¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Diazepam Binding Inhibitor"¿¡ ´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: 4
  • ¿µ¹®
    ÇѱÛ
  • sex hormone-binding globulin
    ¼ºÈ£¸£¸ó°áÇÕ±Û·Îºí¸°
  • sex-hormone binding globulin
  • testosterone-binding globulin
    Å×½ºÅ佺Å×·Ð °áÇմܹé
  • thyroid-binding globulin
  • thyroxin binding globulin
    Ƽ·Ï½Å°áÇձ۷κҸ°.
  • thyroxin binding prealbumin
    Ƽ·Ï½Å°áÇÕÇÁ¸®¾ËºÎ¹Î.
  • thyroxin binding protein
    Ƽ·Ï½Å°áÇմܹéÁú(¡­Ì¿ùêÓ±ÛÜòõ).
  • thyroxine -binding globulin
    Ƽ·Ï½Å°áÇÕ±Û·Îºí¸°
  • thyroxine-binding prealbumin
    Ƽ·Ï½Å°áÇÕÇÁ¸®¾ËºÎ¹Î
  • total iron binding capacity
    ÃÑö°áÇÕ´É
  • total iron binding capacity=TIBC
    ÃÑö°áÇÕ´É
  • unsaturated iron binding capacity
    ºÒÆ÷ȭö°áÇÕ´É(¡­ôÑÌ¿ùêÒö).
  • unsaturated iron binding capacity
    ºÒÆ÷ȭö°áÇÕ´É
  • unsaturated vitamin B12 binding capacity
    ºÒÆ÷È­ºñŸ¹Î B12 °áÇÕ´É
  • acetylcholinesterase inhibitor
    ¾Æ¼¼Æ®Äݸ°¿¡½ºÅÍ·¹À̽º<¿¡½ºÅ×¶óÁ¦> ¾ïÁ¦Á¦.
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
  • ¿µ¹®
    ÇѱÛ
  • iron-binding globulin
    ö°áÇÕ(ôÑÌ¿ùê) ±Û·Îºí¸°
  • latent iron-binding capacity
    ÀáÀçö°áÇÕ´É(íÖî¤ôÑÌ¿ùêÒö)
  • macroscopic binding constant
    °Å½Ã °áÇÕ»ó¼ö(ËÝãÊÌ¿ùêßÈâ¦)
  • microscopic binding constant
    ¹Ì½Ã°áÇÕ»ó¼ö(Ú°ãÊÌ¿ùêßÈâ¦)
  • mononucleotide binding domain
    ¸ð³ë´©Å¬·¹¿ÀŸÀÌµå °áÇÕ¿µ¿ª(Ì¿ùêÖÅæ´)
  • multiple binding
    ´ÙÁß°áÇÕ(ÒýñëÌ¿ùê)
  • nonexclusive binding
    ºñ¹èŸ°áÇÕ(ÞªÛÉöâÌ¿ùê)
  • nonexclusive binding coefficient
    ºñ¹èŸ°áÇÕ»ó¼ö(ÞªÛÉöâÌ¿ùêßÈâ¦)
  • nucleotide-binding domain
    ´©Å¬¸®¿ÀŸÀÌµå °áÇÕ¿µ¿ª(Ì¿ùêÖÅæ´)
  • retinol-binding protein
    ·¹Æ¼³î °áÇÕ ´Ü¹éÁú(Ì¿ùêÓ±ÛÜòõ)
  • ribosome binding site
    ¶óÀ̺¸¼Ø °áÇÕ(Ì¿ùê)ÀÚ¸®
  • ribosome binding technique
    ¶óÀ̺¸¼Ø °áÇÕ¼ú(Ì¿ùêâú)
  • sex hormoe binding globulin
    ¼º(àõ)È£¸£¸ó °áÇÕ(Ì¿ùê)±Û·ÎºÒ¸°
  • sex steroid binding plasma protein
    ¼º(àõ)½ºÅ×·ÎÀÌµå °áÇÕ(Ì¿ùê) Ç÷Àå(úìíì) ´Ü¹éÁú(úìíìÓ±ÛÜòõ)
  • single-strand binding protein
    ¿Ü°¡´Ú °áÇմܹéÁú(Ì¿ùêÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
IBP insulin-like growth factor binding protein; International Biological Program; intra-aortic balloon p...
MBP major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl...
PBP penicillin-binding protein; porphyrin biosynthesis pathway; prostate-binding protein; pseudobulbar p...
RBP retinol-binding protein; riboflavin-binding protein
SBP schizobipolar; serotonin-binding protein; spontaneous bacterial peritonitis; steroid-binding plasma ...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
PIC 2-plasmin inhibitor plasmin complex
ACE-I ACE inhibitor
ACPI Acid cysteine proteinase inhibitor
ARI aldose reductase inhibitor
alpha 1Pi Alpha 1-protease inhibitor
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
trypsin inhibitor, kazal pancreatic <chemical> A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the kunitz bovine pancreatic trypsin inhibitor (aprotinin).
Chemical name: Trypsin inhibitor, pancreatic secretory
(12 Dec 1998)
trypsin inhibitor, kunitz soybean <chemical> A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
Pharmacological action: trypsin inhibitors.
Chemical name: Trypsin inhibitor, Kunitz soybean
(12 Dec 1998)
familial lipoprotein lipase inhibitor An inhibitor found in certain individuals that inhibits lipoprotein lipase resulting in accumulation of chylomicrons, VLDL, and triacylglycerols; similar in symptoms to familial lipoprotein lipase deficiency.
(05 Mar 2000)
lipoprotein-associated coagulation inhibitor Formerly known as anticonvertin; a protein that inhibits the extrinsic pathway of coagulation by binding to the tissue factor III-factor VII-Calcium-factor Xa complex.
(05 Mar 2000)
lupus coagulation inhibitor An antiphospholipid antibody found in association with systemic lupus erythematosus (lupus erythematosus, systemic), antiphospholipid syndrome, and in a variety of other diseases as well as in healthy individuals. In vitro, the antibody interferes with the conversion of prothrombin to thrombin and prolongs the partial thromboplastin time. In vivo, it exerts a procoagulant effect resulting in thrombosis mainly in the larger veins and arteries. It further causes obstetrical complications, including foetal death and spontaneous abortion, as well as a variety of haematologic and neurologic complications.
(12 Dec 1998)
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)
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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °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
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °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