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"muscle 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
  • rectus muscle
    °ðÀº±Ù, Á÷±Ù
  • red muscle
    Àû»ö±ÙÀ°
  • red muscle fiber
    Àû»ö±Ù(À°)¼¶À¯, Àû»ö±Ù(À°)¼¼Æ÷
  • rhomboid major muscle
    Å«¸¶¸§±Ù, ´ë´ÉÇü±Ù
  • rhomboid minor muscle
    ÀÛÀº¸¶¸§±Ù, ¼Ò´ÉÇü±Ù
  • risorius muscle
    ÀÔ²¿¸®´ç±è±Ù, ¼Ò±Ù
  • sartorius muscle
    ³Ò´Ù¸®ºø±Ù, ºÀ°ø±Ù
  • sartorius muscle flap
    ³Ò´Ù¸®ºø±ÙÆÇ, ³ÐÀû´Ù¸®ºø±ÙÆÇ, ºÀ°ø±ÙÆÇ
  • soleus muscle
    °¡Àڹ̱Ù
  • soleus muscle flap
    °¡ÀÚ¹Ì±ÙÆÇ
  • sphincter ani externus muscle
    ¹Ù±ùÇ×¹®Á¶ÀÓ±Ù, ¿ÜÇ×¹®°ý¾à±Ù
  • sphincter muscle
    Á¶ÀÓ±Ù, °ý¾à±Ù
  • sphincter pupillae muscle
    µ¿°øÁ¶ÀÓ±Ù, µ¿°ø°ý¾à±Ù
  • scalene muscle
    ¸ñ°¥ºñ±Ù, »ç°¢±Ù
  • splenius capitis muscle
    ¸Ó¸®³ÎÆÇ±Ù, µÎÆÇ»ó±Ù
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  • ¿µ¹®
    ÇѱÛ
  • rhomboid major muscle
    Å«¸¶¸§±Ù
  • rhomboid minor muscle
    ÀÛÀº¸¶¸§±Ù
  • risorius muscle
    ÀÔ²¿¸®´ç±è±Ù
  • rotator muscle
    ȸÀü±Ù, µ¹¸²±Ù
  • sartorius muscle
    ³Ò´Ù¸®ºø±Ù
  • scalene muscle
    ¸ñ°¥ºñ±ÙÀ°
  • semimembranous muscle
    ¹Ý¸·¸ð¾ç±Ù
  • semispinalis muscle
    ¹Ý°¡½Ã±Ù
  • semitendinosus muscle
    ¹ÝÈûÁÙ¸ð¾ç±Ù
  • serratus anterior muscle
    ¾ÕÅé´Ï±Ù
  • skeletal muscle
    °ñ°Ý±Ù
  • smooth muscle
    ¹Î¹«´Ì±ÙÀ°, ÆòȰ±ÙÀ°
  • soleus muscle
    °¡Àڹ̱Ù
  • sphincter muscle
    Á¶ÀÓ±Ù
  • sphincter ani externus muscle
    ¹Ù±ùÇ×¹®Á¶ÀÓ±Ù
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  • ¿µ¹®
    ÇѱÛ
  • pubovesical muscle ³ª musculus pubovesicalis
    Ä¡°ñ¹æ±¤±Ù(¡­Û¹ÎÍÐÉ).
  • pubovesical muscle ³ª musculus pubovesicalis
    Ä¡°ñ¹æ±¤±Ù(¡­Û¹ÎÍÐÉ).
  • pyloric sphincter muscle
    ³¯¹®Á¶ÀÓ±Ù
  • quadrate pronator muscle ³ª musculus pronator quadratus
    »ç°¢È¸³»±Ù, ¹æÇüȸ³»±Ù(Û°û¡üÞÒ®ÐÉ).
  • quadriangular muscle
    ³×¸ð±ÙÀ°
  • quadriceps muscle of thigh ³ª musculus quadriceps femoris
    ´ëÅð³×°¥·¡ ±Ù, ´ëÅð»çµÎ±Ù(ÓÞ÷ÚÞÌÔéÐÉ).
  • quadriceps muscle of thigh ³ª musculus quadriceps femoris
    ´ëÅð³×°¥·¡ ±Ù, ´ëÅð»çµÎ±Ù(ÓÞ÷ÚÞÌÔéÐÉ).
  • radial flexor muscle of wrist ; muscl
    ¿ä°ñÃø¼ö ±Ù±¼±Ù.
  • rapid muscle
    ¼Ó±Ù(áÜÐÉ).
  • recession of muscle
    ±Ù ÅðÃà.
  • recession of muscle
    ±ÙÅðÃà(ÐÉ÷Üõî)
  • recession of muscle
    ±ÙÈÄÀü(¼ú)
  • rectococcygeal muscle ³ª musculus rec to co ccy geus
    Á÷Àå¹Ì°ñ±Ù( òÁíóÚ­ÍéÐÉ).
  • rectourethral muscle
    °ðâÀÚ¿äµµ±Ù
  • rectouterine muscle
    °ðâÀÚÀڱñÙ
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  • ¿µ¹®
    ÇѱÛ
  • protein s
    ´Ü¹éS
  • protein score
    ´Ü¹é°¡(ËÀËÑ˧) ½ÄǰÀÇ .
  • protein sensitization
    ´Ü¹é°¨ÀÛ(¡­ÊïíÂ).
  • protein separation
    ´Ü¹éºÐ¸®
  • protein sparing effect
    ´Ü¹éÁúÀý¾àÈ¿°ú(Ó±ÛÜòõï½å³üùÍý).
  • protein synthesis
    ´Ü¹éÁúÇÕ¼º.
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ(Ó±ÛÜùêà÷ì×í­).
  • protein therapy
    ´Ü¹é(Áú)¿ä¹ý(¡­èþÛö).
  • protein,actin-binding
    ¾×ƾ-°áÇÕ(´Ü¹é)
  • 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.
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ASMD anterior segment mesenchymal dysgenesis; atonic sclerotic muscle dystrophy
BESM bovine embryonic skeletal muscle
BSMC bronchial smooth muscle cell
CKM creatine kinase, muscle type
CKMM creatine kinase, muscle type
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 16
BTSM bovine tracheal smooth muscle
CM ciliary muscle
DM dry muscle
FDI first dorsal interosseous muscle
FCR flexor carpi radialis muscle
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • secondary local muscle soreness
    ¼Ó¹ß¼º ±¹¼Ò ±Ùµ¿Åë
  • semispinal muscle of neck
    ¸ñ ¹Ý°¡½Ã±Ù, °æºÎ ¹Ý±Ø±Ù
  • serratus anterior muscle
    ¾Õ Åé´Ï±Ù, Àü°Å±Ù
    µ¿ÀǾî=muscle serratus anterior.
  • serratus posterior inferior muscle
    ¾Æ·¡ µÚ Åé´Ï±Ù, ÇÏÈİűÙ
    µ¿ÀǾî=muscle serratus
  • sheath of rectus abdominis muscle
    ¹è °ðÀº ±Ù Áý, º¹Á÷±Ù ÃÊ
  • short palmar muscle
    ´ÜÀå±Ù
    ¼öÀå°Ç¸·ÀÇ Ã´Ãø¿¡¼­ ÀϾ ¼öÀå̫̿ÀÇ ÇǺο¡ ´ê´Â ¼Ò±Ù.
  • skeletal muscle
    °ñ°Ý±Ù
    1. ±ä ¿øÁÖÇü ´ÙÇÙ ¼¼Æ÷ÀÎ ±ÙÀ° ¼¶À¯µéÀÌ ¸ð¿©¼­ ´Ù¹ßÀ» Çü¼ºÇÑ´Ù. ¼öÃà °úÁ¤Àº ºü¸£°í °­·ÂÇÏ¸ç ¼öÀÇÀû
  • skeletal muscle relaxant
    °ñ°Ý±Ù ÀÌ¿Ï ¾à
  • slow muscle fiber
    Áö±Ù¼¶À¯
  • sluggish muscle
    ¿Ï¼­±Ù, Áö±Ù
  • smooth muscle
    ¹Î¹«´Ì±Ù, ÆòȰ±Ù
    1. ¹æÃßÇü ¼¼Æ÷ÀÇ ÁýÇÕÀ¸·Î ÀÌ·ç¾îÁø ±ÙÀ°. ±¤ÇÐÇö¹Ì°æ¿¡¼­ º¸¸é ¹Î¹«´Ì. ¼öÃà °úÁ¤Àº ´À¸®°í ºÒ¼öÀÇÀû
  • smooth muscle cell
    ¹Î¹«´Ì±Ù ¼¼Æ÷, ÆòȰ±Ù ¼¼Æ÷
  • smooth muscle relaxant
    ÆòȰ±Ù ÀÌ¿Ï ¾à
  • soleus muscle
    ³åÄ¡±Ù
    ºñº¹±Ù°ú ´õºÒ¾î ÇÏÅð »ïµÎ±ÙÀ» ±¸¼ºÇϰí ÀÖ´Â ±ÙÀ°. ºñº¹±ÙÀÇ ÇÏÃþ¿¡ ÀÖ´Ù. ¸ð¾çÀÌ ¹°°í±âÀÇ ³ÒÄ¡¿Í °°ÀÌ »ý°Ü ÀÌ·± À̸§ÀÌ ºÙ¾ú´Ù. ÇÏÅð°ñÀÇ Èĸ鿡¼­ ½ÃÀÛÇÏ¿© ¾ÆÅ³·¹½º°ÇÀÌ µÇ°í, ¹ß²ÞÄ¡ »À¿¡ ºÙ¾î ÀÖ´Ù. °æ°ñ ½Å°æÀÇ Áö¹è¸¦ ¹ÞÀ¸¸ç, ¹ß²ÞÄ¡¸¦ µé¾î¿Ã¸®´Â ÀÛ¿ëÀ» ÇÑ´Ù.
  • spasm of muscle
    ±Ù °æ·Ã
    ±Ù ¶Ç´Â ±Ù±ºÀÇ ±Þ°ÝÇÑ ºÒ¼öÀÇÀû ¼öÃà. °£´ë¼º °æ·Ã°ú °­Á÷¼º °æ·ÃÀ¸·Î ³ª´©¾îÁø´Ù. ÀüÀÚ´Â ±ÙÀ°ÀÇ ¼öÃà°ú ÀÌ¿ÏÀÌ ¹Ýº¹µÇ°í °¥Ç×±ÙÀÌ ±×´ë·Î ¼öÃàÇÔÀ¸·Î½á »ý±ä´Ù. ÈÄÀÚ´Â Áö¼ÓÀû ±Ù ¼öÃà¿¡ ÀÇÇØ »ý±ä´Ù. °æ·ÃÀ» ÀÏÀ¸Å°´Â ÁúȯÀ¸·Î´Â °£Áú, È÷½ºÅ׸®, ¶Ç´Â ÆÄ»ódzÀ̳ª ±¤°ßº´ µîÀÇ °¨¿°Áõ, »óÇÇ ¼Òü µîÀÇ ³»ºÐºñ ÀÌ»ó, ½ºÆ®¸®Å©³ªÀÎ µîÀÇ Áßµ¶, ¿äµ¶Áõ µîÀ» µé ¼ö ÀÖ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
protein-histidine kinase <enzyme> Sass involved in transduction of starvation and cell density inputs; hkna isolated from bacillus thuringiensis; ciah isolated from streptococcus pneumoniae; do not confuse with plp1 protein
Registry number: EC 2.7.3.-
Synonym: histidine protein kinase, histidine kinase, hkna gene product, ciah gene product, kinc gene product, prrb gene product, plec gene product, mxcq gene product, rese gene product, hpka gene product, comd gene product, plpa gene product (phytochrome-like), divj gene product, sensor histidine kinase, sass gene product
(26 Jun 1999)
protein hybridization The formation of a protein consisting of two or more polypeptide chains from separate and different polypeptide chains.
(12 Dec 1998)
protein hydrolysate A sterile solution of amino acids and soft chain peptides prepared from a suitable protein by acid or enzymatic hydrolysis; used intravenously for the maintenance of positive nitrogen balance in severe illness, and after surgery involving the alimentary tract; or used orally in the diets of infants allergic to milk or as a supplement when high protein intake from ordinary foods cannot be accomplished.
(05 Mar 2000)
protein isoprenylation A post-translational modification of proteins by the attachment of an isoprenoid to the c-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.
(12 Dec 1998)
protein kinase <enzyme> Enzyme catalysing transfer of phosphate from ATP to hydroxyl side chains on proteins, causing changes in function. most phosphate on proteins of animal cells is on serine residues, less on threonine, with a very small amount on tyrosine residues. Tyrosine kinases phosphorylate proteins on tyrosine, serine / threonine kinases on serine or threonine.
(18 Nov 1997)
protein kinase B kinase <enzyme> Phosphorylates and activates protein kinase b on threonine-308; requires phosphatidylinositol-3,4,5-trisphosphate
Registry number: EC 2.7.10.-
Synonym: upstream kinase, pkb kinase
(26 Jun 1999)
protein kinase c <enzyme> An enzyme that phosphorylates proteins on serine or threonine residues in the presence of physiological concentrations of calcium and membrane phospholipids. The additional presence of diacylglycerols markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by phorbol esters and it is believed that protein kinase c is the receptor protein of tumour-promoting phorbol esters.
Registry number: EC 2.7.1.-
(12 Dec 1998)
protein kinases <enzyme> A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
Chemical name: ATP-protein phosphotransferase
Registry number: EC 2.7.1.37
(12 Dec 1998)
protein-losing enteropathies A series of gastrointestinal disorders which share in common the excessive loss of protein, mainly albumin, across the gut wall. They occur in the stomach (menetrier disease), as well as the small bowel (intestinal lymphangiectases, assorted inflammatory states). They are also occasionally associated with congestive heart failure (again a small bowel protein loss).
(12 Dec 1998)
protein-losing enteropathy Condition in which plasma protein is lost to excess into the intestine. This can be due to diverse causes including gluten enteropathy, extensive ulceration of the intestine, intestinal lymphatic blockage, and infiltration of leukaemic cells into the intestinal wall.
(12 Dec 1998)
protein-lysine 6-oxidase <enzyme> An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide.
Chemical name: Protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Registry number: EC 1.4.3.13
(12 Dec 1998)
protein malnutrition Children are particularly prone to develop protein malnutrition. To grow, children have to consume enough nitrogen-containing food (protein) to maintain a positive nitrogen balance whereas adults need only be in nitrogen equilibrium.
(12 Dec 1998)
protein metabolism Decomposition and synthesis of protein in the tissues.
Synonym: proteometabolism.
(05 Mar 2000)
protein methylesterase <enzyme> Hydrolyzes protein methyl esters to yield methanol and unmethylated protein; found in bacterial and human cells
Registry number: EC 3.1.1.-
(26 Jun 1999)
protein methyltransferases <enzyme> Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-adenosyl-l-methionine acts as the methylating agent.
Registry number: EC 2.1.1
(12 Dec 1998)
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    ±¸ºÐ/º¸Çè±Þ¿©
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