higher concentrations in sera of older persons and in patients with amyloidosis or with diseases known to predispose to amyloidosis. Very high levels of this protein have been reported during acute inflammatory episodes. Antisera to amyloid protein aa cross-react with protein saa.
(12 Dec 1998)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • amyloid
    ¾Æ¹Ð·ÎÀ̵å;À¯ÀüºÐü
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á