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"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
  • ghost cell glaucoma
    ºó¼¼Æ÷³ì³»Àå, À¯·É¼¼Æ÷³ì³»Àå
  • giant cell
    °Å´ë¼¼Æ÷
  • giant cell carcinoma
    °Å´ë¼¼Æ÷¾ÏÁ¾
  • giant cell epulis
    °Å´ë¼¼Æ÷Ä¡ÀºÁ¾
  • giant cell glioblastoma
    °Å´ë¼¼Æ÷¾Æ±³¸ð¼¼Æ÷Á¾, °Å´ë¼¼Æ÷±³¸ð¼¼Æ÷Á¾
  • giant cell granuloma
    °Å´ë¼¼Æ÷À°¾ÆÁ¾
  • giant cell myeloma
    °Å´ë¼¼Æ÷°ñ¼öÁ¾
  • giant cell myocarditis
    °Å´ë¼¼Æ÷½É±Ù¿°
  • giant cell pneumonia
    °Å´ë¼¼Æ÷Æó·Å
  • giant cell tumor
    °Å´ë¼¼Æ÷Á¾¾ç
  • glandular cell
    »ù¼¼Æ÷, ¼±¼¼Æ÷
  • glial cell
    ½Å°æ¾Æ±³¼¼Æ÷
  • glitter cell
    ¹Ý¦¼¼Æ÷
  • globoid cell
    °ø¸ð¾ç¼¼Æ÷
  • globoid cell leukodystrophy
    °ø¼¼Æ÷¹é»öÁúÀå¾Ö, ±¸Çü¼¼Æ÷¹éÁúµð½ºÆ®·ÎÇÇ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
  • ¿µ¹®
    ÇѱÛ
  • helmet cell
    Åõ±¸¼¼Æ÷
  • helper cell
    µµ¿ò¼¼Æ÷, Á¶·Â¼¼Æ÷
  • hemolytic plaque-forming cell
    ¿ëÇ÷ÆÇÇü¼º¼¼Æ÷, ¿ëÇ÷ÇöóÅ©Çü¼º¼¼Æ÷
  • heterotrophic cell
    Á¾¼Ó¿µ¾ç¼¼Æ÷
  • high-threshold cell
    °í¹®Åΰª¼¼Æ÷
  • horizontal cell
    ¼öÆò¼¼Æ÷
  • horny cell
    °¢Áú¼¼Æ÷
  • hybrid cell
    ÀâÁ¾¼¼Æ÷
  • hypersensitized cell
    °ú¹Î°¨¼¼Æ÷
  • immunologically competent cell
    (¢¡immunocyte) ¸é¿ª¼¼Æ÷
  • indeterminate cell
    ºÎÁ¤Çü¼¼Æ÷
  • indifferent cell
    ¹«°ü¼¼Æ÷
  • inducer cell
    À¯µµ¼¼Æ÷
  • inflammatory cell
    ¿°Áõ¼¼Æ÷
  • infundibular cell
    ±ò¶§±â¼¼Æ÷
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
  • ¿µ¹®
    ÇѱÛ
  • giant cell pneumonia
    °Å¼¼Æ÷Æó·Å.
  • giant cell tumor
    °Å¼¼Æ÷Á¾¾ç.
  • giant cell tumor
    °Å´ë¼¼Æ÷Á¾¾ç.(¡­ðþåË)
  • giant cell, langhans
    ¶ûÇѽº °Å´ë¼¼Æ÷, Langhans °Å´ë¼¼Æ÷
  • giant pyramidal cell
    Å«ÇǶó¹Ô½Å°æ¿ø, °Å´ëÃßü¼¼Æ÷(¡­õÐô÷á¬øà).
  • gingiva,giant cell granuloma of
    °Å´ë¼¼Æ÷ À°¾ÆÁ¾
  • glandular cell
    »ù¼¼Æ÷, ¼±¼¼Æ÷(àÍá¬øà).
  • glandular cell
    »ù¼¼Æ÷
  • glassy cell carcinoma of cervix
    À¯¸®¾ç ¼¼Æ÷ ÀڱðæºÎ¾Ï
  • glia cell
    ¾Æ±³¼¼Æ÷, (½Å°æ)±³¼¼Æ÷.
  • gliacyte =glia cell
    ¾Æa¼¼Æ÷, (½Å°æ)a¼¼Æ÷(¡­á¬øà).
  • gliacyte =glia cell
    ¾Æ±³¼¼Æ÷, (½Å°æ)±³¼¼Æ÷(¡­á¬øà).
  • glial cell
    ¾Æa¼¼Æ÷, (½Å°æ)a¼¼Æ÷.
  • glial cell
    ¾Æ±³¼¼Æ÷
  • glial cell body
    ¾Æ±³¼¼Æ÷ü
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
  • ¿µ¹®
    ÇѱÛ
  • dark cell norepinephrine cell
    ¾îµÎ¿î¼¼Æ÷ ³ë¸£¿¡Çdz×ÇÁ¸°¼¼Æ÷
  • interstitial cell dark cell
    »çÀÌÁú¼¼Æ÷
  • interstitial cell leydigs cell
    »çÀÌÁú¼¼Æ÷
  • lupus erythematosus cell = LE cell
    È«¹Ý¼º ·çǪ½º¼¼Æ÷(¡­á¬øà)
  • neurolemmal cell [schwanns cell]
    ½Å°æÁý¼¼Æ÷
  • pale cell acanthoma => clear cell acanthoma
  • parafollicular cell [calcitonin cell]
    ¼ÒÆ÷°ç¼¼Æ÷
  • plasma cell orificial mucositis => plasma cell cheilitis
  • quiescent cell, Q cell
    Á¤Áö¼¼Æ÷
  • secretory epithelial cell [glandular cell]
    ºÐºñ»óÇǼ¼Æ÷ (»ù¼¼Æ÷)
  • supporting cell [sertoli cell]
    ¹öÆÀ¼¼Æ÷
  • supporting cell [type ii glomus cell]
    ¹öÆÀ¼¼Æ÷
  • sustentacular cell [sertoli cell]
    ¹öÆÀ¼¼Æ÷
  • abnormality of cell interaction
    ¼¼Æ÷»óÈ£ÀÛ¿ëÀÌ»ó
  • acantholytic cell
    ±Ø¼¼Æ÷ÇØ¸®¼¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
  • ¿µ¹®
    ÇѱÛ
  • polycephalic protein
    º¹ÇÕ±â´É ´Ü¹éÁú(ÜÜùêѦÒöÓ±ÛÜòõ)
  • polyfunctional protein
    ´Ù±â´É ´Ü¹éÁú(ÒýѦÒöÓ±ÛÜòõ)
  • P protein
    P ´Ü¹éÁú(Ó±ÛÜòõ)
  • prepriming protein
    ÇÁ·¹ÇÁ¶óÀÌ¹Ö ´Ü¹éÁú(Ó±ÛÜòõ)
  • primary derived protein
    ÀÏÂ÷ À¯µµ ´Ü¹éÁú(ìéó­ë¯ÓôÓ±ÛÜòõ)
  • primary protein derivative
    ÀÏÂ÷ ´Ü¹éÁúÀ¯µµÃ¼
  • protein
    ´Ü¹éÁú(Ó±ÛÜòõ)
  • protein A
    ´Ü¹éÁú(Ó±ÛÜòõ) A
  • protein biosynthesis
    ´Ü¹éÁú »ýÇÕ¼º(Ó±ÛÜòõßæùêà÷)
  • protein blotting
    ´Ü¹éÁú(Ó±ÛÜòõ) ºí·ÔÆÃ
  • protein-bound iodine
    ´Ü¹éÁú°áÇÕ(Ó±ÛÜòõÌ¿ùê) ¿äµå
  • protein C
    ´Ü¹éÁú(Ó±ÛÜòõ) C
  • protein-calorie malnutrition
    ´Ü¹éÁú(Ó±ÛÜòõ)-Ä®·Î¸® ¿µ¾ç½ÇÁ¶(ç½å×ã÷ðà)
  • protein coat
    ´Ü¹éÁú(Ó±ÛÜòõ) ÄÚÆ®
  • protein conformation
    ´Ü¹éÁú(Ó±ÛÜòõ) ÀÔüÇüÅÂ(Ø¡ô÷û¡÷¾)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 17
SNGFR single nephron glomerular filtration rate
SOSF single organ system failure
SPACE single potential analysis of cavernous electrical activity
SPECT single photon emission computed tomography
SPT secretin-pancreazymin [test]; single patch technique; sleep period time; spectrin; station pull-thro...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 17
SEVC single electrode voltage clamp
SXA single energy X-ray absorptiometry
SLT single lung transplant
ssDNA single strand DNA
SSB single strand binding
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • laminar II cell
    Á¦ 2Ãþ ¼¼Æ÷
  • laminar ¥± cell
    Á¦ 2Ãþ ¼¼Æ÷
    Á¦ 2ÃþÀÇ ¼¼Æ÷´Â 2Á¾·ù°¡ Àִµ¥ ÃþÀÇ ¹Ù±ù ÂÊ 1/4´Â ´õ¿í ÀÛÀº ¼¼Æ÷·Î ÅëÁõ°ú ¿­¿¡ ´ëÇÑ ¼ö¿ëü¸¦ °¡Áö°í ÀÖ°í, ¾È ÂÊ 3/4´Â Á» ´õ Å« ¼¼Æ÷·Î ¹«µ¶¼ºÀÇ ±â°è¼ö¿ëü¸¦ °¡Áö°í ÀÖ´Ù.
  • Langerhans cell
    ¶û°Ô¸£Çѽº ¼¼Æ÷, Ç¥ÇÇ¼Ó Å« Æ÷½Ä¼¼Æ÷
    µ¿ÀǾî=intrae
  • large cell
    ´ë¼¼Æ÷
    ƯÁ¤ ÀÌÀ¯°¡ ÀÖ¾î
  • LE cell
    LE ¼¼Æ÷, È«¹Ý¼º ³¶Ã¢ ¼¼Æ÷
    µÕ±Û°í, ±ÕÁú·Î º¸ÀÌ´Â ºÀÀÔü¸¦ ޽ÄÇÑ ¼º¼÷ È£Áß±¸¼º ´ÙÇÙ ¹éÇ÷±¸. ±× ºÀÀÔü ÀÚü´Â ´Ù¸¥ È£Áß±¸¿¡¼­ À¯·¡µÈ °ÍÀÌ´Ù. È«¹Ý¼º ·çǪ½º¿¡ ƯÀ¯ÇÑ °ÍÀÌÁö¸¸ °áÇÕ Á¶Á÷ÀÇ À¯»çÇÑ Áúȯ¿¡¼­µµ °üÂûµÈ´Ù.
  • lingual benign giant cell tumor
    ¾ç¼º °Å´ë ¼¼Æ÷ ¼³ Á¾¾ç
  • lupus erythematosus cell
    È«¹Ý¼º ·çǪ½º ¼¼Æ÷, È«¹Ý¼º ³¶Ã¢ ¼¼Æ÷
  • M-cell
    M ¼¼Æ÷
  • malignant plasma cell
    ¾Ç¼º ÇüÁú ¼¼Æ÷
  • mast cell
    ºñ¸¸ ¼¼Æ÷
    µ¿¹°ÀÇ °áÇÕ Á¶Á÷ ¼Ó¿¡ ÀÖ´Â ¼¼Æ÷·Î ¸¸¼º ¿°Áõ¿¡ À־ÀÇ Áõ½Ä Á¶Á÷ ¼Ó¿¡ ¸¹¾Æ¼­ ÀÌ·± À̸§ÀÌ ºÙ¾ú´Ù. ÀÌ ¼¼Æ÷ ¼Ó¿¡´Â ¸¹Àº °ú¸³ÀÌ µé¾îÀÖ¾î ¿°Áõ ¹ÝÀÀ¿¡ °ü¿©Çϰí ÀÖ´Ù.
  • mature daughter cell
    ¼º¼÷ÇÑ µþ ¼¼Æ÷
  • mean cell

    mean cell hemoglobin (Æò±Õ ÀûÇ÷±¸ Ç÷»ö¼Ò

  • mean cell volume
    Æò±Õ ÀûÇ÷±¸ ¿ëÀû
  • megakaryocytic blast cell
    °ÅÇÙ¸ð±¸
  • memory T cell
    ±â¾ï T ¼¼Æ÷
    Ç׿øÀÌ µé¾î¿ÔÀ» ¶§ B ¼¼Æ÷°¡ Èä¼±À» ÀÚ±ØÇÏ¿© T ¸²ÇÁ±¸¸¦ »ý»ê, ºÐÈ­ÇÒ ¶§ Ç׿ø-Ç×ü ¹ÝÀÀÀ» ÇÏÁö ¾Ê°í ³²¾Æ ±× Ç׿øÀ» ±â¾ïÇÏ¿© 2Â÷ Ç׿ø-Ç×ü ¹ÝÀÀ¿¡ ½Å¼ÓÈ÷ ¹ÝÀÀÀ» º¸À̵µ·Ï ÇÏ´Â T ¼¼Æ÷.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 17
protein conformation The characteristic 3-dimensional shape of a protein, imposed upon it by the secondary and tertiary structure of the peptide chain. This stage in the structure of a protein describes the highest level of organization in overall structure assumed by multimeric proteins (aggregates of more than one polypeptide chain). This is the fourth folding level of protein building.
(12 Dec 1998)
protein crystallization This is an essential process in determining a protein's three-dimensional structure, and hence in using that information to design drugs.
(14 Nov 1997)
protein-D-aspartate methyltransferase <enzyme> For protein carboxymethylases consider also protein o-methyltransferase
Registry number: EC 2.1.1.77
Synonym: d-aspartyl-l-isoaspartyl methyltransferase, protein d-aspartate-l-isoaspartate methyltransferase, protein l-isoaspartate o-methyltransferase, protein-beta-aspartate methyltransferase, protein-l-isoaspartate methyltransferase, protein l-isoaspartyl methyltransferase, isoaspartyl-aspartyl protein methyltransferase, protein-d-asp methyltransferase, l-isoaspartyl protein carboxymethyltransferase, pcm gene product, pcmt1 gene product
(26 Jun 1999)
protein deficiency A nutritional condition produced by a deficiency of proteins in the diet, characterised by adaptive enzyme changes in the liver, increase in amino acid synthetases, and diminution of urea formation, thus conserving nitrogen and reducing its loss in the urine. Growth, immune response, repair, and production of enzymes and hormones are all impaired in severe protein deficiency. Protein deficiency may also arise in the face of adequate protein intake if the protein is of poor quality (i.e., the content of one or more amino acids is inadequate and thus becomes the limiting factor in protein utilization).
(12 Dec 1998)
protein disulfide-isomerase <enzyme> An enzyme that catalyses the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of procollagen-proline dioxygenase.
Chemical name: Protein disulfide-isomerase
Registry number: EC 5.3.4.1
(12 Dec 1998)
protein disulfide reductase (glutathione) <enzyme> An enzyme that catalyses the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates.
Chemical name: Glutathione:protein-disulfide oxidoreductase
Registry number: EC 1.8.4.2
(12 Dec 1998)
protein-energy malnutrition The lack of sufficient energy or protein to meet the body's metabolic demands, as a result of either an inadequate dietary intake of protein, intake of poor quality dietary protein, increased demands due to disease, or increased nutrient losses.
(12 Dec 1998)
protein engineering Normally means the use of recombinant DNA technology to produce proteins with desired modifications in the primary sequence.
See: site specific mutagenesis.
(18 Nov 1997)
protein factor The factor (6.25) by which the nitrogen content of a protein is multiplied to give the amount of protein.
(05 Mar 2000)
protein fever Fever produced by the injection of foreign protein, such as milk.
(05 Mar 2000)
protein folding A rapid biochemical reaction involved in the formation of proteins. It begins even before a protein has been completely synthesised and proceeds through discrete intermediates (primary, secondary, and tertiary structures) before the final structure (quaternary structure) is developed.
(12 Dec 1998)
protein G Protein from Group C Streptococci that binds the Fc portion of IgG. Is less species specific than Protein A.
(18 Nov 1997)
protein geranylgeranyltransferase <enzyme> Involved in protein isoprenylation; transfers geranylgeranyl group to cys fourth from the c-terminal of GTP-binding proteins; amino acid sequence of beta subunit of ggtase-i known; genbank l24116; see also rab, ras, and rhoa p21 geranylgeranyl- transferases and component a, rab geranylgeranyltransferase
Registry number: EC 2.5.1.-
Synonym: protein ggtase, geranylgeranyltransferase type-i, ggtase-i, geranylgeranyl-protein transferase type 1
(26 Jun 1999)
protein-glutamine gamma-glutamyltransferase <enzyme> An enzyme that catalyses the reaction of protein glutamine and an alkylamine to yield protein n(5)-alkylglutamine and ammonia. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular n(6)-(5-glutamyl)lysine crosslinks. In the epidermis these cross-linked proteins are involved in the formation of the cornified envelope of the stratum corneum cells. In the plasma, the transglutaminase is called factor xiiia, the activated form of factor xiii. The crosslinking results in the stabilization of the fibrin clot.
Pharmacological action: coagulants.
Chemical name: Protein-glutamine:amine gamma-glutamyltransferase
Registry number: EC 2.3.2.13
(12 Dec 1998)
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)
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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MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 17
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