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"cell factor"¿¡ ´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
  • cell mass
    ¼¼Æ÷µ¢ÀÌ, ¼¼Æ÷±«
  • cell membrane
    ¼¼Æ÷¸·
  • cell membrane permeability
    ¼¼Æ÷¸·Åõ°ú¼º
  • cell organelle
    ¼¼Æ÷¼Ò±â°ü
  • cell respiration
    ¼¼Æ÷È£Èí
  • cell strain
    ¼¼Æ÷ÁÖ
  • cell substitution
    ¼¼Æ÷´ëü, Ç÷±¸´ëü
  • cell surface receptor
    ¼¼Æ÷Ç¥¸é¼ö¿ëü
  • cell swelling
    ¼¼Æ÷Á¾Ã¢
  • cell-associated antibody
    ¼¼Æ÷¿¬°üÇ×ü
  • cell-bound antibody
    ¼¼Æ÷°áÇÕÇ×ü
  • cell-fixed antibody
    ¼¼Æ÷°áÇÕÇ×ü
  • cell-mediated cytolysis
    ¼¼Æ÷¸Å°³¼¼Æ÷¿ëÇØ
  • cell-mediated cytotoxicity
    ¼¼Æ÷¸Å°³¼¼Æ÷µ¶¼º
  • cell-mediated hypersensitivity
    ¼¼Æ÷¸Å°³°ú¹Î¼º
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  • ¿µ¹®
    ÇѱÛ
  • chromophilic cell
    »ö¼Òµë¼¼Æ÷, È£»ö¼Ò¼¼Æ÷
  • chromophobic cell
    »ö¼Ò¾Èµë¼¼Æ÷
  • ciliated cell
    ¼¶¸ð¼¼Æ÷, ÀÜÅм¼Æ÷
  • clear cell
    Åõ¸í¼¼Æ÷
  • clear cell carcinoma
    Åõ¸í¼¼Æ÷¾ÏÁ¾
  • clear cell hidradenoma
    Åõ¸í¼¼Æ÷¶¡»ùÁ¾
  • clear cell sarcoma
    Åõ¸í¼¼Æ÷À°Á¾
  • columnar cell
    ¿øÁÖ¼¼Æ÷
  • columnar absorptive cell
    ±âµÕÈíÂø¼¼Æ÷
  • committed cell
    ¾ô¸Ç¼¼Æ÷, ¼öÀÓ¼¼Æ÷
  • complex cell
    º¹ÇÕ¼¼Æ÷
  • cone cell
    ¿ø»Ô¼¼Æ÷
  • cone cell layer
    ¿ø»Ô¼¼Æ÷Ãþ
  • connective tissue cell
    °áÇÕÁ¶Á÷¼¼Æ÷
  • continuous cell line
    ¹«ÇÑÁõ½Ä¼º¼¼Æ÷ÁÖ, ¿¬¼Ó°è´ë¼¼Æ÷ÁÖ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
  • ¿µ¹®
    ÇѱÛ
  • adult t-cell leukemia/lymphoma
    ¼º¼÷ T-¼¼Æ÷ ¹éÇ÷º´/¸²ÇÁÁ¾(à÷âÙ¡­á¬øà ÛÜúìÜ»/¡­ðþ)
  • alpha cell
    ¾ËÆÄ¼¼Æ÷
  • alpha cell
    ¾ËÆÄ¼¼Æ÷(¡­á¬øà)
  • alpha cell tumor
    ¾ËÆÄ ¼¼Æ÷Á¾(¡­á¬øàðþ)
  • amacrine cell
    ¾Æ¸¶Å©¸° ¼¼Æ÷
  • amacrine cell
    ¹«Ãà»è¼¼Æ÷
  • ameboid cell
    ¾Æ¸Þ¹Ù¸ð¾ç¼¼Æ÷
  • aneuploid cell
    À̼ö¼º¼¼Æ÷
  • anitschkow cell
    ¾Æ´ÏÄ¡ÄÚ¿ì¼¼Æ÷(¡­á¬øà)
  • annular elastotic giant cell granuloma
    ȯ»ó ź·Â ¼¶À¯¼º °Å´ë¼¼Æ÷ À°¾ÆÁ¾
  • anoxic cell
    ¹«»ê¼Ò¼¼Æ÷
  • anti-idiotypic T suppressor cell
    Ç×°³º°Æ¯ÀÌÇü ¾ïÁ¦T¼¼Æ÷
  • antibody dependent cell mediated cytotoxicity
    Ç×üÀÇÁ¸ ¼¼Æ÷¸Å°³ ¼¼Æ÷µ¶¼º.
  • antibody forming cell
    Ç×ü»ý»ê¼¼Æ÷(ù÷ô÷ßæß§á¬øà).
  • antibody producing cell
    Ç×ü»ý»ê¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • inhibition(-tory) factor, macrophage migration
    ´ë½Ä¼¼Æ÷ À¯ÁÖÀúÁöÀÎÀÚ
  • insulin-like growth factor
    Àν¶¸°À¯»ç¼ºÀåÀÎÀÚ
  • intensity factor
    °­µµÀÎÀÚ
  • intrinsic factor
    ³»ÀμºÀÎÀÚ, ³»Àμº¿ä¼Ò, °íÀ¯ÀÎÀÚ
  • intrinsic factor
    ³»ÀÎÀÚ
  • intrinsic factor =IF
    ³»ÀÎÀÚ(Ò®ì×í­).
  • intrinsic factor(if)
    ³»ÀÎÀÚ(Ò®ì×í­)
  • islet-activation factor
    ¶û°Ô¸£Çѽº»ù Ȱ¼ºÀÎÀÚ, ¹éÀÏÇØ±Õµ¶¼Ò
  • isodose shift factor
    µî¼±·®À̵¿°è¼ö
  • kerma factor
    Ä¿¸¶ °è¼ö
  • ketogenic factor
    ÄÉÅæÃ¼Çü¼ºÀÎÀÚ(¡­ô÷û¡à÷ì×í­).
  • labile factor
    ºÒ¾ÈÁ¤ÀÎÀÚ, ºÒ¾ÈÁ¤¿ä¼Ò.
  • lactogenic factor
    ÃÖÀ¯ÀÎÀÚ(¡­ì×í­).
  • lactogenic factor
    À¯ÁóºÐºñÀ¯µµÀÎÀÚ(¡­ì×í­).
  • leucocyte inhibition factor
    ¹éÇ÷±¸¾ïÁ¦ÀÎÀÚ.
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  • ¿µ¹®
    ÇѱÛ
  • permeability factor
    Åõ°ú ÀÎÀÚ(÷âΦì×í­)
  • plasma factor
    Ç÷ÀåÀÎÀÚ(úìíìì×í­)
  • plasma thromboplastic factor
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ(úìíìúìîûû¡à÷ì×í­)
  • plasma thromboplastic factor B
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ B
  • platelet-activating factor
    Ç÷¼ÒÆÇȰ¼º ÀÎÀÚ(úìá³÷ùüÀàõì×í­)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡(úìá³÷ùë¦ÕÎ) ¼ºÀåÀÎÀÚ(à÷íþì×í­)
  • PP factor
    PP ÀÎÀÚ(ì×í­)
  • preexponential factor
    Áö¼ö(ò¦â¦)¾ÕÀÚ¸® ÀÎÀÚ(ì×í­)
  • protein factor
    ´Ü¹éÁú ÀÎÀÚ(Ó±ÛÜòõì×í­)
  • protein release factor
    ´Ü¹éÁú ¹æÃâÀÎÀÚ(Ó±ÛÜòõÛ¯õóì×í­)
  • protein synthesis factor
    ´Ü¹éÁú ÇÕ¼ºÀÎÀÚ(Ó±ÛÜòõùêà÷ì×í­)
  • prothrombin factor
    ÇÁ·ÎÆ®·Òºó ÀÎÀÚ(ì×í­)
  • Prower factor
    ÇÁ¶ó¿ö ÀÎÀÚ(ì×í­)
  • psi factor
    »çÀÌ ÀÎÀÚ(ì×í­)
  • pyruvate oxidation factor
    ÆÄÀÌ·çºê»ê(ß«) »êÈ­ÀÎÀÚ(ß«ûùì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 16
GF gastric fistula; gastric fluid; germ-free; glass factor; glomerular filtration; gluten-free; grandfa...
GIF gastric intrinsic factor; growth hormone-inhibiting factor
HGF hepatocyte growth factor; hyperglycemic-glucogenolytic factor
HLF heat-labile factor; hepatic leukemia factor
HSTF heat shock transcription factor; human serum thymus factor
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 16
SRBC Anti-sheep red blood cell
ADCC Antibody Dependent Cell Cytotoxicity
ADCC Antibody Dependent Cell-Mediated Cytotoxicity
ADCC Antibody-dependent cell-mediated cytolysis
AFC Antibody-forming cell
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cell membrane permeability
    ¼¼Æ÷¸· Åõ°ú¼º
  • cell of parathyroid gland
    ºÎ°©»ó»ù ¼¼Æ÷, ºÎ°©»ó¼± ¼¼Æ÷
  • cell organelles
    ¼¼Æ÷ ¼Ò±â°ü
  • cell physiology
    ¼¼Æ÷ »ý¸®ÇÐ
  • cell pole
    ¼¼Æ÷ ±Ø
  • cell regeneration
    ¼¼Æ÷ Àç»ý
  • cell saver
    Ç÷±¸ ȸ¼ö±â
  • cell sorting
    ¼¼Æ÷ ºÐ·ù
  • cell substitution
    ¼¼Æ÷ ġȯ, Ç÷±¸ Àç»ý
  • cell surface marker
    ¼¼Æ÷ Ç¥¸é Ç¥ÁöÀÚ
  • cell survival curve
    ¼¼Æ÷ »ýÁ¸ °î¼±
  • cell transfer
    ¼¼Æ÷ ÀÌÀÔ
    Á¼Àº Àǹ̿¡¼­´Â °¢Á¾ ¼¼Æ÷¸¦ ¹æ»ç¼± Á¶»ç µîÀÇ Ã³¸®¸¦ °¡ÇÑ µ¿¹°¿¡ ÁÖÀÔÇϰí ÁÖÀÔµÈ ¼¼Æ÷ÀÇ ¼º»óÀ» Á¶»çÇÏ´Â °ÍÀ» ¸ñÀûÀ¸·Î ÇÑ ¼¼Æ÷ ÁÖÀÔÀÇ ¹æ¹ýÀ» °¡¸®Å°¸ç in vitro¿¡¼­ ¼¼Æ÷ ±â´ÉÀ» Á¶»çÇϱⰡ °ï¶õÇÑ °æ¿ì, in vivo¿¡¼­ÀÇ ¹ÝÀÀ¼ºÀ» Á¶»çÇÏ°í ½ÍÀº °æ¿ì, ¶Ç chimera mouse¸¦ Á¦ÀÛÇÒ ¶§¿¡ »ç¿ëµÈ´Ù. ³ÐÀº Àǹ̿¡¼­´Â ¼¼Æ÷°¡ ÇÑÆí¿¡¼­ ´Ù¸¥ ÆíÀ¸·Î À̵¿ÇÏ´Â °ÍÀ» °¡¸®Å²´Ù.
  • cell typing
    Ç÷±¸Çü °Ë»ç
  • cell wall
    ¼¼Æ÷ º®
    µ¿ÀǾî=cell membrane.
  • cell wall inhibitor
    ¼¼Æ÷ º® ÇÕ¼º ¾ïÁ¦Á¦
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 16
thymic factor, circulating <chemical> A thymus-dependent nonapeptide found in normal blood. Stimulates the formation of e rosettes and is believed to be involved in T-cell differentiation.
Chemical name: Thymulin
(12 Dec 1998)
thymic lymphopoietic factor A glycoprotein (MW about 12,000) that has been extracted from thymus; this thymus-produced hormone(s) confers immunological competence on thymus-dependent cells and induces lymphopoiesis.
(05 Mar 2000)
thyroid-stimulating hormone-releasing factor <protein> See thyrotrophic releasing hormone.
(18 Nov 1997)
thyrotoxic complement-fixation factor A form of thyrotoxin; an antigen found most readily in thyroid tissue from thyrotoxic individuals; known to be chemically and immunologically distinct from thyroglobulin, and fixes complement when combined with antibody related to the gamma-globulin fraction of serum. With the exception of extremely small concentrations, the antigen is rarely found in normal glands or in diseased glands that are not associated with thyrotoxicosis; it is probably an intracellular substance (possibly a constituent of the "microsomal fraction"), and does not contain iodine in significant quantity. Not related to the complement-fixation reaction occurring with serum in Hashimoto's disease, in which the antigen is thyroglobulin.
(05 Mar 2000)
thyrotropin-releasing factor Former name for thyrotropin-releasing hormone.
(05 Mar 2000)
tissue factor <cell biology> Integral membrane glycoprotein of around 250 residues, that initiates blood clotting after binding factors VII or VIIa.
(18 Nov 1997)
tissue weighting factor In radiation protection, a factor weighting the equivalent dose in a particular tissue or organ in terms of its relative contribution to the total deleterious effects resulting from uniform irradiation of the whole body.
See: effective dose.
(05 Mar 2000)
elongation factor <biochemistry> Peptidyltransferase components of ribosomes that catalyse formation of the acyl bond between the incoming amino acid residue and the peptide chain.
There are three classes of elongation factor: EF1_ (EF Tu in prokaryotes) binds GTP and aminoacyl tRNA, delivering it to the A site of ribosomes. EF 1_ (EF Ts) helps in regeneration of GTP EF 1_. EF 2 (EF G) binds GTP and peptidyl tRNA and translocates it from the A site to the P site. Diptheria toxin inhibits protein synthesis in eukaryotes by adding an ADP ribosyl group to a modified histidine residue (dipthamide) in elongation factor II.
(18 Nov 1997)
transcription factor <molecular biology> Protein required for recognition by RNA polymerases of specific stimulatory sequences in eukaryotic genes.
Several are known that activate transcription by RNA polymerase II when bound to upstream promoters.
Transcription of the 5S RNA gene in Xenopus by RNA polymerase III is dependent on a 40 kD protein TFIIIA that binds to a regulatory site in the centre of the gene and was the first protein found to exhibit the metal binding domains known as zinc fingers.
(17 Mar 1998)
transcription factor ap-1 A multiprotein complex composed of the products of c-jun and c-fos proto-oncogenes. These proteins must dimerise in order to bind to the ap-1 recognition site, also known as the tpa-responsive element (tre). Ap-1 controls both basal and inducible transcription of several genes.
(12 Dec 1998)
transcription factor, sp1 Promoter-specific RNA polymerase II transcription factor that binds to the gc box, one of the upstream promoter elements (upe) in mammalian cells. The binding of sp1 is necessary to initiate transcription in the promoters of a variety of cellular and viral genes including c-ha-ras and HIV.
(12 Dec 1998)
transfer factor A dialysable factor obtained from sensitised T-cells by freezing and thawing, that may possibly immunopotentiate animals.The transfer of specific immunity from one animal to another has been claimed.
(18 Nov 1997)
transforming factor The DNA responsible for bacterial transformation.
(05 Mar 2000)
transforming growth factor <growth factor> Proteins secreted by transformed cells that can stimulate growth of normal cells.
Unfortunate misnomer, since they induce aspects of transformed phenotype, such as growth in semi solid agar, but do not actually transform.
Transforming growth factor alpha, 50 amino acid polypeptide originally isolated from viral transformed rodent cells, contains EGF like domain and binds to EGF receptor. Stimulates growth of microvascular endothelial cells, i.e. Is angiogenic.
Transforming growth factor beta a homodimer of two 112 chains, polypeptide is secreted by many different cell types, stimulates wound healing but in vitro is also a growth inhibitor for certain cell types. The transforming growth factor family includes many of the bone morphogenetic proteins.
Acronym: TGF
(18 Nov 1997)
transforming growth factor alpha Factor isolated in a variety of tissues including epithelium, and maternal decidua. It is closely related to epidermal growth factor (epidermal growth factor-urogasterone) and binds to the egf receptor. Tgf-alpha acts synergistically with tgf-beta in inducing phenotypic transformation, but its physiological role is unknown.
(12 Dec 1998)
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    ±¸ºÐ/º¸Çè±Þ¿©
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