¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Receptor, Interferon alpha-beta"¿¡ ´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: 2
  • ¿µ¹®
    ÇѱÛ
  • corpuscular receptor
    ¼Òü¼ö¿ëü
  • cell surface receptor
    ¼¼Æ÷Ç¥¸é¼ö¿ëü
  • cholinergic receptor
    Äݸ°¼ö¿ëü
  • distance receptor
    ¿ø°Ý¼ö¿ë±â
  • dominant receptor
    ¿ì¼º¼ö¿ëü
  • early receptor potential
    Á¶±â¼ö¿ëüÀüÀ§, Á¶±â½Ã°¢¼¼Æ÷ÀüÀ§
  • estrogen receptor
    ¿¡½ºÆ®·Î°Õ¼ö¿ëü
  • free receptor
    À¯¸®¼ö¿ëü
  • gustatory receptor
    ¹Ì°¢¼ö¿ë±â
  • H1 receptor
    H1¼ö¿ëü
  • H2 receptor
    H2¼ö¿ëü
  • heat receptor
    ¿­¼ö¿ë±â
  • hairy skin receptor
    ÅÐÇǺμö¿ë±â
  • histamine receptor
    È÷½ºÅ¸¹Î¼ö¿ëü
  • homing receptor
    ±Í¼Ò¼ö¿ëü
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • cold receptor
    ³Ã°¢¼ö¿ëü
  • complement receptor
    µµ¿òü¼ö¿ëü, º¸Ã¼¼ö¿ëü
  • corpuscular receptor
    ¼Òü¼ö¿ëü
  • receptor cell
    ¼ö¿ëü¼¼Æ÷
  • distance receptor
    (¢¡teleceptor) ¿ø°Ý¼ö¿ëü
  • dominant receptor
    ¿ì¼º¼ö¿ëü
  • early receptor potential
    Á¶±â½Ã°¢¼¼Æ÷ÀüÀ§
  • electromagnetic receptor
    ÀüÀÚ±â¼ö¿ëü
  • receptor destroying enzyme
    ¼ö¿ëüÆÄ±«È¿¼Ò
  • free receptor
    À¯¸®¼ö¿ëü
  • gustatory receptor
    ¹Ì°¢¼ö¿ëü
  • receptor gradient
    ¼ö¿ë´Ü¹é±â¿ï±â, ¼ö¿ë´Ü¹é°æ»ç
  • hairy skin receptor
    ÅÐÇǺμö¿ëü
  • heat receptor
    ¿­¼ö¿ëü
  • histamine receptor
    È÷½ºÅ¸¹Î¼ö¿ëü
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • T cell receptor gene
    T¼¼Æ÷[Ç׿ø]¼ö¿ëü À¯ÀüÀÚ
  • acetylcholine receptor
    ¾Æ¼¼Æ¿Äݸ° ¼ö¿ëü(¼ö¿ë±â, °¨¼ö±â)
  • acetylcholine receptor
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëü
  • acetylcholine receptor antibody
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëüÇ×ü
  • acetylcholine receptor antibody assay
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëü Ç×Ã¼ÃøÁ¤
  • alpha-adrenal receptor antagonist
    ¾ËÆÄ ¾Æµå·¹³¯¸°¼ö¿ëüÂ÷´ÜÁ¦
  • alpha-adrenergic receptor
    ¾ËÆÄ-¾Æµå·¹³¯¸°¼ö¿ëü.
  • alpha-adrenergic receptor
    ¾ËÆÄ¾Æµå·¹³¯¸°¼ö¿ëü
  • androgen receptor
    ³²¼ºÈ£¸£¸ó ¼ö¿ëü
  • antigen binding receptor
    Ç׿ø°áÇÕ¼ö¿ëü
  • antigen receptor
    Ç׿ø¼ö¿ëü.
  • homing receptor
    ±Í¼Ò¼ö¿ëü
  • immunoglobulin receptor
    ¸é¿ª±Û·ÎºÒ¸° ¼ö¿ëü
  • insulin receptor
    Àν¶¸°¼ö¿ëü(áôé»ô÷).
  • insulin receptor
    Àν¶¸°¼ö¿ëü.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • interferon-¥â (INF-¥â)
    º£Å¸ÀÎÅÍÆä·Ð
  • interferon-¥ã (INF-¥ã)
    °¨¸¶ÀÎÅÍÆä·Ð
  • acetylcholine receptor
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëü
  • acetylcholine receptor
    ¾Æ¼¼Æ¿Äݸ° ¼ö¿ëü(¼ö¿ë±â, °¨¼ö±â)
  • acetylcholine receptor antibody
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëüÇ×ü
  • acetylcholine receptor antibody assay
    ¾Æ¼¼Æ¿Äݸ°¼ö¿ëü Ç×Ã¼ÃøÁ¤
  • adrenergic receptor
    ¾Æµå·¹³¯¸°¼º ¼ö¿ëü(¼ö¿ë±â, °¨¼ö±â,°¨¼öü)
  • alpha-adrenal receptor antagonist
    ¾ËÆÄ ¾Æµå·¹³¯¸°¼ö¿ëüÂ÷´ÜÁ¦
  • alpha-adrenergic receptor
    ¾ËÆÄ-¾Æµå·¹³¯¸°¼ö¿ëü.
  • alpha-adrenergic receptor
    ¾ËÆÄ¾Æµå·¹³¯¸°¼ö¿ëü
  • androgen receptor
    ³²¼ºÈ£¸£¸ó ¼ö¿ëü
  • antigen binding receptor
    Ç׿ø°áÇÕ¼ö¿ëü
  • antigen receptor
    Ç׿ø¼ö¿ëü.
  • benzodiazepine receptor agonists(s)
    º¥Á¶´ÙÀ̾ÆÁ¦ÇÉ ¼ö¿ëü ÀÛ¿ëÁ¦
  • benzodiazepine receptor antagonist(s)
    º¥Á¶´ÙÀ̾ÆÁ¦ÇÉ ¼ö¿ëü ±æÇ×Á¦
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • ligand-receptor internalization
    ¸®°£µå-¼ö¿ëü(áôé»ô÷) ³»ÀÔ(Ò®ìý)
  • mineralocorticoid receptor
    ±¤Áú(ÎÎòõ) ÄÚ¸£Æ¼ÄÚÀÌµå ¼ö¿ëü(áôé»ô÷)
  • mobile receptor model
    À̵¿¼ö¿ëü(ì¹ÔÑáôé»ô÷) ¸ðµ¨
  • muscarinic receptor
    ¹«½ºÄ«¸°¼ö¿ëü(áôéÄô÷)
  • nicotinic receptor
    ´ÏÄÚÆ¾¼ö¿ëü(â¥é»ô÷)
  • opiate receptor
    ¾ÆÆíÁ¦(ð¥) ¼ö¿ëü(áôé»ô÷)
  • opioid receptor
    ¾ÆÆí°è(ͧ) ¾à¹°¼ö¿ëü(å·Úªáôé»ô÷)
  • receptor
    ¼ö¿ëü(áôé»ô÷)
  • receptor destroying enzyme
    ¼ö¿ëü ÆÄ±«È¿¼Ò(áôé»ô÷÷òÎÕý£áÈ)
  • receptor down regulation
    ¼ö¿ëü ÇÏÇâ Á¶Àý(áôé»ô÷ù»ú¾ðàï½)
  • receptor element
    ¼ö¿ëü Á¶Àý ¿ä¼Ò(áôé»ô÷ðàï½é©áÈ)
  • receptor gradient
    ¼ö¿ëü ±¸¹è(áôé»ô÷ÎþÛÕ)
  • receptor internalization
    ¼ö¿ëü ³»ÀÔ(áôé»ô÷Ò®ìý)
  • receptor-mediated endocytosis
    ¼ö¿ëü¸Å°³ ¼¼Æ÷³» ÀÌÀÔ(áôé»ô÷ØÚË¿á¬øàÒ®ì¹ìý)
  • ribosome receptor
    ¶óÀ̺¸¼Ø ¼ö¿ëü(áôé»ô÷)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
HFI hereditary fructose intolerance; human fibroblast interferon
HFIF human fibroblast interferon
HLBI human lymphoblastoid interferon
HLI human leukocyte interferon
HUIFM human leukocyte interferon meloy
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
alpha IFN Alpha interferon
IFN Alpha-2-interferon
IFN Anti-interferon
IFN-gamma Anti-interferon-gamma
beta-IFN Beta interferon
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • Fc receptor
    Fc ¼ö¿ëü
    Ç×üÀÇ Fc ºÐÀý°ú °áÇÕÇÏ´Â ¼¼Æ÷ Ç¥¸é ¼ö¿ëüÀ̸ç B ¼¼Æ÷, macro
  • free receptor
    À¯¸® ¼ö¿ëü
  • image receptor
    »ó ¼ö¿ë±â
  • k receptor
    k ¼ö¿ë±â
  • kapa receptor
    Ä«ÆÄ ¼ö¿ëü
  • ligand receptor binding
    ¸®°£µå ¼ö¿ë±â °áÇÕ
  • multiple somatic receptor
    ´Ù¹ß¼º ü ¼ö¿ëü, ´Ù¹ß¼º ü ¼ö¿ë±â
  • opiate analgesia receptor
    ¾ÆÆí¼º ÁøÅë ¼ö¿ëü, ¾ÆÆí¼º ÁøÅë ¼ö¿ë±â
  • opiate receptor
    ¾ÆÆí ¼ö¿ëü, ¾ÆÆí ¼ö¿ë±â
    1. ¥ì : ¥ì1Àº µ¿Åë Á¶Àý ¾àÁ¦°¡ °áÇÕ, ¥ì2¿Í °áÇսô ȣÈíÀÌ ¾ïÁ¦µÈ´Ù. 2. ¥ê¿Í °áÇÕ ½Ã Â÷ºÐÇØÁø´Ù. 3. ¥ä : ¸ö¿¡¼­ »ý¼ºµÇ´Â ³»Àμº o
  • peripheral receptor
    ¸»ÃÊ ¼ö¿ëü, ¸»ÃÊ ¼ö¿ë±â
  • pressure receptor
    ¾Ð¼ö¿ë±â, ¾Ð·Â¼ö¿ëü
    µ¿ÀǾî=
  • receptor
    ¼ö¿ë±â, ¼ö¿ëü, °¨¼öü
    1. ¼¼Æ÷Áú ³» ¶Ç´Â ¼¼Æ÷ Ç¥¸é¿¡ Á¸ÀçÇÏ´Â ºÐÀÚ ±¸Á¶·Î¼­
  • receptor activation
    ¼ö¿ëü Ȱ¼ºÈ­, ¼ö¿ë±â Ȱ¼ºÈ­
  • receptor blocking agent
    ¼ö¿ëü Â÷´ÜÁ¦
  • receptor complex
    ¼ö¿ëü º¹ÇÕü, ¼ö¿ë±â º¹ÇÕü
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
type II interferon <chemical> The major interferon produced by mitogenically or antigenically stimulated lymphocytes. It is structurally different from type I interferon (interferon type I) and its major activity is immunoregulation. It has been implicated in the expression of class II histocompatibility antigens in cells that do not normally produce them, leading to autoimmune disease.
Pharmacological action: antineoplastic agent, antiviral agents.
Chemical name: Interferon-gamma (human lymphocyte protein moiety reduced)
(12 Dec 1998)
type I interferon <chemical> Interferon secreted by leukocytes, fibroblasts, or lymphoblasts in response to viruses or interferon inducers other than mitogens, antigens, or allo-antigens. They include alpha- and beta-interferons (interferon-alpha and interferon-beta).
Pharmacological action: antineoplastic agent, antiviral agents.
(12 Dec 1998)
fibroblast interferon <cytokine> One of the type I interferons produced by fibroblasts in response to stimulation by live or inactivated virus or by double-stranded RNA. It is a cytokine with antiviral, antiproliferative, and immunomodulating activity.
Synonym: fibroblast interferon.
Pharmacological action: adjuvants, immunologic, antineoplastic agent, antiviral agents.
Chemical name: Interferon-alphaB (human leukocyte protein moiety reduced)
(12 Dec 1998)
leukocyte interferon <cytokine> One of the type I interferons produced by peripheral blood leukocytes or lymphoblastoid cells when exposed to live or inactivated virus, double-stranded RNA, or bacterial products.
It is the major interferon produced by virus-induced leukocyte cultures and, in addition to its pronounced antiviral activity, causes activation of NK cells. It is used experimentally in the treatment of hairy-cell leukaemia.
A number of different subtypes exist that are elaborated by leukocytes in response to viral infection or stimulation with double-stranded RNA; IFN-alpha-2A and -2B are protein products made by recombinant DNA techniques and are used as antineoplastic agents.
See: interferon-alpha 2a, interferon-alpha 2b
Synonym: leukocyte interferon.
Pharmacological action: antineoplastic agent, antiviral agent.
(20 Sep 2002)
acetylcholine receptor antibodies <neurology, investigation> A test used to measure the amount of antibodies to acetylcholine receptors on nerve endings. This is a diagnostic test for myasthenia gravis. A normal value is no antibodies in the bloodstream.
Acetylcholine receptor (AChR) binding autoantibodies (i.e. Antibodies reactive with several epitopes other than the binding site for acetylcholine or alpha-bungarotoxin) are present in approximately 88% of patients with generalised myasthenia gravis, 70% of ocular myasthenia and in approximately 80% of myasthenia gravis in remission.
Although serum concentrations of AChR binding autoantibodies do not in general correlate well with severity of weakness, there is typical decrease in concentration as weakness improves with immunosuppressive therapy.
AChR blocking autoantibodies (i.e., antibodies reactive with the AChR binding site) are present in about 50% of patients with myasthenia gravis, 30% with ocular myasthenia gravis and 20% of myasthenia gravis in remission, AChR blocking autoantibodies are the only AChR autoantibodies present in about 1% of myasthenia gravis.
AChR modulating autoantibodies (i.e., autoantibodies which cross-link AChRs and cause their removal from muscle membrane surfaces) are present in more than 90% of myasthenia gravis and occasionally are the only AchR autoantibodies detectable in mild, recent onset or ocular-restricted myasthenia gravis.
Results for AChR modulating autoantibodies can be transiently false-positive due to curare-like drugs used during general anesthesia. AChR autoantibodies of one or more types are found in at least 80% of ocular myasthenia gravis.
Although generally absent in neurological conditions other than myasthenia gravis(and consequently unlikely to cause confusion in neurodiagnosis), false-positive results for AChR autoantibodies occasionally occur in primary biliary cirrhosis, tardive dyskinesia, autoimmune thyroiditis, the elderly, amyotrophic lateral sclerosis patients treated with cobra venom and patients with thymoma in the absence of myasthenia gravis. Approximately 1% of patients with rheumatoid arthritis treated with D-penicillamine develop AChR autoantibodies and myasthenia gravis, both of which disappear when the drug is discontinued.
Babies born to ~10% of myasthenia gravis mothers have a transient neonatal form of myasthenia gravis that responds well to anticholinesterase therapy and usually remits within 1 month as maternal IgG disappears.
(29 Dec 1997)
amino acid receptor <biochemistry> Ligand gated ion channels with specific receptors for amino acid transmitters. An extended protein superfamily that also includes subunits of the nicotinic acetylcholine receptor.
(18 Nov 1997)
AMPA receptor <cell biology> Glutamate operated ion channel.
See: excitatory amino acid receptor channels.
(05 Feb 1998)
ANP receptor <molecular biology> Family of 3 receptors for atrial natriuretic peptide. ANP A and ANP B have intracellular guanylate cyclase and protein kinase like domains. ANP C, shares the extracellular ligand binding and transmembrane domains, but lacks the functional intracellular domains and is not thought to be involved in signal transduction.
(18 Nov 1997)
asialoglycoprotein receptor A surface receptor found in hepatocytes that binds galactose-terminal glycoproteins; thus, this receptor removes those proteins from circulation and they are in turn acted upon by hepatocyte lysosomes.
(05 Mar 2000)
auditory receptor cells Columnar cell's in the epithelium of the organ of Corti, having hairs (stereocilia) on their apical ends.
See: Corti's cells.
(05 Mar 2000)
beta-adrenergic receptor blocking agent A class of drugs that compete with beta-adrenergic agonists for available receptor sites; some compete for both b1 and b2 receptors (e.g., propranolol) while others are primarily either b1 (e.g., metoprolol) or b2 blockers; used in the treatment of a variety of cardiovascular diseases where beta-adrenergic blockade is desirable.
Synonym: beta-adrenergic receptor blocking agent, beta-adrenoreceptor antagonist, beta-blocker.
(05 Mar 2000)
beta-adrenergic receptor kinase <enzyme> Cyclic-AMP protein kinase which specifically phosphorylates the agonist-occupied form of beta-adrenergic receptor
Registry number: EC 2.7.1.-
Synonym: beta-ar kinase, beta-adrenergic receptor kinase 1, g-protein-coupled receptor kinase 2, grk2 (kinase), beta-adrenergic receptor kinase 2, beta-ar kinase 2
(26 Jun 1999)
cAMP receptor protein catabolite (gene) activator protein
GABA receptor <physiology> Ligand gated chloride ion channel forming receptor opened by gamma aminobutyric acid. Two distinct types: A and B.
A receptor: One of a family of neurotransmitter receptors with fast intrinsic ion channels that includes the glycine receptor and the nicotinic acetylcholine receptor. Distinct from another major receptor family, the muscarininc acetylcholine receptor and rhodopsin, with no intrinsic ion channel. The A receptor is specifically blocked by bicuculline. It consists of two pairs of protein chains forming an A2B2 complex, the A chains bind benzodiazepine and the B chains bind GABA. The 4 subunits are thought to form a tight group with the chloride channel in the middle. There is considerable similarity between the amino acid sequences of the receptor subunits and those of the nicotinic acetylcholine receptor suggesting that both receptors are derived from some evolutionary ancestor.
See: amino acid receptor superfamily.
B receptor: Brain receptor (80 kD) for the inhibitory neurotransmitter gamma amino butyric acid. Differs from the A receptor both in agonist specificity (baclofen is a specific agonist) and its effects on cells. It modulates intracellular calcium levels through a Go mediated effect on N type calcium channels and also lowers intracellular cAMP levels by an effect on adenylyl cyclase, thereby reducing the secretion of catecholamines.
(05 Jan 1998)
p60 tumour necrosis factor receptor-associated kinase <enzyme> Interacts with and causes phosphorylation of the cytoplasmic domain of the tnf receptor
Registry number: EC 2.7.10.-
Synonym: p60 tnf receptor-associated kinase, p60-trak
(26 Jun 1999)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • 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: 2
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
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: 2
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: 2
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
ÅëÇÕ°Ë»ö ¿Ï·á