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  • ¿µ¹®
    ÇѱÛ
  • heat receptor
    ¿­¼ö¿ë±â
  • hairy skin receptor
    ÅÐÇǺμö¿ë±â
  • histamine receptor
    È÷½ºÅ¸¹Î¼ö¿ëü
  • homing receptor
    ±Í¼Ò¼ö¿ëü
  • insulin receptor
    Àν¶¸°¼ö¿ëü
  • insulin receptor substrate-1
    Àν¶¸°¼ö¿ëü±âÁú-1
  • interferon receptor
    ÀÎÅÍÆä·Ð¼ö¿ëü
  • internalization receptor
    ³»ÀçÈ­¼ö¿ëü
  • joint receptor
    °üÀý¼ö¿ë±â
  • kinesthetic receptor
    ¿îµ¿°¨°¢¼ö¿ë±â
  • labyrinthine receptor
    ¹Ì·Î¼ö¿ë±â
  • muscarinic receptor
    ¹«½ºÄ«¸°¼ö¿ëü
  • neuromuscular receptor
    ½Å°æ±Ù(À°)¼ö¿ëü
  • nicotinic receptor
    ´ÏÄÚÆ¾¼ö¿ëü
  • olfactory receptor
    Èİ¢¼ö¿ë±â
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  • ¿µ¹®
    ÇѱÛ
  • 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
  • homing receptor
    ±Í¼Ò¼ö¿ëü
  • receptor hypothesis
    ¼ö¿ëü°¡¼³
  • insulin receptor
    Àν¶¸°¼ö¿ëü
  • interferon receptor
    ÀÎÅÍÆä·Ð¼ö¿ëü
  • internalization receptor
    ³»È­¼ö¿ëü
  • irritant receptor
    Àڱؼö¿ëü
  • receptor imaging
    ¼ö¿ëü¿µ»ó, ¼ö¿ëü¿µ»óÈ­
  • receptor internalization
    ¼ö¿ëü¼¼Æ÷³»À̵¿
  • receptor-ligand interaction
    ¼ö¿ëü¹èÀ§ÀÚ»óÈ£ÀÛ¿ë
  • joint receptor
    °üÀý¼ö¿ë±â
  • kinesthetic receptor
    ¿îµ¿°¨°¢¼ö¿ëü
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  • ¿µ¹®
    ÇѱÛ
  • immunoglobulin detection
    ¸é¿ª±Û·ÎºÒ¸°°ËÃâ
  • immunoglobulin domain
    ¸é¿ª±Û·ÎºÒ¸°¿µ¿ª.
  • immunoglobulin e(ige)
    ¸é¿ª±Û·ÎºÒ¸° E(Øó湡­)
  • immunoglobulin g(igg)
    ¸é¿ª±Û·ÎºÒ¸° G(Øó湡­)
  • immunoglobulin gene
    ¸é¿ª±Û·ÎºÒ¸°À¯ÀüÀÎÀÚ
  • immunoglobulin m(igm)
    ¸é¿ª±Û·ÎºÒ¸° M(Øó湡­)
  • immunoglobulin production
    ¸é¿ª±Û·ÎºÒ¸°»ý¼º<--»ý»ê>
  • immunoglobulin structure
    ¸é¿ª±Û·ÎºÒ¸° ±¸Á¶
  • immunoglobulin subclass
    ¸é¿ª±Û·ÎºÒ¸°¼­ºêŬ·¡½º.
  • immunoglobulin subgroup analysis
    ¸é¿ª±Û·ÎºÒ¸°¾ÆÇüºÐ¼®
  • immunoglobulin supergene family
    ¸é¿ª±Û·ÎºÒ¸° À¯ÀüÀÚÃʰŴëÁý´Ü
  • immunoglobulin, surface
    ¼¼Æ÷Ç¥¸é ¸é¿ª±Û·ÎºÒ¸°
  • immunoglobulin-coated erythrocyte
    ¸é¿ª±Û·ÎºÒ¸°ºÎÂøÀûÇ÷±¸
  • polyclonal immunoglobulin
    ´ÙŬ·Ð¼º¸é¿ª±Û·ÎºÒ¸°
  • radiolabeled immunoglobulin therapy
    ¹æ»ç¼ºÇ¥Áö¸é¿ª±Û·ÎºÒ¸°Ä¡·á
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  • ¿µ¹®
    ÇѱÛ
  • immunoglobulin production
    ¸é¿ª±Û·ÎºÒ¸°»ý¼º<--»ý»ê>
  • immunoglobulin structure
    ¸é¿ª±Û·ÎºÒ¸° ±¸Á¶
  • immunoglobulin subclass
    ¸é¿ª±Û·ÎºÒ¸°¼­ºêŬ·¡½º.
  • immunoglobulin subgroup analysis
    ¸é¿ª±Û·ÎºÒ¸°¾ÆÇüºÐ¼®
  • immunoglobulin supergene family
    ¸é¿ª±Û·ÎºÒ¸° À¯ÀüÀÚÃʰŴëÁý´Ü
  • immunoglobulin, surface
    ¼¼Æ÷Ç¥¸é ¸é¿ª±Û·ÎºÒ¸°
  • immunoglobulin-coated erythrocyte
    ¸é¿ª±Û·ÎºÒ¸°ºÎÂøÀûÇ÷±¸
  • isotype of immunoglobulin
    ¸é¿ª±Û·ÎºÒ¸°µ¿Á¾Çü
  • monoclonal immunoglobulin
    ´ÜÀÏŬ·Ð¸é¿ª±Û·ÎºÒ¸°
  • monoclonal immunoglobulin detection
    ´ÜÀÏŬ·Ð¸é¿ª±Û·ÎºÒ¸°°ËÃâ
  • monoclonal immunoglobulin disorders
    ´Ü(ÀÏ)Ŭ·Ð¼º ¸é¿ª±Û·ÎºÒ¸°ÀÌ»ó.
  • monoclonal immunoglobulin disorders
    ´Ü(ÀÏ)Ŭ·Ð¼º ¸é¿ª±Û·ÎºÒ¸°ÀÌ»ó.
  • monoclonal immunoglobulin disorders
    ´Ü(ÀÏ)Ŭ·Ð¼º ¸é¿ª±Û·ÎºÒ¸°ÀÌ»ó.
  • monoclonal immunoglobulin disorders
    ´Ü(ÀÏ)Ŭ·Ð¼º ¸é¿ª±Û·ÎºÒ¸°ÀÌ»ó.
  • polyclonal immunoglobulin
    ´ÙŬ·Ð¼º¸é¿ª±Û·ÎºÒ¸°
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  • ¿µ¹®
    ÇѱÛ
  • 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÷)
  • spare receptor
    ¿¹ºñ(çãÝá) ¼ö¿ëü (â¥é»ô÷)
  • SRP receptor
    SRP ¼ö¿ëü(áôé»ô÷)
  • steroid receptor
    ½ºÅ×·ÎÀÌµå ¼ö¿ëü (áôé»ô÷)
  • virus receptor
    ¹ÙÀÌ·¯½º ¼ö¿ëü (â¥é»ô÷)
  • volume receptor
    ¿ëÀû ¼ö¿ë±â(é»îÝáôé»Ðï)
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INSRR insulin receptor-related receptor
IRR insulin receptor-related receptor; intrarenal reflux
IRS immunoreactive secretion; infrared spectrophotometry; insulin receptor species; insulin receptor sub...
AH   1) Atrial Hypertrophy
  2) Anti-Hyaluronidase
  3) Amyloid imm...
AL Amyloid immunoglobulin Light chain protein
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IgAN Immunoglobulin A nephropathy
IgA1 Immunoglobulin A1
IBF Immunoglobulin Binding Factor
ICC Immunoglobulin Containing Cells
IgD Immunoglobulin D
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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
  • receptor destroying enzyme
    ¼ö¿ëü ÆÄ±« È¿¼Ò
    ¼ö¿ëü¸¦ ÆÄ±«ÇÏ¿© ÀûÇ÷±¸ÀÇ ¹ÙÀÌ·¯½º ¿ëÇ÷¿¡ ´ëÇÑ °¨¼ö¼ºÀ» ÀÒ¾î¹ö¸®°Ô ÇÏ´Â È¿¼Ò.
  • receptor potential
    ¼ö¿ë±â ÀüÀ§
    ÀÏÁ¤ÇÑ ¹°¸®È­ÇÐÀû Àڱؿ¡ ´ëÇÏ¿© ½Å°æ ´ÜÀ§ ¼ö¿ëü¿¡¼­ ¹ß»ýÇÏ´Â Å»ºÐ±Ø.
  • receptor site
    ¼ö¿ëü ºÎÀ§, ¼ö¿ëºÎ
    ƯÁ¤ÇÑ »ý¹°ÇÐÀû ¹ÝÀÀÀ» ÃÊ·¡ÇÏ´Â ºÐÀÚ °áÇÕÀÌ ÀϾ´Â ƯÁ¤ ºÎÀ§.
  • receptor theory
    ¼ö¿ë±â ÀÌ·Ð
    Ç×ü »ý¼º ¼¼Æ÷ÀÇ Ç¥¸é¿¡´Â ƯÁ¤ Ç×ü¿¡ »óÀÀÇÏ´Â Ç׿øÀÌ °áÇÕÇ϶ó ¼ö¿ëü°¡ Á¸ÀçÇÏ¸ç ±× ¼ö¿ëüÀÇ ±¸Á¶´Â Ç×üÀÇ ±¸Á¶¿Í °°´Ù´Â ÀÌ·Ð.
  • specific membrane receptor
    ƯÁ¤ ¸· ¼ö¿ë±â
  • specific opiate receptor site
    Ưº°ÇÑ ¾ÆÆí ¼ö¿ëºÎ
  • specific receptor
    ƯÀÌ ¼ö¿ëü, ƯÀÌ ¼ö¿ë±â
  • stretch receptor
    ½ÅÀå ¼ö¿ë±â
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
immunoglobulin isotypes The classes of immunoglobulins found in any species of animal. In man there are nine classes that migrate in five different groups in electrophoresis; they each consist of two light and two heavy protein chains, and each group has distinguishing structural and functional properties.
(12 Dec 1998)
immunoglobulin joining region Segment of light and heavy chains of mouse and human immunoglobulins where the genes for the variable region upstream join those of the constant region downstream (an important part of the antibody diversity mechanism). In the joining region of the light chain are the genes coding for amino acids 96 to 107.
(12 Dec 1998)
immunoglobulin M <immunology> An immunoglobulin M molecule (970 kD) is built up from five immunoglobulin G type monomers joined together, with the assistance of J chains, to form a cyclic pentamer.
Immunoglobulin M binds complement and a single molecule bound to a cell surface can lyse that cell. Immunoglobulin M is usually produced first in an immune response before immunoglobulin G.
The human red cell isoantibodies are immunoglobulin M antibodies. Heavy chain (mu chain) is rather larger than the heavy chains of other immunoglobulins.
(30 Mar 1998)
immunoglobulin superfamily <immunology> A large group of proteins with immunoglobulin like domains. most are involved with cell surface recognition events.
Sequence homologyy suggests that immunoglobulins, MHC molecules, some cell adhesion molecules and cytokines receptors share close homology and thus belong to a multigene family.
(30 Mar 1998)
immunoglobulin switch region Site on a segment of a B-cell immunoglobulin heavy-chain gene where recombination or rearrangement can occur, expressed as isotype or allotype switching, maturation of immune response, or recombination of DNA molecules. It is found on genes encoding all five immunoglobulin heavy chains.
(12 Dec 1998)
immunoglobulin variable region That region of the immunoglobulin (antibody) molecule that varies in its amino acid sequence and composition, confers the antigenic specificity, and is thought to comprise the binding site for the antigen. It is located at the n-terminus of the fab fragment of the immunoglobulin. It includes hypervariable and framework regions, vh family subgroups, and the complementarity-determining region.
(12 Dec 1998)
intravenous immunoglobulin <pharmacology> A sterile solution of concentrated antibodies extracted from healthy people. IVIG is used to prevent bacterial infections in people with low or inappropriate antibody production. Injected into a vein or muscle.
(09 Oct 1997)
tetanus immunoglobulin <protein> A protein antibody to tetanus toxin, given as passive immunity for those lacking any prior tetanus vaccination.
(27 Sep 1997)
thyroid stimulating immunoglobulin <protein> 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)
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)
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