¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"single cell 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.
À̰ÍÀ» ¿øÇϼ̽À´Ï±î?
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  • ¿µ¹®
    ÇѱÛ
  • horny cell
    °¢Áú¼¼Æ÷
  • human diploid cell vaccine
    »ç¶÷µÎ¹è¼ö¼¼Æ÷¹é½Å
  • human T-cell lymphoma/leukemic virus
    »ç¶÷T¼¼Æ÷¸²ÇÁÁ¾/¹éÇ÷º´¹ÙÀÌ·¯½º
  • human T-cell lymphotropic virus
    »ç¶÷T¼¼Æ÷¸²ÇÁģȭ¹ÙÀÌ·¯½º
  • Hurthle cell adenoma
    ÈÖ¸£Æ²·¹¼¼Æ÷»ùÁ¾
  • hybrid cell
    ÀâÁ¾¼¼Æ÷
  • islet cell
    ¼¶¼¼Æ÷
  • islet cell adenoma
    ¼¶¼¼Æ÷»ùÁ¾
  • islet cell carcinoma
    ¼¶¼¼Æ÷¾ÏÁ¾
  • immunologically competent cell
    ¸é¿ª¼¼Æ÷
  • indeterminate cell
    ºÎÁ¤Çü¼¼Æ÷
  • indifferent cell
    ¹«°ü¼¼Æ÷
  • inducer cell
    À¯µµ¼¼Æ÷
  • inflammatory cell
    ¿°Áõ¼¼Æ÷
  • infundibular cell
    ±ò¶§±â¼¼Æ÷, ´©µÎ¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • mononuclear cell
    ´ÜÇÙ¼¼Æ÷
  • mossy cell
    À̳¢¼¼Æ÷
  • mother cell
    ¸ð¼¼Æ÷, ¾î¹Ì¼¼Æ÷
  • motor cell
    ¿îµ¿½Å°æ¼¼Æ÷
  • mucous cell
    Á¡¾×¼¼Æ÷
  • mulberry cell
    ¿Àµð¼¼Æ÷
  • multinuclear giant cell
    ¹µÇÙ°Å´ë¼¼Æ÷
  • multipolar nerve cell
    ¹µ±Ø½Å°æ¼¼Æ÷
  • myeloid cell
    (¢¡marrow cell) °ñ¼ö¼¼Æ÷
  • myeloma cell
    °ñ¼öÁ¾¼¼Æ÷
  • myoepithelial cell
    ±ÙÀ°»óÇǼ¼Æ÷
  • myoid cell
    À¯»ç±ÙÀ°¼¼Æ÷
  • natural killer cell
    ÀÚ¿¬¼¼Æ÷µ¶¼º¼¼Æ÷, ÀÚ¿¬¼¼Æ÷µ¶¼º¼¼Æ÷
  • nerve cell
    ½Å°æ¼¼Æ÷
  • neural crest cell
    ½Å°æ´É¼±¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • granulosa theca cell tumor
    °ú¸³Çù¸·¼¼Æ÷Á¾ ¾ç(¡­úõØ¯á¬øàðþåË).
  • granulosa theca cell tumor
    °ú¸³Çù¸·¼¼Æ÷Á¾ ¾ç(¡­úõØ¯á¬øàðþåË)
  • great alveolar cell
    Å«ÆóÆ÷(»óÇÇ)¼¼Æ÷<°ú¸³Æó Æ÷¼¼Æ÷>, ´ëÆóÆ÷¼¼Æ÷.
  • growth factor, B cell (BCGF)
    B¼¼Æ÷ Áõ½ÄÃËÁøÀÎÀÚ
  • hair cell
    Åм¼Æ÷, À¯¸ð¼¼Æ÷(êóÙ¾á¬øà).
  • hair cell
    Åм¼Æ÷
  • hairy cell
    ¸ð¹ß»ó¼¼Æ÷.
  • hairy cell
    ¸ð¹ß»ó¼¼Æ÷
  • hairy cell leukemia
    ¸ð¹ß»ó¼¼Æ÷¹éÇ÷º´
  • hairy cell leukemia
    ¸ð¹ß»ó¼¼Æ÷¹éÇ÷º´, Åм¼Æ÷¹éÇ÷º´
  • hairy cell leukemia
    Åм¼Æ÷ ¹éÇ÷º´
  • hairy cell leukemia
    ¸ð¹ß»ó¼¼Æ÷ ¹éÇ÷º´
  • hairy-cell leukemia
    ¸ð¹ß»ó¼¼Æ÷¹éÇ÷º´
  • heart failure cell
    ½ÉºÎÀü¼¼Æ÷(¡­á¬øà)
  • helmet cell
    Åõ±¸¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • antibody forming cell
    Ç×ü»ý»ê¼¼Æ÷(ù÷ô÷ßæß§á¬øà).
  • antibody producing cell
    Ç×ü»ý»ê¼¼Æ÷
  • antigen presenting cell
    Ç׿øÁ¦½Ã¼¼Æ÷.
  • antigen reactive cell
    Ç׿ø¹ÝÀÀ¼¼Æ÷.
  • antigen recognizing cell
    Ç׿ø½Äº°¼¼Æ÷.
  • apex of cell
    ¼¼Æ÷²À´ë±â
  • apical cell
    Á¤(´Ü)¼¼Æ÷(ð¢Ó®á¬øà)
  • aplasia, red cell
    ÀûÇ÷±¸ Çü¼ººÎÀü(îåúìϹû¡à÷Üôîï)
  • argentaffin chromaffin cell
    Å©·Òģȭ¼º ¼¼Æ÷
  • argyrophil(e) cell
    ÀºÄ£È­¼º ¼¼Æ÷(ëÞöÑûúàõá¬øà)
  • arsenical basal cell carcinoma
    ºñ¼Ò¼º(Ý÷áÈàõ) ±âÀú¼¼Æ÷¾Ï
  • arteritis,giant cell of aorta
    ´ëµ¿¸Æ(ÓÞÔÑØæ)ÀÇ °Å¼¼Æ÷¼º(ËÝá¬øààõ)
  • aschoff cell
    ¾Æ¼îÇÁ ¼¼Æ÷(¡­á¬øà)
  • aschoff giant cell
    ¾Æ¼îÇÁ °Å¼¼Æ÷(¡­ËÝá¬øà)
  • asymmetric cell division
    ºñ´ëμº ¼¼Æ÷ºÐ¿­
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  • ¿µ¹®
    ÇѱÛ
  • 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)
  • retinol-binding protein
    ·¹Æ¼³î °áÇÕ ´Ü¹éÁú(Ì¿ùêÓ±ÛÜòõ)
  • ribosomal protein
    ¶óÀ̺¸¼Ø ´Ü¹éÁú(Ó±ÛÜòõ)
  • r-protein
    r-´Ü¹éÁú(Ó±ÛÜòõ)
  • scaffold protein
    °ñ°Ý ´Ü¹éÁú(Íé̫ӱÛÜòõ)
  • secondary derived protein
    ÀÌÂ÷ À¯µµ´Ü¹éÁú(ì£ó­ë¯ÓôÓ±ÛÜòõ)
  • secondary protein derivative
    ÀÌÂ÷ ´Ü¹éÁúÀ¯µµÃ¼(ì£ó­Ó±ÛÜòõë¯Óôô÷)
  • secretory protein
    ºÐºñ ´Ü¹éÁú(ÝÂÝôÓ±ÛÜòõ)
  • sensor protein
    ¼¾¼­ ´Ü¹éÁú(Ó±ÛÜòõ)
  • sex steroid binding plasma protein
    ¼º(àõ)½ºÅ×·ÎÀÌµå °áÇÕ(Ì¿ùê) Ç÷Àå(úìíì) ´Ü¹éÁú(úìíìÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 20
sv sievert; single vibration
SVD single vessel disease; singular value decomposition; small vessel disease; spontaneous vaginal deliv...
vs see above [Lat. vide supra]; single vibration; versus; vibration seconds; vital signs
B-J protein Bence-Jones Protein
  ÀÇÀÇ; Multiple Myeloma
PEM Protein-Energy Malnutrition
  = PCM; Protein Calorie Malnutrition
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 20
APC T-cell-antigen-presenting cell
B cell cell
G cell gastrin cell
BSAP B cell specific activator protein
CC10 Clara Cell 10 kDa protein
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 20
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • nociceptive projection cell
    Ä§ÇØ ¼ö¿ë¼º Åõ»ç ¼¼Æ÷, À¯ÇØ ¼ö¿ë¼º Åõ»ç ¼¼Æ÷
  • nociceptive-specific cell
    Ä§ÇØ ¼ö¿ë-ƯÀ̼º ¼¼Æ÷, À¯ÇØ ¼ö¿ë-ƯÀ̼º ¼¼Æ÷
  • non-caseating epithelioid cell granulomata
    ºñ°Ç¶ô¼º À¯»óÇÇ ¼¼Æ÷ À°¾ÆÁ¾
  • non-keratinized squamous cell carcinoma
    ºñ°¢È­¼º ÆíÆò »óÇÇ ¼¼Æ÷ ¾Ï
  • non-nociceptive cell
    ºñÄ§ÇØ ¼ö¿ë¼º ¼¼Æ÷, ºñÀ¯ÇØ ¼ö¿ë¼º ¼¼Æ÷
  • null cell
    ´­ ¼¼Æ÷
    B, T ¼¼Æ÷ Ç¥¸é Ç¥Áö¸¦ °¡ÁöÁö ¾ÊÀº ¸²ÇÁ±¸.
  • off-cell pause
    ²¨Áü ¼¼Æ÷ ÁßÁö
  • on-cell
    ÄÑÁü ¼¼Æ÷
  • osteoprogenitor cell
    °ñ Á¶»ó ¼¼Æ÷, »À Á¶»ó ¼¼Æ÷
    1. °ñÀÇ À¯¸® Ç¥¸é ȤÀº ±× ±Ùó¿¡¼­ º¼ ¼ö ÀÖ´Â ºñ±³Àû ¹ÌºÐÈ­µÈ ¼¼Æ÷·Î¼­, ¾î¶² ȯ°æ¿¡¼­´Â ¼¼Æ÷ ºÐ¿­ÇÏ¿© °ñ¾Æ¼¼Æ÷·Î ÀüȯµÇµç°¡ ȤÀº À¶ÇÕÇÏ¿© ÆÄ°ñ ¼¼Æ÷·Î µÇ±âµµ ÇÑ´Ù. 2. ÀÏ¹Ý °ÉÇÕ Á¶Á÷ÀÇ ¼¼Æ÷µé°ú ¸¶Âù°¡Áö·Î °£Áú Á¶Á÷¿¡¼­ À¯·¡ÇÑ ¼¼Æ÷·Î¼­ À¯»ç ºÐ¿­ ´É·Â°ú »À ¼¼Æ÷·Î ºÐÈ­µÉ ¼ö ÀÖ´Â ´É·ÂÀ» °®°í ÀÖ´Ù. Áß°£¿± ¼¼Æ÷¿Í À¯»çÇϸç, ÇÙÀº ¿°±â¼º ¿°·á¿¡ ¹Ì¾àÇÏ°Ô ¿°»öµÇ°í ¼¼Æ÷ÁúÀº ¾çÀÌ Àû¾î »ê¼º ¿°·á¿¡ ¹Ì¾àÇÏ°Ô ¿°»öµÈ´Ù.
  • oxyntic cell
    »ê ºÐºñ¼º ¼¼Æ÷
    »ê ºÐºñ¼ºÀÇ À§º® ¼¼Æ÷¿Í °°ÀÌ »êÀ» ºÐºñÇÏ´Â ¼¼Æ÷.
  • oxyphil cell
    È£»ê¼º ¼¼Æ÷
  • oxyphilic cell
    È£»ê ¼¼Æ÷, È£»ê¼º ¼¼Æ÷
  • packed cell volume
    ÃæÀü ¼¼Æ÷ ¿ëÀû
  • packed red blood cell
    ³óÃà ÀûÇ÷±¸, ÃæÀü ÀûÇ÷±¸
    1. Ç÷¾×À» ¿ø½É ºÐ¸®ÇßÀ» ¶§ ¹Ù´Ú¿¡ ¹ÐÁýÇØ ÀÖ´Â °Í, ÃæÀü ÀûÇ÷±¸ ºÎÇǸ¦ Ç츶ÅäÅ©¸®Æ®¶óÇÑ´Ù. 2. hematocrit °ü¿¡ äÃëÇÑ ÀüÇ÷À» ÃÖ´ë·Î ¿ø½É ºÐ¸®ÇÏ¿© ¾ò¾îÁö´Â ÀûÇ÷±¸ÀÇ Ä§ÀüÃþ.
  • paneth cell
    È£»ê¼º °ú¸³ ¼¼Æ÷
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 20
protein-serine-threonine kinases <enzyme> A group of enzymes that catalyses the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Registry number: EC 2.7.10
(12 Dec 1998)
protein-serine-threonine phosphatase <enzyme> Consider also EC 3.1.3.16 phosphoprotein phosphatases
Registry number: EC 3.1.3.-
Synonym: serine phosphatase, threonine phosphatase, protein-serine phosphatase, serine-threonine phosphatase
(26 Jun 1999)
protein shock The systemic reaction following the parenteral administration of a protein.
(05 Mar 2000)
protein shock therapy The injection of a foreign protein to induce fever as a means of treating certain diseases.
Synonym: foreign protein therapy.
(05 Mar 2000)
protein-S-isoprenylcysteine O-methyltransferase <enzyme> Methylates carboxyl-terminal cysteine of yeast sex factors and ha-ras oncogene protein; c-terminal s-geranylgeranylcysteine and s-geranylcysteine residues are also methylated more slowly
Registry number: EC 2.1.1.100
Synonym: pcc methyltransferase, farnesyl cysteine c-terminal methyltransferase, protein-cysteine-carboxyl methyltransferase, 5-prenylcysteine methyltransferase, isoprenylated protein methyltransferase, ste14 gene product, prenylated protein carboxyl methyltransferase, ppmtase, protein c-terminal prenylcysteine methyltransferase
(26 Jun 1999)
protein splicing Excision of in-frame internal protein sequences (inteins) of a precursor protein, coupled with ligation of the flanking sequences (exteins). Protein splicing is an autocatalytic reaction and results in the production of two proteins from a single primary translation product: the intein and the mature protein.
(12 Dec 1998)
protein status A term used to indicate the level of protein in a person's system. A severe lack of protein can result in protein-calorie malnutrition.
(16 Dec 1997)
protein structure The amino acids and their manner of arrangement in constituting a protein. The four stages of protein structuring are primary (protein structure, primary see amino acid sequence), secondary (protein structure, secondary), tertiary (protein structure, tertiary), and quaternary (protein structure, quaternary see protein conformation).
(12 Dec 1998)
protein structure, secondary The stage in the development of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices and beta sheets. This is the first folding level of protein building.
(12 Dec 1998)
protein structure, tertiary The stage in the structural development of a protein in which combinations of alpha helices and beta sheets pack together to form compactly folded globular units named domains. Small proteins consist of only one domain but larger proteins contain a number of domains which are usually connected by open lengths of polypeptide chain. This stage is a combination of the second and third folding levels of protein building.
(12 Dec 1998)
protein synthesis The process in which individual amino acids, whether of exogenous or endogenous origin, are connected to each other in peptide linkage in a specific order dictated by the sequence of nucleotides in DNA; this governing sequence is conveyed to the synthesizing apparatus in the ribosomes by mRNA, formed by base-pairing on the DNA template.
(05 Mar 2000)
protein synthesis inhibitor Compounds which inhibit the synthesis of proteins. They are usually antibiotics or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the the a site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.
(12 Dec 1998)
protein targeting The process through which newly-made proteins are sorted and carriedto different parts of a cell.
(09 Oct 1997)
protein-tyrosine kinase <enzyme> An enzyme that catalyses the phosphorylation of tyrosine residues in proteins with ATP or other nucleotides as phosphate donors.12.
Chemical name: ATP:protein-tyrosine O-phosphotransferase
Registry number: EC 2.7.1.112
(12 Dec 1998)
protein-tyrosine-phosphatase <enzyme> An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with protein-tyrosine kinase, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.
Chemical name: Protein-tyrosine-phosphate phosphohydrolase
Registry number: EC 3.1.3.48
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ±¸ºÐ/º¸Çè±Þ¿©
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