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"Bone Morphogenetic Protein Receptors, Type II"¿¡ ´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: 9
  • ¿µ¹®
    ÇѱÛ
  • bone deposition
    »ÀÄ§Âø, °ñÄ§Âø
  • bone dislocation
    °ñÀüÀ§, »À¾î±ß³²
  • bone drill
    »Àõ°ø±â
  • bone fragment
    »ÄÁ¶°¢, °ñÆí
  • bone fragmentation
    »ÄÁ¶°¢Çü¼º, °ñÆíÇü¼º
  • bone graft
    »ÀÀ̽Ä, °ñÀ̽Ä
  • bone hook
    »À°¥°í¸®
  • bone inlay
    »À¼Ó³Ö±â, °ñ³»Àç
  • bone knife
    »ÀÄ®, °ñµµ
  • bone marrow
    °ñ¼ö, »À¼ÓÁú
  • bone marrow biopsy
    °ñ¼ö»ý°Ë
  • bone marrow blood
    °ñ¼öÇ÷¾×
  • bone marrow depression
    °ñ¼ö¾ïÁ¦
  • bone marrow needle
    °ñ¼ö¹Ù´Ã
  • bone marrow transplantation
    °ñ¼öÀ̽Ä(¼ú)
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • bone dislocation
    °ñÀüÀ§, °ñÀÌÅ», »À¾î±ß³²
  • bone drill
    »Àõ°ø±â
  • bone fragment
    »ÀÁ¶°¢, °ñÆí
  • bone fragmentation
    »ÀÁ¶°¢Çü¼º, °ñÆíÇü¼º
  • bone graft
    »ÀÀ̽Ä, °ñÀ̽Ä
  • bone hook
    »À°¥°í¸®
  • bone inlay
    »À¼Ó³Ö±â, °ñ³»Àç
  • bone knife
    »ÀÄ®, °ñµµ
  • bone marrow
    »À¼ÓÁú, °ñ¼ö
  • bone matrix
    »À¹ÙÅÁÁú
  • bone onlay
    (¢¡onlay bone graft) ¾ñ±â»ÀÀ̽Ä, Áßø°ñÀ̽Ä
  • bone pain
    »ÀÅëÁõ
  • bone peg
    »À¸ø, °ñÁ¤
  • bone resorption
    »ÀÈí¼ö
  • bone saw
    »ÀÅé
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • hip bone
    °ü°ñ(ΰÍé), µÐ°ñ(ÔëÍé), °í°ñ(ÍÆÍé), °ñ¹Ý°ñ(ÍéÚïÍé), ¹«¸í°ñ(ÙíÙ£Íé), ¾ûÄ¡»À.
  • horn of hyoid bone
    ¼³°ñ»Ô, »ó°¢(ß¾ÊÇ).
  • hyoid bone
    ¼³°ñ.
  • hyoid bone
    ¸ñ»Ô»À ¼³°ñ
  • hyoid bone
    ¼³°ñ
  • iliac bone <³ª> os ilium
    Àå°ñ(Àå°ñ).
  • iliac bone ³ª os ilium
    Àå°ñ(íóÍé).
  • immature compact bone
    ¹Ì¼º¼÷Ä¡¹Ð»À
  • incisive bone
    (¾Õ´Ï»À)
  • incisive bone premaxilla ; os incisivum ³ª
    ¾Õ´Ï°ñ, ÀýÄ¡°ñ(ôîöÍÍé).
  • inferior body of hyoid bone
    ¸ñ»Ô»À¾Æ·¡¸öÅë
  • inlay bone graft
    ³»Àç °ñ À̽Ä(Ò®î¤Íéì¹ãÕ), °¨ÀÔ °ñ À̽Ä(ÊîìýÍéì¹ãÕ).
  • innominate bone ³ª os coxae
    °ü°ñ.
  • innominate bone ³ª os coxae
    ¹«¸í°ñ(ÙíÙ£Íé), µÐ°ñ(ÔëÍé), °ñ¹Ý°ñ(ÍéÚïÍé), ¾ûÄ¡ »À, °ü°ñ.
  • petrosal cartilage of temporal bone
    °üÀÚ»À¹ÙÀ§¿¬°ñ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • protein 4.1
    ´Ü¹é 4.1
  • protein A
    ´Ü¹éÁú A (Æ÷µµ±¸±ÕÀÇ)
  • protein C
    C ´Ü¹é
  • protein S
    S ´Ü¹é
  • protein binding
    (Ç÷Àå)´Ü¹é°áÇÕ.
  • protein binding
    ´Ü¹éÁú °áÇÕ
  • protein bound iodine
    ´Ü¹éÁú°áÇÕ¿ä¿Àµå
  • protein bound iodine =PBI
    ´Ü¹éÁú°áÇÕ¿ä¿Àµå.
  • protein c
    ´Ü¹é C
  • protein calorie malnutrition
    ´Ü¹é¿­·®¿µ¾ç ½ÇÁ¶.
  • protein calorie malnutrition
    ´Ü¹é¿­·®¿µ¾ç ½ÇÁ¶(Ó±ÛÜæðÕáç½å× ã÷ðà)
  • protein decomposition
    ´Ü¹éºÐÇØ(Ó±ÛÜÝÂú°).
  • protein digest
    ´Ü¹é¼ÒÈ­¹°(Ó±ÛÜá¼ûùÚª).
  • protein error
    ´Ü¹é¿ÀÂ÷(Ó±ÛÜè¦ó¬).
  • protein extract
    ´Ü¹éÁúÃßÃâ¹°.
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • Histogenesis of bone
    »ÀÁ¶Á÷¹ß»ý
    [¿¾ ¿ë¾î] °ñ¹ß»ý
  • Reticulofibrous bone tissue
    ¼¼¸Á¼¶À¯»ÀÁ¶Á÷
    [¿¾ ¿ë¾î] ¼¼¸Á¼¶À¯¼º°ñÁ¶Á÷
  • Cuboid bone
    ÀÔ¹æ»À
    [¿¾ ¿ë¾î] ÀÔ¹æ°ñ
  • Tuberosity of cuboid bone
    ÀÔ¹æ»À°ÅÄ£¸é
    [¿¾ ¿ë¾î] ÀÔ¹æ°ñÁ¶¸é
  • Pisiform bone
    Äá¾Ë»À
    [¿¾ ¿ë¾î] µÎ»ó°ñ
  • Long bone
    ±ä»À
    [¿¾ ¿ë¾î] Àå°ñ
  • Short bone
    ªÀº»À
    [¿¾ ¿ë¾î] ´Ü°ñ
  • Sponge bone
    ÇØ¸é»À
    [¿¾ ¿ë¾î] ÇØ¸é°ñ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • iron-sulfur protein
    ö-À¯È² ´Ü¹éÁú(ôÑ×¼üÜÓ±ÛÜòõ)
  • isoelectric protein
    µîÀü´Ü¹éÁú(Ôõï³Ó±ÛÜòõ)
  • isoionic protein
    µî(Ôõ)À̿ ´Ü¹éÁú(Ó±ÛÜòõ)
  • late protein
    ¸¸±â´Ü¹éÁú(عѢӱÛÜòõ)
  • leader protein
    ¼±µµ´Ü¹éÁú(à»ÓôÓ±ÛÜòõ)
  • leaky protein
    ´©Ãâ´Ü¹éÁú(שõóÓ±ÛÜòõ)
  • LETS protein
    LETS ´Ü¹éÁú(Ó±ÛÜòõ)
  • light-harvesting Chl a/b protein
    Áý±¤¼º¿±·Ïü(ó¢ÎÃàõç¨Öàô÷) a/b ´Ü¹éÁú(Ó±ÛÜòõ)
  • link protein
    ¿¬°á´Ü¹éÁú(֧̿ӱÛÜòõ)
  • lipid-globular protein mosaic model
    "ÁöÁú-±¸»ó´Ü¹éÁú(ò·òõϹßÒÓ±ÛÜòõ) , ¸ðÀÚÀÌÅ©¸ðµ¨"
  • liquid protein diet
    ¾×ü´Ü¹éÁú½Ä(äûô÷Ó±ÛÜòõãÝ)
  • low-potential iron protein
    ÀúÀüÀ§ ö´Ü¹éÁú(î¸ï³êÈôÑÓ±ÛÜòõ)
  • low-quality protein
    ÀúÁú´Ü¹éÁú(î¸òõÓ±ÛÜòõ)
  • matrix protein
    ±âÁú´Ü¹éÁú(ѨòõÓ±ÛÜòõ)
  • maturation protein
    ¼º¼÷´Ü¹éÁú(à÷âÙÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
ABMI autologous bone marrow transplantation
ABMT American Board of Medical Toxicology; autologous bone marrow transplantation
AC/BC air conduction/bone conduction [time ratio]
ADR activation, depression, repetition [in bone remodeling]; adrenodoxin reductase; Adriamycin; adverse ...
ANB avascular necrosis of bone
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
TNFRs TNF receptors
TR Thyroid Hormone Receptors
VEGFR Vascular Endothelial Growth Factor Receptors
beta 2R beta 2-Adrenergic receptors
PRc progesterone receptors
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone and joint surgery
    °ñ°üÀý ¿Ü°ú
  • bone ash
    °ñȸ
    »À¸¦ Å¿ö¼­ ¸¸µç °¡·ç, ºñ·á¿¡ ¾²À̱⵵ ÇÑ´Ù.
  • bone augmentation
    °ñ Áõ´ë¼ú
  • bone blend
    °ñ È¥ÇÕ
  • bone cell
    °ñ ¼¼Æ÷
    °ñÁ¶Á÷ÀÇ ±âº» ¼¼Æ÷. °ñ Á¶Á÷¿¡´Â µüµüÇÑ °ñ ±âÁú¾È¿¡ °ñ¼Ò°­À̶ó°í ÇÏ´Â Æ´ÀÌ ±ºµ¥±ºµ¥ ÀÖ°í, ±× ¼Ó¿¡ 1°³¾¿ÀÇ °ñ ¼¼Æ÷°¡ µé¾î ÀÖ´Ù. °ñ ¼¼Æ÷ÀÇ ÇüÅ´ °ñ¼Ò°­°ú ÀÏÄ¡ÇÏ¿© ÆíÆòÇÑ Å¸¿øÇüÀ¸·Î, ±æÀÌ´Â 15¡­27 ¥ìmÀÌ´Ù. °ñ ¼¼Æ÷´Â ´Ù¼öÀÇ °¡´Â ¿øÇüÁú µ¹±â°¡ À־, À̰ÍÀÌ ±âÁú ³»ÀÇ °ñ ¼¼°üÀ» ÅëÇÏ¿© °¡±îÀÌ ÀÖ´Â °ñ ¼¼Æ÷ÀÇ µ¹±â¿Í ÇÕÄ£´Ù. °ñ ¼¼Æ÷´Â º»·¡ °áÇÕÁ¶Á÷ÀÇ ¼¶À¯¾Æ¼¼Æ÷¿¡¼­ Çü¼ºµÇ´Â °ÍÀ¸·Î, ¸ÕÀú °ñ¾Æ¼¼Æ÷°¡ µÇ¾î, À̰ÍÀÌ ±âÁúÀ» ¸¸µé°í ÀÚ½ÅÀº ±× ±âÁú ¼Ó¿¡ µé¾î°¡ °ñ¼¼Æ÷·Î µÈ´Ù. À̰ÍÀº °ñ Á¶Á÷ÀÇ Á¦Á¶ÀÚÀ̸ç, ¼¼Æ÷ÁúÀº ¹Ì·®ÀÇ ¹ÌÅäÄܵ帮¾Æ¸¦ Æ÷ÇÔÇϰí, È£¾à¿°±â¼ºÀ» ³ªÅ¸³½´Ù.
  • bone chisel
    »À ²ø
  • bone conduction test
    °ñÀüµµ ½ÃÇè
  • bone curette
    °ñÅ¥·¿, °ñ ¼ÒÆÄ
  • bone cyst
    °ñ ³¶
  • bone density
    °ñ ¹Ðµµ
  • bone disease
    °ñ Áúȯ
    µ¿ÀǾî=osteo
  • bone dislocation
    °ñ ÀüÀÌ, °ñ ÀüÀ§
  • bone factor
    °ñ ÀÎÀÚ
    Ȱ¼ºÀ̳ª ÀÚÁï¿¡ ´ëÇÑ Ä¡Á¶°ñÀÇ »ó´ë ¹ÝÀÀ.
  • bone file
    ¿Ü°ú¿ë ÁÙ
  • bone forcep
    °ñ °âÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
receptors, neurokinin-2 A class of cell surface receptors for tachykinins that prefers neurokinin a (nka, substance k, neurokinin alpha, neuromedin l), neuropeptide k (npk), or neuropeptide gamma over other tachykinins. Neurokinin-2 (nk-2) receptors have been cloned and are similar to other g-protein coupled receptors.
(12 Dec 1998)
receptors, neurokinin-3 A class of cell surface receptors for tachykinins that prefers neurokinin b (neurokinin beta, neuromedin k) over other tachykinins. Neurokinin-3 (nk-3) receptors have been cloned and are members of the g-protein coupled receptor superfamily. They have been found in the central nervous system and in peripheral tissues.
(12 Dec 1998)
receptors, neuropeptide Cell surface receptors that bind specific neuropeptides with high affinity and trigger intracellular changes influencing the behaviour of cells. Many neuropeptides are also hormones outside of the nervous system.
(12 Dec 1998)
receptors, neuropeptide y Cell surface proteins that bind neuropeptide y with high affinity and trigger intracellular changes which influence the behaviour of cells.
(12 Dec 1998)
receptors, neurotensin Cell surface proteins that bind neurotensin with high affinity and trigger intracellular changes which influence the behaviour of cells. Neurotensin and neurotensin receptors are found in the central nervous system and in the periphery.
(12 Dec 1998)
receptors, neurotransmitter Cell surface receptors that bind signalling molecules released by neurons and convert these signals into intracellular changes influencing the behaviour of cells. Neurotransmitter is used here in its most general sense, including not only messengers that act to regulate ion channels, but also those which act on second messenger systems and those which may act at a distance from their release sites. Included are receptors for neuromodulators, neuroregulators, neuromediators, and neurohumors, whether or not located at synapses.
(12 Dec 1998)
receptors, nicotinic One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for nicotine over muscarine. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, molecular biology, and biophysical properties of the channels.
(12 Dec 1998)
receptors, n-methyl-d-aspartate A class of ionotropic glutamate receptors characterised by affinity for n-methyl-d-aspartate. Nmda receptors have an allosteric binding site for glycine which must be occupied for the channel to open efficiently and a site within the channel itself to which magnesium ions bind in a voltage-dependent manner. The positive voltage dependence of channel conductance and the high permeability of the conducting channel to calcium ions (as well as to monovalent cations) are important in excitotoxicity and neuronal plasticity.
(12 Dec 1998)
receptors, odourant Proteins, usually projecting from the cilia of olfactory receptor neurons, that specifically bind odourant molecules and trigger responses in the neurons. The large number of different odourant receptors appears to arise from several gene families or subfamilies rather than from DNA rearrangement.
(12 Dec 1998)
receptors, opioid Cell membrane proteins that bind opioids and trigger intracellular changes which influence the behaviour of cells. The endogenous ligands for opioid receptors in mammals include three families of peptides, the enkephalins, endorphins, and dynorphins. The receptor classes include mu, delta, and kappa receptors. Sigma receptors bind several psychoactive substances, including certain opioids, but their endogenous ligands are not known.
(12 Dec 1998)
receptors, opioid, delta A class of opioid receptors recognised by its pharmacological profile. Delta opioid receptors bind endorphins and enkephalins with approximately equal affinity and have less affinity for dynorphins.
(12 Dec 1998)
receptors, opioid, kappa A class of opioid receptors recognised by its pharmacological profile. Kappa opioid receptors bind dynorphins with a higher affinity than endorphins which are themselves preferred to enkephalins.
(12 Dec 1998)
receptors, opioid, mu A class of opioid receptors recognised by its pharmacological profile. Mu opioid receptors bind, in decreasing order of affinity, endorphins, dynorphins, met-enkephalin, and leu-enkephalin. They have also been shown to be molecular receptors for morphine.
(12 Dec 1998)
receptors, oxytocin Cell surface proteins that bind oxytocin with high affinity and trigger intracellular changes which influence the behaviour of cells. Oxytocin receptors in the uterus and the mammary glands mediate the hormone's stimulation of contraction and milk ejection. The presence of oxytocin and oxytocin receptors in neurons of the brain probably reflects an additional role as a neurotransmitter.
(12 Dec 1998)
receptors, pancreatic hormone Cell surface proteins that bind pancreatic hormones with high affinity and trigger intracellular changes which influence the behaviour of cells. These include receptors for glucagon (secreted by alpha cells), insulin (secreted by beta cells), somatostatin (secreted by delta cells), and pancreatic peptide (secreted by pp cells). Some of these hormones and receptors also support neurotransmission.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ±¸ºÐ/º¸Çè±Þ¿©
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    ÇѱÛ
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    ÇѱÛ
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    ÇѱÛ
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KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
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CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 9
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 9
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 9
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