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"fatty acid binding protein"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • oleic acid
    ¿Ã·¹»ê
  • organic acid
    À¯±â»ê
  • orotic acid
    ¿À·ÎÆ®»ê
  • oxalic acid
    ¿Á»ì»ê
  • oxaloacetic acid
    ¿Á»ì¾Æ¼¼Æ®»ê
  • phenolic acid
    Æä³î»ê
  • phenolsulfuric acid
    Æä³îȲ»ê
  • phenylpyruvic acid
    Æä´ÒÇÇ·çºê»ê
  • phosphopyruvic acid
    Æ÷½ºÆ÷ÇÇ·çºê»ê
  • phosphoric acid
    Àλê
  • phosphorus acid
    ¾ÆÀλê
  • p-aminobenzoic acid
    ÆÄ¶ó¾Æ¹Ì³ëº¥Á¶»ê
  • p-aminosalicylic acid
    ÆÄ¶ó¾Æ¹Ì³ë»ì¸®½Ç»ê
  • phytanic acid storage disease
    ÇÇź»êÃàÀûº´
  • picramic acid
    ÇÇÅ©¶÷»ê
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 16
  • ¿µ¹®
    ÇѱÛ
  • nucleic acid hybridization
    ÇÙ»êºÎÇÕÈ­
  • uric acid infarct
    ¿ä»ê°æ»ö
  • nucleic acid probe
    ÇÙ»ê´õµëÀÚ
  • uric acid nephropathy
    (¢¡urate nephropathy) ¿ä»ê¿°ÄáÆÏº´Áõ
  • periodic acid-Schiff stain
    ÇÇ¿¡ÀÌ¿¡½º¿°»ö
  • uric acid stone
    ¿ä»êµ¹
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  • ¿µ¹®
    ÇѱÛ
  • gastric acid secretion
    À§(êÖ)(¾×(äû))»êºÐºñ(ß«ÝÂÝô).
  • gastric acid secretory studies
    À§»êºÐºñ °Ë»ç.
  • general acid
    ÀϹݻê(ìéÚõß«).
  • glacial acetic acid
    ºùÃÊ»ê.
  • glucosidase, alpha-glucosidase(acid maltase)
    -±Û·çÄڽõ¥À̽º, -glucosidase
  • glucuronic acid
    ±Û·çÄí·Ð»ê.
  • glucuronic acid pathway
    ±Û·çÄí·Ð»ê°æ·Î.
  • glutamic acid
    ±Û·çŽ»ê.
  • glutamic acid dehydrogenase
    ±Û·çŽ»êÅ»¼ö¼ÒÈ¿¼Ò, ±Û·çŽ»êµ¥È÷µå·Î°Ô<³ª>Á¦.
  • glutaric acid
    ±Û·çŸ¸£»ê.
  • glyceric acid
    ±Û¸®¼¼¸°»ê(¡­ß«).
  • glyceroboric acid
    ±Û¸®¼¼¸£ºØ»ê
  • glycocholic acid
    ±Û¸®ÄÚÄÝ»ê.
  • glycolic acid
    ±Û¶óÀÌÄÝ»ê
  • gout,uric acid stones
    ¿ä»ê°á¼®
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
  • ¿µ¹®
    ÇѱÛ
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ(Ó±ÛÜùêà÷ì×í­).
  • protein therapy
    ´Ü¹é(Áú)¿ä¹ý(¡­èþÛö).
  • protein,al
    AL(´Ü¹é)
  • protein,bence jones
    º¥½º-Á¸½º(´Ü¹é)
  • protein-calorie deficiency
    ´Ü¹é(Áú)¿­·®°áÇÌ(Ó±ÛÜ(òõ)æðÕáÌÀù¹)
  • protein-calorie malnutrition
    ´Ü¹é(Áú)¿­·®¿µ¾ç½ÇÁ¶(Áõ)(Ó±ÛÜ(òõ)æðÕáç½å×ã÷ðà(ñø))
  • protein-energy malnutrition
    ´Ü¹é(Áú)¿¡³ÊÁö¿µ¾ç½ÇÁ¶(Áõ)(¡­ç½å×ã÷ðà(ñø))
  • protein-losing
    ´Ü¹é»ó½Ç¼º.
  • protein-losing enteropathy
    ´Ü¹é»ó½Ç¼º À庴Áõ(íóÜ»ñø)
  • protein-losing enteropathy
    ´Ü¹é»ó½ÇÀ庴Áõ(Ó±ÛÜßÃã÷íóÜ»ñø)
  • purified protein derivative
    Á¤Á¦´Ü¹éÁúÀ¯µµÃ¼.
  • racemized protein
    ¶ó¼¼¹ÌÈ­´Ü¹éÁú(¡­ûùÓ±ÛÜòõ).
  • ras protein
    ras ´Ü¹é(¡­Ó±ÛÜ)
  • reserve protein
    ÀúÀå´Ü¹éÁú.
  • serum protein
    Ç÷û´Ü¹é
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  • ¿µ¹®
    ÇѱÛ
  • protein-sparing action
    ´Ü¹éÁú Àý¾à ÀÛ¿ë(Ó±ÛÜòõï½å³íÂéÄ)
  • protein structure
    ´Ü¹éÁú ±¸Á¶(Ó±ÛÜòõϰðã)
  • protein synthesis
    ´Ü¹éÁú ÇÕ¼º(Ó±ÛÜòõùêà÷)
  • protein synthesis factor
    ´Ü¹éÁú ÇÕ¼ºÀÎÀÚ(Ó±ÛÜòõùêà÷ì×í­)
  • protein-synthesizing system
    ´Ü¹éÁú ÇÕ¼º(Ó±ÛÜòõùêà÷) ½Ã½ºÅÛ
  • protein turnover
    ´Ü¹éÁú Àüȯ(Ó±ÛÜòõï®üµ)
  • protein value
    ´Ü¹éÁú(Ó±ÛÜòõ)°ª
  • read-through protein
    ÆÇµ¶ ´Ü¹éÁú(÷÷ÔÁÓ±ÛÜòõ)
  • Rec A protein
    Rec A ´Ü¹éÁú(Ó±ÛÜòõ)
  • regulatory protein
    Á¶Àý ´Ü¹éÁú(ðàï½Ó±ÛÜòõ)
  • relaxation protein
    ÀÌ¿Ï ´Ü¹éÁú(ì¬èÐÓ±ÛÜòõ)
  • relaxing protein
    ÀÌ¿Ï ´Ü¹éÁú(ì¬èÐÓ±ÛÜòõ)
  • rep protein
    rep ´Ü¹éÁú(Ó±ÛÜòõ)
  • respiratory protein
    È£Èí ´Ü¹éÁú(Ó±ÛÜòõ)
  • ribosomal protein
    ¶óÀ̺¸¼Ø ´Ü¹éÁú(Ó±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 16
TCA T-cell A locus; terminal cancer; tetracyclic antidepressant; total cholic acid; total circulating al...
TPA tannic acid, polyphosphomolybdic acid, and amino acid; 12-0-tetradecanoyl-phorbol-13-acetate; third-...
UA absorption unsharpness; ultra-audible; ultrasonic arteriography; umbilical artery; unauthorized abse...
CPBA Competitive Protein Binding Assay
RBP Retinol Binding Protein
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 16
C/EBP delta CCAAT enhancer binding protein delta
C/EBP-beta CCAAAT/enhancer-binding protein-beta
C/EBPalpha CAAT/enhancer binding protein-alpha
CBP CPP-binding protein
CREB CRE binding protein
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • umbellic acid
    ¿òº§»ê
  • uric acid test
    ¿ä»ê °Ë»ç
  • urocanic acid
    ¿ì·ÎÄ«´Ñ»ê
    È÷½ºÅ¸¹ÎÀÇ Áß°£ ´ë»ç »ê¹°. º¸Åë ±Û·çŸ¹Î»êÀ¸·Î ÀüȯµÈ´Ù.
  • urodeoxycholic acid
    ¿ì¸£¼Ò µð¿Á½ÃÄÝ»ê
    »ç¶÷¿¡°Ô´Â ¼Ò·®¸¸ÀÌ Á¤»óÀûÀ¸·Î Á¸ÀçÇÏ´Â ´ãÁó»ê. chenodeoxycholic acidÀÇ À̼ºÃ¼. °õÀÇ ´ãÁó¿¡¼­ óÀ½À¸·Î ºÐ¸®µÇ¾ú´Ù. ÄÝ·¹½ºÅ×·Ñ ´ã¼®À» ¿ëÇØ½Ã۱â À§Çؼ­ Åõ¿©µÈ´Ù.
  • uroleucic acid
    ¿ì·Î·ù½Å»ê
    °áÁ¤»ê. ¾Ëİſ´¢Áõ ȯÀÚÀÇ ¿ä¿¡¼­ ¹ß°ßµÈ´Ù.
  • uronic acid
    ¿ì·Ð»ê
    ´Ü´ç·ù ź¼Ò¼âÀÇ ¾ËÄݱ⠸»´ÜÀÇ »êÈ­¿¡ ÀÇÇØ »ý¼ºµÈ ¾Ëµ¥ÇÏÀ̵å»ê.
  • valproic acid
    ¹ßÇÁ·Î»ê, º§ÇÁ·ÎÀÍ»ê
    2-ÇÁ·ÎÇÊÆæÅ¸³ëÀÍ »ê. 8°³ÀÇ Åº¼Ò Ãø¼â¸¦ °®´Â Áö¹æ»ê. Ç×°£ÁúÁ¦ÀÌ´Ù.
  • vanillyl mandelic acid
    ¹Ù´Ò¸± ¸¸µ¨»ê
    Ä«Å×ÄݾƹÎÀÇ ¸¶Áö¸· ´ë»ç¹°.
  • vinylacetic acid
    ºñ´Ò ÃÊ»ê
  • volatile acid
    Èֹ߼º »ê
  • weak acid
    ¾à»ê
    ÇØ¸®µµ°¡ ³·Àº »ê
  • xanthenuric acid
    Ű»êÅ×´©¸£ »ê
    Æ®¸³ÅäÆÇ¿¡¼­ Ű´­·¹´Ñ¼ö»êÈ­ Ű´­·¹´ÑÀ» °ÅÃÄ »ý±â´Â À¯±â»ê.
  • xanthourenic acid
    ÀÜÅõ·»»ê
    4,8-dihydroxyquinaldic acid. L-try
  • xylic acid
    ÀÚÀϸ°[Å©½Ç]»ê
    °áÁ¤»ê.
  • zinc oxide-ethoxybenzoic acid cement
    EBA ½Ã¸àÆ®
    »êÈ­ ¾Æ¿¬ À¯Áö³î ½Ã¸àÆ®ÀÇ ¾×Áß¿¡¼­ À¯Áö³îÀÇ ´ëºÎºÐÀ» EBA·Î ´ëüÇÑ Ä¡°ú¿ë ½Ã¸àÆ®.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
peripheral membrane protein <protein> Membrane proteins that are bound to the surface of the membrane and not integrated into the hydrophobic region. Usually soluble and were originally thought to bind to integral proteins by ionic and other weak forces (and could therefore be removed by high ionic strength, for example). However, it is now clear that some peripheral membrane proteins are covalently linked to molecules that are part of the membrane bilayer (see acylated proteins and glypiation) and that there are others that fit the original definition but are perhps more appropriately considered proteins of the cytoskeleton (e.g. Band 4.1 and spectrin) or extracellular matrix (e.g. Fibronectin).
(18 Nov 1997)
peripheral protein <protein> A water-soluble protein that is loosely bound (by hydrogen bonds orelectrostatic forces) to a membrane.
(09 Oct 1997)
periplasmic protein disulfide oxidoreductase <enzyme> Isolated from haemophilus influenzae; may be required for assembly or folding of one or more disulfide-containing cell envelope proteins; ccmg isolated from paracoccus denitrificans
Registry number: EC 1.8.4.-
Synonym: por disulfide oxidoreductase, por gene product, periplasmic oxidoreductase, ccmg gene product
(26 Jun 1999)
ribosomal protein <protein> Proteins present within the ribosomal subunits. In prokaryotes there are 31 proteins in the large subunit and 21 in the small subunit. Eukaryotic subunits have 50 (large subunit) and 33 (small subunit) proteins.
(18 Nov 1997)
ribosomal protein s6 kinase <enzyme> A protein serine/threonine kinase which is involved in cell transformation by polyoma virus and is connected to the expression of igf2. The immunosuppressant rapamycin inhibits the activation of the kinase, leading to reduced translation of certain mRNAs and a decrease in protein synthesis.
Registry number: EC 2.7.10.-
(12 Dec 1998)
ribosomal protein S6 kinase kinase <enzyme> Isolated from unfertilised xenopus eggs; a 41 kD enzyme that is associated, in vivo, with phosphorylation on threonine and tyrosine residues and, in vitro, with phosphorylation on serine as well
Registry number: EC 2.7.1.-
Synonym: rsk kinase
(26 Jun 1999)
chk1 protein kinase <enzyme> A yeast protein kinase homolog, involved in cell-cycle arrest when DNA damage has occurred or when unligated DNA is present; named chk1 for checkpoint kinase; genbank af016582 (human), af016583 (murine)
Registry number: EC 2.7.1.-
Synonym: chk1 kinase, chk1 gene product, rad27 protein, rad27 gene product, hchk1 (human), mchk1 (murine), mammalian chk1
(26 Jun 1999)
green fluorescent protein <protein> A protein found in jellyfish which fluoresces, or glows green visible light when excited by UV light with a wavelength of 395 nanometres.
It can function as a biological marker when attached to other proteins. The structure of the protein is cylindrical with the glowing component, an amino acid complex called a fluorophore, in the middle of it.
(09 Oct 1997)
groel protein A chaperonin 60 heat-shock protein isolated from escherichia coli.
(12 Dec 1998)
groes protein A chaperonin 10 heat-shock protein isolated from escherichia coli.
(12 Dec 1998)
GTPase activating protein <molecular biology> Originally purified as a 125 kD protein from bovine brain (1044 amino acids), stimulates the GTPase activity of ras p21 and thereby switches it to the inactive state.
GAP may itself be regulated by phospholipids and by phosphorylation on a tyrosine residue by growth factor receptors (PDGF R, EGF R). The neurofibromatosis type 1 gene NF1) codes for a protein homologous to GAP. GAP has both SH2 and SH3 domains. Another example is sar 1 (from yeast).
(18 Nov 1997)
RLK5-associated protein phosphatase <enzyme> Associated with serine-threonine receptor-like kinase, rlk5; from arabidopsis thaliana; composed of 3 domains, an amino-terminal signal anchor, a kinase interaction domain and a type 2c protein phosphatase catalytic domain; mw 65 kD; genbank u09505
Registry number: EC 3.1.3.-
Synonym: kapp, kinase-associated protein phosphatase
(26 Jun 1999)
methyl accepting chemotaxis protein Methyl accepting chemotaxis proteins. Proteins of the inner cytoplasmic face of the bacterial plasma membane with which the receptors of the outer face interact. Four different MCPs are known in E. Coli, each with a separate set of receptors. Can be methylated at various sites, methylation is part of the adaptation to the signal. Although important intermediate signal integration sites, they are not directly connected to the motor.
(18 Nov 1997)
PfKIN protein kinase <enzyme> Snf1 type protein kinase from plasmodium flaciparum; genbank z22868
Registry number: EC 2.7.10.-
(26 Jun 1999)
MHC class II protein <protein> The antigen-presenting molecule found primarily on macrophages and B lymphocytes.
(09 Oct 1997)
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