¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"receptor"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
  • nicotinic receptor
    ´ÏÄÚÆ¾ ¼ö¿ëü
  • olfactory receptor
    Èİ¢°¨¼ö±â
  • olfactory receptor cells
    Èİ¢¼ö¿ë¼¼Æ÷
  • opiate receptor
    ¾ÆÆí¼ö¿ëü(áôé»ô÷)
  • opiate receptor
    ¾ÆÆí¼ö¿ëü.
  • opioid receptor
    ¾ÆÆí¾ç¼ö¿ëü
  • opioid receptor
    ¾ÆÆí°è¹°Áú¼ö¿ëü.
  • opioid receptor
    ¾ÆÆí¾ç¹°Áú¼ö¿ëü.
  • opioid receptor
    ¾ÆÆí¾ç¹°Áú¼ö¿ëü.
  • paciniform receptor
    ÆÄÄ¡´Ï¾ç °¨¼ö±â
  • pathogen receptor
    º´¿ø±Õ¼ö¿ëü
  • platelet receptor
    Ç÷¼ÒÆÇ¼ö¿ëü
  • postsynaptic receptor
    ¿¬Á¢Èļö¿ëü
  • prejunctional neuromuscular receptor
    ½Å°æ±ÙÁ¢ÇÕÀü¼ö¿ëü
  • pressor receptor
    ¾Ð·Â¼ö¿ëü(äâæ³áôé»ô÷).
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 5
ADRBK beta-1-adrenergic receptor kinase
ADRBR adrenergic beta-receptor
AIRA anti-insulin receptor antibody
AR absolute risk; accounts receivable; achievement ratio; actinic reticuloid [syndrome]; active resista...
ARB adrenergic receptor binder
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 5
A(1)-ADOR A(1)-adenosine receptor
A(2A)AR A(2A) adenosine receptor
A2AR A2 adenosine receptor
A(2A)R A(2A) receptor
A(3)AR A(3) adenosine receptor
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 15 ÆäÀÌÁö: 5
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)
receptors, drug Proteins that bind specific drugs with high affinity and trigger intracellular changes influencing the behaviour of cells. Drug receptors are generally thought to be receptors for some endogenous substance not otherwise specified.
(12 Dec 1998)
receptors, eicosanoid Cell surface proteins that bind eicosanoids with high affinity and trigger intracellular changes influencing the behaviour of cells. Among the eicosanoid receptors are receptors for the prostaglandins, thromboxanes, and leukotrienes.
(12 Dec 1998)
receptors, endothelin Cell surface proteins that bind endothelin with high affinity and trigger intracellular changes which influence the behaviour of 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, erythropoietin Cell surface proteins that bind erythropoietin with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, estradiol Cytoplasmic proteins that bind estradiol, migrate to the nucleus, and regulate DNA transcription.
(12 Dec 1998)
receptors, fc Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognise and combine with the fc (crystallizable) portion of immunoglobulin molecules.
(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, fibronectin Specific sites or molecular structures on or in cells with which fibronectins react or to which they bind. Studies have shown that these receptors function in certain types of adhesive contact as well as playing a major role in matrix assembly. These are the traditional fibronectin receptors, also called vla-5 receptors or alpha 5 beta 1 integrins. There are also other integrins that bind fibronectin, including alpha v beta 1.
(12 Dec 1998)
receptors, fsh Cell surface proteins that bind follicle-stimulating hormone (follitropin, fsh) with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, gaba Cell-surface proteins that bind gaba with high affinity and trigger changes that influence the behaviour of cells. Gaba-a receptors control chloride channels formed by the receptor complex itself. They are blocked by bicuculline and usually have modulatory sites sensitive to benzodiazepines and barbiturates. Gaba-b receptors act through g-proteins on several effector systems, are insensitive to bicuculline, and have a high affinity for l-baclofen.
(12 Dec 1998)
receptors, gaba-a Cell surface proteins which bind gaba and control an integral membrane chloride channel. Gaba-a receptors are the most prevalent inhibitory neurotransmitter receptors in the brain. Several isoforms have been cloned, and they belong to a superfamily which includes nicotinic receptors, glycine receptors, and 5ht-3 receptors. Most gaba-a receptors have separate modulatory sites sensitive to benzodiazepines and to barbiturates.
(12 Dec 1998)
receptors, gaba-b Cell surface proteins which bind gaba and influence cells via interactions with g-proteins. Gaba-b receptors are pharmacologically characterised by their insensitivity to the blocker bicuculline and sensitivity to the agonist l-baclofen. They are found both presynaptically and postsynaptically, and act variously by inhibition of adenylate cyclase, activation of phospholipase a2, activation of potassium channels, and inactivation of voltage-activated calcium channels.
(12 Dec 1998)
receptors, gastrointestinal hormone Cell surface proteins that bind gastrointestinal hormones with high affinity and trigger intracellular changes influencing the behaviour of cells. most gastrointestinal hormones also act as neurotransmitters so these receptors are also present in the central and peripheral nervous systems.
(12 Dec 1998)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 5
TGF-beta receptor protein kinase <enzyme> Belongs to the receptor-type serine-threonine kinase subfamily; from chick embryo, related to type II receptor for tgf-beta; 502 aa residues, mw 56,766 da; aa sequence given in first source
Registry number: EC 2.7.1.-
Synonym: tgf-beta rpk, rpk-1, rpk-2
(26 Jun 1999)
early receptor potential A voltage arising across the eye from a charge displacement within photoreceptor pigment, in response to an intense flash of light.
(05 Mar 2000)
thyroid receptor antibody A test that measures the amount of an antibody (thyroid stimulating antibody) which is directed against a receptor for TSH on the thyroid gland. This antibody acts like TSH and stimulates the thyroid to produce excessive amounts of thyroid hormone. The presence of this antibody generally indicates Grave's disease (hyperthyroidism).
(27 Sep 1997)
TIE-2 receptor tyrosine kinase <enzyme> Expressed in developing vascular endothelial cells; unlike tie-1, also expressed in lens epithelium and heart epicardium; has the same organization of amino acid sequence motifs characteristic of tie-1; aa sequence of the intracellular and extracellular regions of tie-1 and tie-2 are 79% and 32% identical, respectively; aa sequence of both kinases given in first source
Registry number: EC 2.7.10.-
Synonym: tie-2-rtk
(26 Jun 1999)
tie receptor tyrosine kinase <enzyme> From human leukaemia cells; expressed in developing vascular endothelial cell; has homology with egf, bfgf, csf-1, pdgf and stem cell factor receptors; ligand and biologic function not known as of 12/92; tie-1 receptor tyrosine kinase is rat homolog of tie receptor tyrosine kinase; aa sequence known
Registry number: EC 2.7.10.-
Synonym: tie-1 receptor tyrosine kinase, tie-1 rtk
(26 Jun 1999)
endothelin receptor Simple squamous epithelium lining blood vessels, lymphatics and other fluid filled cavities (such as the anterior chamber of the eye). Mesodermally derived, unlike most epithelia.
(18 Nov 1997)
epidermal growth factor receptor protein-tyrosine kinase <enzyme> The catalytic protein-tyrosine kinase domain found on the cytoplasmic beta-portion of epidermal growth factor receptor.
Registry number: EC 2.7.1.-
(12 Dec 1998)
estradiol receptor tyrosine kinase <enzyme> Calcium and calmodulin dependent
Registry number: EC 2.7.1.-
Synonym: ertk
(26 Jun 1999)
kainate receptor A type of glutamate receptor that participates in excitatory neurotransmission and also binds kainate and acts as a cation channel; injection of kainate causes death of neurons but preserves glial cells and axons.
(05 Mar 2000)
Fc receptor Receptors present on a variety of cells for the Fc fragment of immunoglobulins. These receptors recognise immunoglobulins of the IgG and IgE class.
(05 Mar 2000)
fibroblast growth factor receptor Family of receptor tyrosine kinases for fibroblast growth factor.
(18 Nov 1997)
fibroblast growth factor receptor-like embryonic kinase <enzyme> Found in avian embryonic tissue; involved in early differentiation of skeletal muscle.
Registry number: EC 2.7.1.-
Synonym: frek
(26 Jun 1999)
laminin receptor A receptor found in many cell types that binds laminin and has a role in cell attachment and neurite outgrowth.
(05 Mar 2000)
L-AP4 receptor A type of glutamate receptor that also binds a particular synthetic agonist and acts as a cation channel.
(05 Mar 2000)
LDL receptor disorder Abnormality in clearance of LDL from the plasma due to abnormality in LDL receptor activity; causes hypercholesterolaemia.
(05 Mar 2000)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 5
  • Receptor, EphA1 - »õâ The founding member of the Eph family receptors. It was first cloned from an erythropoietin-producing human hepatocellular carcinoma cell line and is highly conserved among many mammalian species. Overproduction of the EphA1 receptor is associated with tumors and tumor cells of epithelial origin. It is also expressed at high levels in LIVER; LUNG; and KIDNEY; which is in contrast to many other members of the Eph receptor that are found primarily in tissues of the nervous system.
    Synonyms : EPHA1 Protein, EPHA1 Receptor Tyrosine Kinase, Eph Receptor
  • Receptor, EphA2 - »õâ An Eph family receptor found abundantly in tissues of epithelial origin. It is expressed in a diverse array of tissues during embryonic development, suggesting that it may play a role in embryogenesis. In adult tissues high levels of the receptor are expressed in the LUNG; SKIN; SMALL INTESTINE and OVARY.
    Synonyms : EphA2 Protein, EphA2 Receptor, EphA2 Receptor Tyrosine Kinase, EphA2-Tyrosine Kinase, Epithelial Cell Kinase Protein, Mammary-Derived Tyrosine Kinase 2, EphA2 Tyrosine Kinase, Mammary Derived Tyrosine Kinase 2
  • Receptor, EphA3 - »õâ An eph family receptor that is found primarily in adult BRAIN and variety of tissues in the developing embryo tissues. During embryonic development high levels of EphA3 receptor expression is seen in the nervous system and coincides with neuronal cell migration, suggesting a role for this protein in axonal pathfinding.
    Synonyms : Cek4 Eph Receptor, Cek4 Receptor Protein-Tyrosine Kinase, Eph Receptor Cek4, EphA3 Protein, Cek4 Receptor Protein Tyrosine Kinase, Cek4, Eph Receptor, Eph Receptor, Cek4
  • Receptor, EphA4 - »õâ An eph family receptor found in variety of tissues including BRAIN. During embryogenesis, EphA4 receptor exhibits a diverse spatial and temporal pattern of expression suggesting its role in multiple developmental processes.
    Synonyms : Cek-8 Kinase, Eph-A4 Receptor Tyrosine Kinase, EphA4 Protein, Ephrin Receptor A4, Receptor Tyrosine Kinase Eph-A4, Sek-1 Receptor Tyrosine Kinase, Cek 8 Kinase, Eph A4 Receptor Tyrosine Kinase, Receptor Tyrosine Kinase Eph A4, Sek 1 Receptor Tyrosine Kinase
  • Receptor, EphA5 - »õâ An eph family receptor found primarily in differentiated neuronal tissues. Several isoforms of EphA5 receptor occur due to multiple alternative RNA splicing. The protein is prominently expressed in the NEURONS of the LIMBIC SYSTEM during development and throughout adult life, suggesting its role in the plasticity of limbic structure and function.
    Synonyms : Brain-Specific Kinase, EphA5 Protein, bsk Tyrosine Kinase, Brain Specific Kinase, Tyrosine Kinase, bsk
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 5 ÆäÀÌÁö: 5
receptor A large molecule that recognizes specific chemicals (normally neurotransmitters, hormones, and similar endogenous substances) and transmits the message carried by the chemical into the cell on which the receptor resides. [5]
Ãâó: teens.drugabuse.gov/utilities/glossary2.asp
receptor A specific molecule on the surface of or within the cell that recognizes and binds with other specific molecules.
Ãâó: urology.ucsf.edu/patientGuides/termsR.html
receptor A site on the surface of a cell which in a lock and key fashion fits into a complementary site on another cell or protein, as in the binding of an antibody to an antigen.
Ãâó: www.pemphigus.org/glossary.html
receptor A protein or group of associated proteins in a cell or on its surface that selectively binds a specific substance (called a ligand).
Ãâó: www.i-bio.gov.uk/UkBioportal/Beginners/html/glossa...
receptor A cell component that combines with a drug, hormone, or chemical to alter the function of that cell
Ãâó: www.betterbones.com/utilities/glossary.htm
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • 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: 5
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 5
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: 5
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: 5
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 5
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 5
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 5
ÅëÇÕ°Ë»ö ¿Ï·á