¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Bone Morphogenetic Protein Receptors, Type II"¿¡ ´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: 11
  • ¿µ¹®
    ÇѱÛ
  • collar bone
    ºøÀå»À, ¼â°ñ
  • compact bone
    Ä¡¹Ð»À
  • cortical bone
    °ÑÁú»À, ÇÇÁú°ñ
  • costal bone
    °¥ºñ»À, ´Á°ñ
  • cranial bone
    ¸Ó¸®»À, µÎ°³°ñ
  • cranial bone flap
    ¸Ó¸®»ÀÇÇÆÇ(¼ú), µÎ°³°ñÇÇÆÇ
  • cuboid bone
    ÀÔ¹æ»À
  • cuneiform bone
    ½û±â»À, ¼³»ó°ñ
  • carpal bone
    ¼Õ¸ñ»À, ¼ö±Ù°ñ
  • cartilage bone
    ¿¬°ñ»À
  • cancellous bone
    °¹¼Ø»À, ÇØ¸é°ñ
  • endochondral bone
    ¿¬°ñ³»»À
  • ethmoid bone
    ¹úÁý»À, »ç°ñ
  • fibrous dysplasia of bone
    »À¼¶À¯Çü¼ºÀÌ»ó
  • flat bone
    ³³ÀÛ»À, ÆíÆò°ñ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
  • bone marrow function test
    °ñ¼ö±â´É°Ë»ç
  • bone marrow transplantation retinopathy
    °ñ¼öÀ̽ĸÁ¸·º´Áõ
  • bone marrow-derived cell
    °ñ¼öÀ¯·¡¼¼Æ÷
  • bone mineral metabolism
    »À±¤¹°´ë»ç, °ñ±¤¹°Áú´ë»ç
  • brittle bone
    (¢¡osteogenesis imperfecta) ºÒ¿ÏÀü»À¹ß»ý, ºÒ¿ÏÀü°ñÇü¼ºÁõ
  • cancellous bone
    (¢¡spongy bone) °¹¼Ø»À, ÇØ¸é»À
  • capitate bone
    ¾Ë¸Ó¸®»À
  • carpal bone
    ¼Õ¸ñ»À
  • cartilage bone
    ¿¬°ñ»À
  • collar bone
    (¢¡clavicle) ºøÀå»À, ¼â°ñ
  • compact bone
    Ä¡¹Ð»À
  • cortical bone
    °ÑÁú»À
  • costal bone
    (¢¡rib) °¥ºñ»À, ´Á°ñ
  • cranial bone
    ¸Ó¸®»À, µÎ°³°ñ
  • cuboid bone
    ÀÔ¹æ»À
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
  • quadrate bone
    ¹æ°ñ(Û°Íé), ¹æÇü°ñ.
  • reactive bone excrescence
    ¹ÝÀÀ¼º °ñ µ¹Ãâ
  • red bone marrow
    Àû»ö°ñ¼ö(îåßäÍéâÐ).
  • red bone marrow
    Àû»ö°ñ¼ö (Àû»ö»À¼ÓÁú)
  • red bone marrow
    Àû»ö°ñ¼ö(îåßäÍéâÐ).
  • AA protein
    ¾Æ¹Ð·ÎÀ̵åA´Ü¹é(¡­Ó±ÛÜ)
  • ABP=> androgen-binding protein
    ¾Èµå·ÎÁ¨°áÇմܹé
  • Bence Jones protein
    º¥½º-Á¸½º´Ü¹é.
  • Bence-Jones protein
    º¥½º-Á¸½º ´Ü¹éÁú
  • C protein
    C´Ü¹éÁú
  • C-Fos protein
    ¾¾-Æ÷½º´Ü¹é(Ó±ÛÜ)
  • C-reative protein =CRP
    C¹ÝÀÀ¼º ´Ü¹é(Áú).
  • C-reative protein =CRP
    [¸é¿ª] [ÀÓº´]C¹ÝÀÀ¼º ´Ü¹éÁú.
  • DNA-binding protein
    DNA °áÇմܹéÁú
  • G protein
    G ´Ü¹é(Ó±ÛÜ)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
  • protein score
    ´Ü¹é°¡(ËÀËÑ˧) ½ÄǰÀÇ .
  • protein sensitization
    ´Ü¹é°¨ÀÛ(¡­ÊïíÂ).
  • protein separation
    ´Ü¹éºÐ¸®
  • protein sparing effect
    ´Ü¹éÁúÀý¾àÈ¿°ú(Ó±ÛÜòõï½å³üùÍý).
  • protein synthesis
    ´Ü¹éÁúÇÕ¼º.
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ(Ó±ÛÜùêà÷ì×í­).
  • 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.
  • protein-losing enteropathy
    ´Ü¹é»ó½Ç¼º À庴Áõ(íóÜ»ñø)
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
  • peripheral protein
    ÁÖº¯´Ü¹éÁú(ñ²Ü«Ó±ÛÜòõ)
  • polycephalic protein
    º¹ÇÕ±â´É ´Ü¹éÁú(ÜÜùêѦÒöÓ±ÛÜòõ)
  • polyfunctional protein
    ´Ù±â´É ´Ü¹éÁú(ÒýѦÒöÓ±ÛÜòõ)
  • P protein
    P ´Ü¹éÁú(Ó±ÛÜòõ)
  • prepriming protein
    ÇÁ·¹ÇÁ¶óÀÌ¹Ö ´Ü¹éÁú(Ó±ÛÜòõ)
  • primary derived protein
    ÀÏÂ÷ À¯µµ ´Ü¹éÁú(ìéó­ë¯ÓôÓ±ÛÜòõ)
  • primary protein derivative
    ÀÏÂ÷ ´Ü¹éÁúÀ¯µµÃ¼
  • protein
    ´Ü¹éÁú(Ó±ÛÜòõ)
  • protein A
    ´Ü¹éÁú(Ó±ÛÜòõ) A
  • protein biosynthesis
    ´Ü¹éÁú »ýÇÕ¼º(Ó±ÛÜòõßæùêà÷)
  • protein blotting
    ´Ü¹éÁú(Ó±ÛÜòõ) ºí·ÔÆÃ
  • protein-bound iodine
    ´Ü¹éÁú°áÇÕ(Ó±ÛÜòõÌ¿ùê) ¿äµå
  • protein C
    ´Ü¹éÁú(Ó±ÛÜòõ) C
  • protein-calorie malnutrition
    ´Ü¹éÁú(Ó±ÛÜòõ)-Ä®·Î¸® ¿µ¾ç½ÇÁ¶(ç½å×ã÷ðà)
  • protein coat
    ´Ü¹éÁú(Ó±ÛÜòõ) ÄÚÆ®
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 11
BIS bone cement implantation syndrome; Brain Information Service; building illness syndrome
BL Barre-Lieou [syndrome]; basal lamina; baseline; Bessey-Lowry [unit]; black light; bladder; bleeding;...
BM Bachelor of Medicine; barium meal; basal medium; basal metabolism; basement membrane; basilar membra...
BMA bone marrow arrest; British Medical Association
BMAP bone marrow acid phosphatase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 11
Type 1 type
type I type B
CRBP(II) Cellular retinol-binding protein type II
H-FABP Heart-type Fatty Acid Binding Protein
PP-1 Protein phosphatase type 1
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone marrow needle
    °ñ¼ö õÀÚ Ä§
  • bone marrow puncture
    °ñ¼ö õÀÚ
  • bone marrow suppression
    °ñ¼ö ¾ïÁ¦
  • bone marrow-derived lymphocyte
    °ñ¼ö À¯·¡ Àӯı¸
  • bone maturation
    °ñ ¼ºÀå
  • bone meal
    »À°¡·ç, °ñºÐ
  • bone metastasis
    °ñ ÀüÀÌ
  • bone onlay
    °ñ ÀÌ½ÄÆí
  • bone peg
    »À¸ø, °ñÁ¤
  • bone proliferation
    °ñ Áõ½Ä
  • bone reduction procedure
    °ñ Á¦°Å¼ú
  • bone remodeling
    °ñ ÀçÇü¼º
  • bone repair
    °ñ ȸº¹
  • bone resorption
    °ñ Èí¼ö
  • bone saw
    °ñ Åé
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
receptors, retinoic acid Proteins in the nucleus or cytoplasm that specifically bind retinoic acid or retinol and trigger changes in the behaviour of cells. Retinoic acid receptors, like steroid receptors, are ligand-activated transcription regulators. Several types have been recognised.
(12 Dec 1998)
receptors, sensory Specialised neurons or parts of neurons which transduce sensory information and relay it centrally. Included are receptors for stimuli outside the body (exteroceptors) as well as receptors for stimuli from within the body itself (interoceptors and proprioceptors). Sensory receptors may include accessory structures which condition (e.g., filter) the input received by the receptor neurons themselves.
(12 Dec 1998)
receptors, serotonin Cell-surface proteins that bind serotonin and trigger intracellular changes which influence the behaviour of cells. Several types of serotonin receptors have been recognised which differ in their pharmacology, molecular biology, and mode of action.
(12 Dec 1998)
receptors, sigma A class of cell surface receptors recognised by its pharmacological profile. Sigma receptors were originally considered to be opioid receptors because they bind certain synthetic opioids. However they also interact with a variety of other psychoactive drugs, and their endogenous ligand is not known (although they can react to certain endogenous steroids). Sigma receptors are found in the immune, endocrine, and nervous systems, and in some peripheral tissues.
(12 Dec 1998)
receptors, somatomedin Cell surface receptors that bind somatomedins and trigger intracellular changes which influence the behaviour of cells. Studies have disclosed two types of receptors for this family of peptide hormones. The type I receptor is homologous to the insulin receptor and has tyrosine kinase activity. The type II receptor is identical to the mannose-6-phosphate receptor which is important in trafficking of lysosomal enzymes.
(12 Dec 1998)
receptors, somatostatin Cell surface proteins that bind somatostatin and trigger intracellular changes which influence the behaviour of cells. Somatostatin is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Activated somatostatin receptors on pituitary cells inhibit the release of growth hormone; those on endocrine and gastrointestinal cells regulate the absorption and utilization of nutrients; and those on neurons mediate somatostatin's role as a neurotransmitter.
(12 Dec 1998)
receptors, somatotropin Cell surface proteins that bind somatotropin with high affinity and trigger intracellular changes influencing the behaviour of cells. Activation of growth hormone receptors regulates amino acid transport through cell membranes, RNA translation to protein, DNA transcription, and protein and amino acid catabolism in many cell types. Many of these effects are mediated indirectly through stimulation of the release of somatomedins.
(12 Dec 1998)
receptors, steroid Proteins found usually in the cytoplasm or nucleus that specifically bind steroid hormones and trigger changes influencing the behaviour of cells. The steroid receptor-steroid hormone complex regulates the transcription of specific genes.
(12 Dec 1998)
receptors, tachykinin Cell surface proteins that bind tachykinins with high affinity and trigger intracellular changes influencing the behaviour of cells. Three classes of tachykinin receptors have been characterised, the nk-1, nk-2, and nk-3, which prefer, respectively, substance p, neurokinin a (substance k, neurokinin alpha, neuromedin l), and neurokinin b (neurokinin beta, neuromedin k).
(12 Dec 1998)
receptors, thrombin Cell surface proteins that specifically bind thrombin and trigger changes in the behaviour of blood cells. There are at least two types of thrombin receptors on platelets. The higher affinity receptors mediate the inhibition of stimulated adenylate cyclase, the secretion of acid hydrolases, and the activation of phospholipase a2. The lower affinity receptors are linked to phospholipase c and trigger platelet aggregation and exposure of fibrinogen binding sites. A human platelet thrombin receptor has been cloned and is a member of the family of peptide receptors. There are also thrombin receptors on endothelial cells and smooth muscle cells.
(12 Dec 1998)
receptors, thromboxane Cell surface proteins that bind thromboxanes with high affinity and trigger intracellular changes influencing the behaviour of cells. at least a subset of thromboxane receptors act via the inositol phosphate and diacylglycerol second messenger systems.
(12 Dec 1998)
receptors, thyroid hormone Proteins, usually found in the nucleus, that specifically bind thyroid hormones and regulate DNA transcription. These proteins, termed c-erba, are activated by hormones and cause differentiation of erythroid progenitor cells which irreversibly lose proliferative potential. Thus c-erba proteins act as growth suppressors. The c-erba proteins are encoded by at least two genes, c-erba alpha and c-erba beta. Each of these has two isoforms. Mutations in the ligand-binding domain of the beta form causes thyroid hormone resistance syndrome.
(12 Dec 1998)
receptors, thyrotropin Cell surface proteins that bind thyrotropin and trigger intracellular changes influencing the behaviour of cells. These receptors are present in the nervous system and on cells in the thyroid gland. Autoantibodies to these receptors are implicated in graves', hashimoto's, and other thyroid diseases.
(12 Dec 1998)
receptors, thyrotropin-releasing hormone Cell surface receptors that bind thyrotropin releasing hormone (trh) with high affinity and trigger intracellular changes which influence the behaviour of cells. Activated trh receptors in the anterior pituitary stimulate the release of thyrotropin (thyroid stimulating hormone, tsh). Trh receptors on neurons mediate neurotransmission by trh.
(12 Dec 1998)
receptors, transferrin Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • 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: 11
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 11
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 11
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: 11
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: 11
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 11
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 11
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 11
ÅëÇÕ°Ë»ö ¿Ï·á