¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Bone Morphogenetic Protein Receptors"¿¡ ´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: 4
  • ¿µ¹®
    ÇѱÛ
  • protein quotient
    ´Ü¹éÁúÁö¼ö
  • protein S
    ´Ü¹éÁúS
  • protein score
    ´Ü¹éÁú°¡
  • protein sensitization
    ´Ü¹éÁú¹Î°¨È­
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ
  • 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
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • structural protein
    ±¸Á¶´Ü¹é, ±¸Á¶´Ü¹éÁú
  • vehicle protein
    ¿î¹Ý´Ü¹éÁú
  • stable plasma protein solution
    ¾ÈÁ¤Ç÷Àå´Ü¹é¿ë¾×
  • air-bone gap
    °ø±â»ÀÀüµµÂ÷ÀÌ
  • alveolar bone
    ÀÌÆ²»À
  • alveolar bone graft
    ÀÌÆ²»ÀÀ̽Ä, Ä¡Á¶°ñÀ̽Ä
  • aneurysmal bone cyst
    µ¿¸Æ·ù»À³¶Á¾
  • autogenous bone graft
    ÀÚ±â»ÀÀ̽Ä, ÀÚ°¡°ñÀ̽Ä
  • bone age
    »À³ªÀÌ, °ñ¿¬·É
  • bone conduction audiometry
    »ÀÀüµµÃ»·Â°Ë»ç
  • herring bone appearance
    û¾î»À¸ð¾ç
  • herring bone artifact
    û¾î»ÀÇã»ó, û¾î»ÀÀΰø¹°
  • bone
    »À, °ñ
  • bone canaliculus
    »À¼¼°ü, °ñ¼Ò°ü
  • bone chip
    »ÀÁ¶°¢, °ñÆÄÆí, °ñ¼¼Æí
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • hearing, bone conduction
    °ñµµÃ»·Â
  • heel bone =calcaneus
    Á¾°ñ(ñ¢Íé).
  • heel bone =calcaneus
    Á¾°ñ(ñ¢Íé)£¬µÚ²ÞÄ¡ »À.
  • hereditary fragility of bone
    À¯Àü¼º °ñ Ãë¾àÁõ (¡­Íéöªå°ñø).
  • hereditary fragility of bone
    À¯Àü¼º °ñÃë¾àÁõ (¡­Íéöªå°ñø).
  • herring bone appearance
    û¾î»À ¸ð¾ç
  • hip bone
    °ü°ñ(ΰÍé).
  • hip bone
    º¼±â»À °ü°ñ
  • hip bone
    °ü°ñ(ΰÍé), µÐ°ñ(ÔëÍé), °í°ñ(ÍÆÍé), °ñ¹Ý°ñ(ÍéÚïÍé), ¹«¸í°ñ(ÙíÙ£Íé), ¾ûÄ¡»À.
  • horn of hyoid bone
    ¼³°ñ»Ô, »ó°¢(ß¾ÊÇ).
  • hyoid bone
    ¼³°ñ.
  • hyoid bone
    ¸ñ»Ô»À ¼³°ñ
  • hyoid bone
    ¼³°ñ
  • iliac bone <³ª> os ilium
    Àå°ñ(Àå°ñ).
  • iliac bone ³ª os ilium
    Àå°ñ(íóÍé).
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • cytotoxic cell protein
    ¼¼Æ÷µ¶¼º ¼¼Æ÷´Ü¹é
  • denatured protein
    º¯¼º´Ü¹éÁú
  • deposit protein
    ÀúÀå´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • derived protein
    À¯µµ´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • different membrane protein
    À¯°ü(êóμ)¸·´Ü¹é
  • early protein
    ÃʱâÃâÇö´Ü¹éÁú
  • endogenous protein
    ³»Àμº ´Ü¹éÁú.
  • envelope,protein
  • eosinophil cationic protein
    È£»ê±¸¾çÀ̿´ܹé
  • eosinophil protein X
    È£»ê±¸´Ü¹é X
  • estrogen receptor protein
    ¸®¿¡½ºÆ®·Î°Õ ¼ö¿ë(áôé») ´Ü¹éÁú(Ó±ÛÜòõ).
  • estrogen receptor protein
    ¿¡½ºÆ®·Î°Õ¼ö¿ëü´Ü¹éÁú.
  • foreign protein
    ÀÌÁ¾´Ü¹é.
  • ganglioside activator protein
    °»±Û¸®¿À»çÀ̵å Ȱ¼º´Ü¹éÁú
  • glial fibrillary acidic protein
    ½Å°æ±³¿ø¼¶À¯(Îïê«àéë«)»ê(ß«)´Ü¹é
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • Lamella of bone
    »ÀÃþÆÇ
    [¿¾ ¿ë¾î] °ñÃþÆÇ
  • Fibrous bone marrow
    ¼¶À¯°ñ¼ö [¼¶À¯»À¼ÓÁú]
    [¿¾ ¿ë¾î] ¼¶À¯¼º°ñ¼ö
  • Reticulofibrous periosteal bone
    ¼¼¸Á¼¶À¯»À¹Ù±ù¸·»À
    [¿¾ ¿ë¾î] ¼¼¸Á¼¶À¯¼º°ñ¸·°ñ
  • Triquetral bone
    ¼¼¸ð»À
    [¿¾ ¿ë¾î] »ï°¢±Ù
  • Third metacarpal bone
    ¼Â°¼ÕÇ㸮»À
    [¿¾ ¿ë¾î] Á¦1Áß¼ö°ñ
  • Scaphoid bone
    ¼Õ¹è»À
    [¿¾ ¿ë¾î] ÁÖ»ó°ñ
  • Tubercle of scaphoid bone
    ¼Õ¹è»À°áÀý
    [¿¾ ¿ë¾î] ÁÖ»ó°ñ°áÀý
  • Gelatinous bone marrow
    ¾Æ±³°ñ¼ö [¾Æ±³»À¼ÓÁú]
    [¿¾ ¿ë¾î] ±³¾ç°ñ¼ö
  • Gelatinous bone marrow
    ¾Æ±³°ñ¼ö [¾Æ±³»À¼ÓÁú]
    [¿¾ ¿ë¾î] ¾Æ±³°ñ¼ö
  • Medial cuneiform bone
    ¾ÈÂʽû±â»À
    [¿¾ ¿ë¾î] ³»Ãø¼³»ó°ñ
  • Capitate bone
    ¾Ë¸Ó¸®»À
    [¿¾ ¿ë¾î] À¯µÎ°ñ
  • Perichondral bone
    ¿¬°ñ¸·»À
    [¿¾ ¿ë¾î] ¿¬°ñ¸·°ñ
  • Cartilagenous bone
    ¿¬°ñ»À
    [¿¾ ¿ë¾î] ¿¬°ñ¼º°ñ
  • Definite compact bone
    ¿Ï¼ºÄ¡¹Ð»À
    [¿¾ ¿ë¾î] ¿Ï¼ºÄ¡¹Ð°ñ
  • Frontal bone
    À̸¶»À [ÀüµÎ°ñ]
    [¿¾ ¿ë¾î] ÀüµÎ°ñ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • CRO protein
    CRO ´Ü¹éÁú (Ó±ÛÜòõ)
  • crystal protein
    °áÁ¤ ´Ü¹éÁú(Ì¿ïÜÓ±ÛÜòõ)
  • cyclic AMP receptor protein
    °í¸®AMP ¼ö¿ëü ´Ü¹éÁú(áôé»ô÷Ó±ÛÜòõ)
  • delipidized protein
    Å»Áö´Ü¹éÁú(÷­ò·Ó±ÛÜòõ)
  • derived protein
    À¯µµ´Ü¹éÁú(ë¯ÓôÓ±ÛÜòõ)
  • DNA binding protein
    DNA °áÇÕ ´Ü¹éÁú(Ì¿ùêÓ±ÛÜòõ) (ÔÒ) single strand binding protein
  • dna G protein
    dna G ´Ü¹éÁú(Ó±ÛÜòõ)
  • DNA-melting protein
    "DNAÀ¶ÇØ ´Ü¹éÁú(ë×ú°Ó±ÛÜòõ), (ÔÒ) single-strand binding protein"
  • DNA unwinding protein
    "DNA Ç®±â ´Ü¹éÁú(Ó±ÛÜòõ), (ÔÒ) single-strand binding protein"
  • docking protein
    µµÅ· ´Ü¹éÁú(Ó±ÛÜòõ)
  • early protein
    Á¶±â ´Ü¹éÁú (ðÄÑ¢Ó±ÛÜòõ)
  • ectopic protein
    ÀÌ¼Ò ´Ü¹éÁú(ì¶á¶Ó±ÛÜòõ)
  • eIF-2 stimulating protein
    eIF-2 ÀÚ±Ø ´Ü¹éÁú(í©Ð½Ó±ÛÜòõ)
  • electron transfer protein
    ÀüÀÚÀü´Þ ´Ü¹éÁú(ï³í­îîÓ¹Ó±ÛÜòõ)
  • encephalitogenic protein
    ³ú¿°»ý¼º ´Ü¹éÁú(Òàæúßæà÷Ó±ÛÜòõ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • metatarsal bone
    ÁßÁ·°ñ
  • navicular bone
    ¹ß¹è°ñ, ÁÖ»ó°ñ
  • new bone formation
    ½Å°ñÇü¼º
  • occipital bone
    逵롖
  • palatine bone
    ±¸°³°ñ
  • parietal bone
    µÎÁ¤°ñ
  • periosteal bone
    °ñ¸·(¼º)°ñ
  • periosteal new bone
    °ñ¸·¼º½Å»ý°ñ
  • pubic bone
    Ä¡°ñ
  • reactive bone excrescence
    ¹ÝÀÀ¼º°ñµ¹Ãâ
  • resorption of bone
    °ñÈí¼ö
  • scaphoid bone
    ¼Õ¹è°ñ, ÁÖ»ó°ñ
  • sclerotic bone island
    °æÈ­¼º°ñ¼¶
  • sesamoid bone
    Á¾ÀÚ°ñ
  • solitary bone cyst
    °í¸³°ñ³¶
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
MCP maximum closure pressure; maximum contraction pattern; malanocortin receptor; melphalan, cyclophosph...
SCP single-celled protein; standard care plan; sodium cellulose phosphate; soluble cytoplasmic protein; ...
TP temperature and pressure; temperature probe; temporal peak; temporoparietal; tension pneumothorax; t...
TSP testis-specific protein; thrombin-sensitive protein; thrombospondin; total serum protein; total susp...
BC Bone Conduction
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
CB1 cannabinoid 1 receptors
EGFr Epithelial Growth Factor receptors
ER, PR Estrogen and progesterone receptors
FcR Fc gamma Receptors
GRPR Gastrin-releasing peptide receptors
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone activity
    °ñ Ȱ¼º
  • bone age
    °ñ·É, °ñ ¿¬·É
    °ñ ¼º¼÷µµ¸¦ ³ªÅ¸³»´Â °³³äÀÌ°í °Ç°­¿¡¼­ ¾òÀº ÀÏÁ¤ÇÑ Ç¥ÁØÀ» ¿¬·É°úÀÇ °ü°è·Î Ç¥ÇöÇÑ °ÍÀÌ´Ù.
  • bone and joint surgery
    °ñ°üÀý ¿Ü°ú
  • bone ash
    °ñȸ
    »À¸¦ Å¿ö¼­ ¸¸µç °¡·ç, ºñ·á¿¡ ¾²À̱⵵ ÇÑ´Ù.
  • bone augmentation
    °ñ Áõ´ë¼ú
  • bone blend
    °ñ È¥ÇÕ
  • bone cell
    °ñ ¼¼Æ÷
    °ñÁ¶Á÷ÀÇ ±âº» ¼¼Æ÷. °ñ Á¶Á÷¿¡´Â µüµüÇÑ °ñ ±âÁú¾È¿¡ °ñ¼Ò°­À̶ó°í ÇÏ´Â Æ´ÀÌ ±ºµ¥±ºµ¥ ÀÖ°í, ±× ¼Ó¿¡ 1°³¾¿ÀÇ °ñ ¼¼Æ÷°¡ µé¾î ÀÖ´Ù. °ñ ¼¼Æ÷ÀÇ ÇüÅ´ °ñ¼Ò°­°ú ÀÏÄ¡ÇÏ¿© ÆíÆòÇÑ Å¸¿øÇüÀ¸·Î, ±æÀÌ´Â 15¡­27 ¥ìmÀÌ´Ù. °ñ ¼¼Æ÷´Â ´Ù¼öÀÇ °¡´Â ¿øÇüÁú µ¹±â°¡ À־, À̰ÍÀÌ ±âÁú ³»ÀÇ °ñ ¼¼°üÀ» ÅëÇÏ¿© °¡±îÀÌ ÀÖ´Â °ñ ¼¼Æ÷ÀÇ µ¹±â¿Í ÇÕÄ£´Ù. °ñ ¼¼Æ÷´Â º»·¡ °áÇÕÁ¶Á÷ÀÇ ¼¶À¯¾Æ¼¼Æ÷¿¡¼­ Çü¼ºµÇ´Â °ÍÀ¸·Î, ¸ÕÀú °ñ¾Æ¼¼Æ÷°¡ µÇ¾î, À̰ÍÀÌ ±âÁúÀ» ¸¸µé°í ÀÚ½ÅÀº ±× ±âÁú ¼Ó¿¡ µé¾î°¡ °ñ¼¼Æ÷·Î µÈ´Ù. À̰ÍÀº °ñ Á¶Á÷ÀÇ Á¦Á¶ÀÚÀ̸ç, ¼¼Æ÷ÁúÀº ¹Ì·®ÀÇ ¹ÌÅäÄܵ帮¾Æ¸¦ Æ÷ÇÔÇϰí, È£¾à¿°±â¼ºÀ» ³ªÅ¸³½´Ù.
  • bone chisel
    »À ²ø
  • bone conduction test
    °ñÀüµµ ½ÃÇè
  • bone curette
    °ñÅ¥·¿, °ñ ¼ÒÆÄ
  • bone cyst
    °ñ ³¶
  • bone density
    °ñ ¹Ðµµ
  • bone disease
    °ñ Áúȯ
    µ¿ÀǾî=osteo
  • bone dislocation
    °ñ ÀüÀÌ, °ñ ÀüÀ§
  • bone factor
    °ñ ÀÎÀÚ
    Ȱ¼ºÀ̳ª ÀÚÁï¿¡ ´ëÇÑ Ä¡Á¶°ñÀÇ »ó´ë ¹ÝÀÀ.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
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, complement Molecules on the surface of some B-lymphocytes and macrophages, that recognise and combine with the c3b, c3d, c1q, and c4b components of complement.
(12 Dec 1998)
receptors, complement 3b Molecular sites on or in some B-lymphocytes and macrophages that recognise and combine with complement 3b. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids.
(12 Dec 1998)
receptors, complement 3d Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognise and combine with complement 3d. Human cr2 serves as a receptor for both c3dg and the gp350/220 glycoprotein of herpes virus 4, human, and binds the monoclonal antibody okb7, which blocks binding of both ligands to the receptor.
(12 Dec 1998)
receptors, concanavalin a Glycoprotein moieties on the surfaces of cell membranes that bind concanavalin a selectively; the number and location of the sites depends on the type and condition of the cell.
(12 Dec 1998)
receptors, corticotropin Cell surface receptors that bind corticotropin (acth, adrenocorticotropic hormone) with high affinity and trigger intracellular changes. Pharmacology suggests there may be multiple acth receptors. An acth receptor has been cloned and belongs to a subfamily of g-protein-coupled receptors. In addition to the adrenal cortex, acth receptors are found in the brain and immune systems.
(12 Dec 1998)
receptors, corticotropin-releasing hormone Cell surface proteins that bind corticotropin-releasing hormone with high affinity and trigger intracellular changes which influence the behaviour of cells. The corticotropin releasing-hormone receptors on anterior pituitary cells mediate the stimulation of corticotropin release by hypothalamic corticotropin releasing factor. The physiological consequence of activating corticotropin-releasing hormone receptors on central neurons is not well understood.
(12 Dec 1998)
receptors, cxcr4 Seven-transmembrane G-protein-coupled receptors for alpha-chemokines. They also function as fusion cofactors for T-cell-tropic HIV-1 strains.
(12 Dec 1998)
receptors, cyclic AMP Cell surface proteins that bind cyclic AMP with high affinity and trigger intracellular changes which influence the behaviour of cells. The best characterised cyclic AMP receptors are those of the slime mold dictyostelium discoideum. The transcription regulator cyclic AMP receptor protein of prokaryotes is not included nor are the eukaryotic cytoplasmic cyclic AMP receptor proteins which are the regulatory subunits of cyclic AMP-dependent protein kinases.
(12 Dec 1998)
receptors, cytoadhesin A group of integrins that includes the platelet outer membrane glycoprotein gpiib-iiia (platelet glycoprotein gpiib-iiia complex) and the vitronectin receptor (receptors, vitronectin). They play a major role in cell adhesion and serve as receptors for fibronectin, von willebrand factor, and vitronectin.
(12 Dec 1998)
receptors, cytokine Cell surface proteins that bind cytokines and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, cytoplasmic and nuclear Proteins in the cytoplasm or nucleus that specifically bind signalling molecules and trigger changes which influence the behaviour of cells. The major groups are the steroid hormone receptors, which usually are found in the cytoplasm, and the thyroid hormone receptors, which usually are found in the nucleus. Receptors, unlike enzymes, generally do not catalyze chemical changes in their ligands.
(12 Dec 1998)
receptors, dopamine Cell-surface proteins that bind dopamine with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, dopamine d1 A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, by their mode of action.
(12 Dec 1998)
receptors, dopamine d2 A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, their mode of action.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • 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: 4
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
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