¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Core Binding Factor beta Subunit"¿¡ ´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
  • olfactory binding protein
    Èİ¢°áÇմܹéÁú
  • orthodontic binding wire
    ±³Á¤¿ë¹­±âö»ç, ±³Á¤¿ë°áÂû¼±
  • protein binding
    ´Ü¹éÁú°áÇÕ
  • receptor binding
    ¼ö¿ëü°áÇÕ
  • sex hormone-binding globulin
    ¼ºÈ£¸£¸ó°áÇձ۷κҸ°
  • antihemophilic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÎÀÚ, Ç׎½ÄÀÎÀÚ
  • antiplatelet factor
    Ç×Ç÷¼ÒÆÇÀÎÀÚ
  • antirachitic factor
    Ç×±¸·çº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ³ªÆ®·ýÀÌ´¢ÀÎÀÚ, ½É¹æ¼ÒµãÀÌ´¢ÀÎÀÚ
  • activation factor
    Ȱ¼ºÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • activation factor
    Ȱ¼ºÀÎÀÚ
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ, ÇãÆÄ²Ê¸®Èñ¼®ÀÎÀÚ
  • amplification factor
    ÁõÆøÀÎÀÚ
  • antihemophlic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÛ¿ëÀÎÀÚ
  • antirachitic factor
    Ç×±¸·íº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ³ªÆ®·ýÀÌ´¢ÀÎÀÚ
  • colonizing factor antigen
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø
  • behavioral risk factor
    ÇൿÀ§Çè¿äÀÎ
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • Christmas factor
    Å©¸®½º¸¶½º ÀÎÀÚ(ì×í­)
  • Christmas factor.
    Å©¸®½º¸¶½ºÀÎÀÚ
  • D factor
    DÀÎÀÚ
  • Decay accelerating factor
    ºØ±«°¡¼Ó¿ä¼Ò(¿äÀÎ)
  • EDCF (endothlium-derived contracting factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ¼öÃàÀÎÀÚ(â¥õêì×í­)
  • EDRF (endothlium-derived relaxing factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ÀÌ¿ÏÀÎÀÚ(ì¬èÐì×í­)
  • EDRF=£¾endothelium derived relaxing factor
    ³»ÇǼ¼Æ÷¼ºÀÌ¿ÏÀÎÀÚ.
  • F factor
    FÀÎÀÚ
  • Factor IX
    IX ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor V
    V ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor VII
    VII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor VIII
    VIII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor X activated
    Ȱ¼ºÈ­(üÀàõûù)µÈ X ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor XI
    XI ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor XII
    XII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • binding site
    °á ÇÕºÎÀ§.
  • calcium-binding protein
    Ä®½· °áÇմܹé(Ì¿ùêÓ±ÛÜ)
  • cap binding protein
    ĸ°áÇմܹéÁú
  • cell growth,ligand receptor binding
    ¸®°£µå¼ö¿ë±â°áÇÕ (¡­áôé»ÐïÌ¿ùê)
  • cellular retinol-binding protein
    ¼¼Æ÷³» ·¹Æ¼³î °áÇմܹé
  • competitive protein binding radioassay
    °æÇÕÀû ´Ü¹é°áÇÕ¹æ»çºÐ¼®(¹ý)(¡­Ó±ÛÜ Ì¿ùêÛ¯ÞÒÝÂà°Ûö).
  • complement binding antibody
    º¸Ã¼°áÇÕÇ×ü(ÜÍô÷Ì¿ùêù÷ô÷).
  • corticosteroid binding globulin =CSG
    ÄÚ¸£Æ¼ÄÚ½ºÅ×·ÎÀ̵å°áÇÕ ±Û·ÎºÒ ¸°.
  • cortisol binding globulin
    ÄÚ¸£Æ¼¼Ö°áÇÕ±Û·Îºí¸°.
  • cortisol-binding globulin=transcortin
    ÄÚ¸£Æ¼¼Ö°áÇձ۷κҸ°=Æ®¶õ½ºÄÚ¸£Æ¾
  • cross binding
    ±³Â÷¿¬°á(±³Â÷¿¬°á).
  • human zona binding assay
    »ç¶÷Á¤ÀÚ Åõ¸í´ëºÎÂø°Ë»ç
  • iron binding capacity =IBC
    ö°áÇÕ´É(ôÑÌ¿ùêÒö).
  • iron binding protein =IBP
    ö°áÇÕ ´Ü¹éÁú.
  • iron-binding capacity
    ö°áÇÕ´É
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • beta ray
    º£Å¸¼±(àÊ)
  • beta ray spectrometer
    º£Å¸¼±(àÊ)ºÐ±¤°è(ÝÂÎÃͪ)
  • beta receptor
    º£Å¸ ¼ö¿ëü(áôé»ô÷)
  • beta sheet
    º£Å¸ ½¬Æ®
  • beta structure
    º£Å¸ ±¸Á¶(ϰðã)
  • beta threshold
    º£Å¸ ¹®ÅÎ
  • beta turn
    º£Å¸ µ¹ÀÌ
  • broad-beta lipoprotein
    ±¤´ë(ÎÆÓá) º£Å¸ÁöÁú´Ü¹éÁú(ò·òõÓ±ÛÜòõ)
  • floating beta lipoprotein
    ºÎÀ¯(Ý©ë´) º£Å¸ ÁöÁú´Ü¹éÁú(ò·òõÓ±ÛÜòõ)
  • pre-beta fraction
    ÇÁ·¹º£Å¸ºÐȹ(ÝÂüñ)
  • Q-beta
    Q º£Å¸.
  • Q-beta replicase
    Q º£Å¸ ¸®Çø®ÄÉÀ̽º
  • androgen-binding protein
    ¾Èµå·ÎÀü°áÇÕ(Ì¿ùê) ´Ü¹éÁú(Ó±ÛÜòõ)
  • antibody binding fraction
    Ç×ü°áÇÕºÐȹ (ù÷ô÷Ì¿ùêÝÂüò)
  • antigen binding capacity
    Ç׿ø °áÇÕ´É(ù÷ê«Ì¿ùêÒö)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
SU salicyluric acid; secretory unit; sensation unit; solar urticaria; sorbent unit; spectrophotometric ...
IBP insulin-like growth factor binding protein; International Biological Program; intra-aortic balloon p...
DF decapacitation factor; decontamination factor; deferoxamine; deficiency factor; defined flora [anima...
GRF gastrin-releasing factor; genetically related macrophage factor; gonadotropin-releasing factor; grow...
HSF heat shock factor; hepatocyte stimulatory factor; histamine sensitizing factor; human serum esterase...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
TGF beta Transforming Growth Factor Beta
TGF-beta 1 Transforming Growth Factor beta 1
TGF-beta 1 Transforming growth factor -beta
TGF-beta 1 Transforming growth factor beta type 1
TGF-beta RII Transforming growth factor beta type II receptor
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • hypothalamic beta-endorphin neuron
    ½Ã»ó ÇϺÎÀÇ º£Å¸-¿£µ¹ÇÉ ´º¿ì·±
  • absorbed dose conversion factor
    Èí¼ö¼±·® º¯È¯ °è¼ö
  • accessory food factor
    ¿µ¾ç º¸Á¶ ÀÎÀÚ
    F.G Ho
  • air kerma calibration factor
    °ø±â Ä¿¸¶ ÃøÁ¤ °è¼ö, ´«±Ý ¸ÂÃã °è¼ö
  • alveolar dilution factor
    ÆóÆ÷ Èñ¼® ÀÎÀÚ
  • angiogenesis factor
    Ç÷°ü Çü¼º ÀÎÀÚ
    ½Å»ý Ç÷°ü Áõ½ÄÀ» À¯µµÇÏ´Â ¹°Áú·Î¼­, Á¾¾çÀ̳ª ¸Á¸· °°Àº ½ÅÁø´ë»ç·®ÀÌ Å« Á¶Á÷¿¡¼­ ¹ß°ßµÈ´Ù. ÀÌ ÀÎÀÚ´Â »óóÀÇ °¡ÀåÀÚ¸®³ª Ç¥¸é¿¡ ÀÖ´Â Àú»ê¼Ò »óÅÂÀÇ ´ë½Ä¼¼Æ÷¿¡¼­ ºÐºñµÇ¸ç, »óó Ä¡À¯ °úÁ¤¿¡¼­ Ç÷°ü ÀçÇü¼ºÀ» À¯µµÇÑ´Ù.
  • anisotropy factor
    ºñµî¹æ¼º °è¼ö
  • antiangiogenesis factor
    Ç×Ç÷°ü»ý¼º ÀÎÀÚ
    Harvard ´ëÇп¡¼­ ¿¬±¸µÈ °ÍÀε¥ ¿¬°ñ¿¡´Â ¸ð¼¼Ç÷°üÀÌ Ä§ÅõµÇÁö ¾Ê´Â Çö»óÀ» °üÂûÇÏ°í ¾Ï Á¶Á÷¿¡ ¿¬°ñÁ¶Á÷¿¡¼­ À¯·¡µÈ antiangiogenesis factor¶ó´Â °ÍÀ» »ç¿ëÇÏ¿© ¾Ï Á¶Á÷ÀÇ ¼èÅ𸦠ÃÊ·¡ÇÏ¿´´Ù.
  • antihemophilic factor
    Ç×Ç÷¿ìº´ ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰 ÀÎÀÚ
  • antistiffness factor
    Ç×°­Á÷ ÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ¼º ³ªÆ®·ý ÀÌ´¢ ÀÎÀÚ
  • attenuation factor
    °¨¾à ¿ä¼Ò, °¨¼è ¿äÀÎ
  • B cell growth factor
    B ¼¼Æ÷ ¼ºÀå ÀÎÀÚ, B ¼¼Æ÷ Áõ½Ä ÀÎÀÚ
    B ¼¼Æ÷°¡ ÇüÁú ¼¼Æ÷·Î ºÐÈ­ÇÏ´Â °úÁ¤Àº Å©°Ô 2´Ü°è·Î ³ª´©¾îÁø´Ù. Ç׿ø ÀÚ±ØÀ» ¹ÞÀº B ¼¼Æ÷´Â ¿ì¼± Áõ½ÄÇϰí, ±× ÈÄ¿¡ Ç×ü¸¦ »ý»êÇÏ¿© ºÐºñÇÏ´Â ÇüÁú ¼¼Æ÷·Î ºÐÈ­¸¦ ¿Ï¼öÇÑ´Ù. Ç׿ø ÀÚ±ØÀ» ¹ÞÀº B ¼¼Æ÷´Â ±× ÀÚÁ¦¸¸À¸·Î´Â Áõ½ÄÇÏÁö ¸øÇϰí T¼¼Æ÷ À¯·¡ÀÇ B ¼¼Æ÷ Áõ½Ä ÀÎÀÚ³ª Ž½Ä ¼¼Æ÷ À¯·¡ ÀÎÀÚ IL-1ÀÇ ÀÚ±ØÀÌ Ãß°¡µÇ¾î Áõ½ÄÀ» ½ÃÀÛÇÑ´Ù. B ¼¼Æ÷ Áõ½Ä ÀÎÀÚ´Â Á¤»óÀÇ T¼¼Æ÷¸¦
  • B cell stimulating factor 1
    B ¼¼Æ÷ ÃËÁø ÀÎÀÚ 1
    µ¿ÀǾî´Â Interleukin 4·Î ¾Ë·ÁÁø ´ç´Ü¹éÀ¸·Î¼­ T ¼¼Æ÷, ºñ¸¸¼¼Æ÷ µî¿¡¼­ »ý»êµÈ´Ù. À̰ÍÀº B ¼¼Æ÷¿¡ ´ëÇØ comitogenÀ¸·Î ÀÛ¿ëÇϴµ¥ ±× ¿µÇâÀº B ¼¼Æ÷ÀÇ ¼º¼÷µµ¿¡ µû¶ó ´Ù¸£´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
receptors, transforming growth factor beta Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone).
(12 Dec 1998)
transforming growth factor beta Factor synthesised in a wide variety of tissues including platelets, placenta, and both normal and transformed cell lines. It acts synergistically with tgf-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. Tgf-beta also has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. There are at least three forms of tgf-beta: tgf-beta1, tgf-beta2, and tgf-beta1.2. The latter is a heterodimer made up of both tgf-beta1 and tgf-beta2.
(12 Dec 1998)
tumour necrosis factor-beta <cytokine> A cytolytic factor that is produced by CD4 and CD8 T-cells after their exposure to an antigen.
(05 Mar 2000)
androgen binding protein A protein secreted by testicular Sertoli cells along with inhibin and mullerian inhibiting substance. Androgen binding protein probably maintains a high concentration of androgen in the seminiferous tubules.
(05 Mar 2000)
androgen-binding proteins Carrier proteins produced in the sertoli cells of the testis, secreted into the seminiferous tubules, and transported via the efferent ducts to the epididymis. Participate in the transport of androgens; include also synthetic androgens binding proteins.
(12 Dec 1998)
antigen-binding site <immunology> In immune network theory, an idiotope, an antigenic site of an antibody that is responsible for that antibody binding to an antigenic determinant (epitope).
Also used of the site on a ligand molecule to which a cell surface receptor binds.
(18 Nov 1997)
binding <biochemistry, chemistry, molecular biology> The adherence of molecules to one another, for example, enzymes to substrates, antibodies to antigens, DNA strands to their complementary strands.
Binding occurs because the shape and chemical natures of parts of the molecules surfaces are complementary. A common metaphor is the "lock-and-key," used to describe how enzymes fit around their substrate.
(14 Nov 1997)
binding constant <chemistry> Reciprocal of dissociation constant. A measure of the extent of a reversible association between two molecular species at equilibrium.
(18 Nov 1997)
binding energy <chemistry, radiobiology> The binding energy of a nucleus is the minimum energy required to dissociate it into its component neutrons and protons. Neutron or proton binding energies are those required to remove a neutron or proton, respectively, from a nucleus. Electron binding energy is that required to remove an electron from an atom or a molecule.
(16 Dec 1997)
binding sites The reactive parts of a macromolecule that directly participate in its specific combination with another molecule.
(12 Dec 1998)
binding sites, antibody Local surface sites on antibodies which react with antigen determinant sites on antigens. They are formed from parts of the variable regions of the fab fragment of the immunoglobulin.
(12 Dec 1998)
calcium-binding protein <biochemistry> There are two main groups of calcium binding proteins, those that are similar to calmodulin and are called EF hand proteins and those that bind calcium and phospholipid (e.g. Lipocortin) and that have been grouped under the generic name of annexins.
Many other proteins will bind calcium, although the binding site usually has considerable homology with the calcium-binding domains of calmodulin. They can act as transport proteins, regulator proteins or activator proteins.
There is also a vitamin D-dependent variant which is a protein that plays a fundamental role in the vitamin d mediated transport of calcium in reptiles, amphibians, birds and mammals. It is found in the intestine, kidneys, egg shell gland, brain, and possibly other organs. Its molecular weight is species dependent.
(12 May 2002)
calmodulin-binding proteins Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including f-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium atpases.
(12 Dec 1998)
cap binding protein <molecular biology, protein> Protein (24 kD) with affinity for cap structure at 5' end of mRNA that probably assists, together with other initiation factors, in binding the mRNA to the 40S ribosomal subunit. Translation of mRNA in vitro is faster if it has a cap binding protein.
(18 Nov 1997)
galactose binding protein <protein> A bacterial periplasmic protein, most studied in E. Coli, that acts both as a sensory element in the detection of galactose as a chemotactic signal and in the uptake of the sugar.
(18 Nov 1997)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • prime factor
    ¼ÒÀμö
  • releasing factor
    È£¸£¸ó ¹æÃâÀÎÀÚ
  • rheumatoid factor
    ·ù¸ÓƼÁòÀÎÀÚ(¸¸¼º °üÀý ·ù¸ÓƼÁò ȯÀÚÀÇ ÀÚ±â Ç×ü)
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
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 4
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 4
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: 4
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: 4
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 4
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 4
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 4
ÅëÇÕ°Ë»ö ¿Ï·á