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  • ¿µ¹®
    ÇѱÛ
  • carrier protein
    ¿î¹Ý´Ü¹éÁú
  • catabolite (gene) activator protein
    ºÐÇØ´ë»ç»ê¹°(À¯ÀüÀÚ)Ȱ¼º´Ü¹éÁú
  • catabolite activator protein
    ºÐÇØ´ë»ç»ê¹°È°¼º´Ü¹éÁú
  • denatured protein
    º¯¼º´Ü¹éÁú
  • derived protein
    À¯µµ´Ü¹éÁú
  • different membrane protein
    À¯°ü¸·´Ü¹éÁú
  • extracellular matrix protein
    ¼¼Æ÷¹Ù±ù¹ÙÅÁÁú´Ü¹éÁú, ¼¼Æ÷¿Ü±âÁú´Ü¹éÁú
  • endogenous protein
    ³»ÀδܹéÁú
  • foreign protein
    ÀÌÁ¾´Ü¹éÁú
  • glial fibrillary acidic protein
    ¾Æ±³¼¼Æ÷¼¶À¯»ê¼º´Ü¹éÁú, ±³¼¶À¯»ê¼º´Ü¹éÁú
  • globular protein
    °ø¸ð¾ç´Ü¹éÁú, ±¸»ó´Ü¹éÁú
  • heat-shock protein
    ¿­Ãæ°Ý´Ü¹éÁú
  • heterologous protein
    ÀÌÁ¾´Ü¹éÁú
  • high-protein diet
    °í´Ü¹éÁú½Ä»ç
  • human plasma protein fraction
    »ç¶÷Ç÷Àå´Ü¹éºÐÀ²
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • deposit protein
    ÀúÀå´Ü¹éÁú
  • derived protein
    À¯µµ´Ü¹éÁú
  • different membrane protein
    À¯°ü¸·´Ü¹é
  • endogenous protein
    ³»ÀδܹéÁú
  • extracellular matrix protein
    ¼¼Æ÷¿Ü°£Áú´Ü¹é
  • protein-losing enteropathy
    ´Ü¹é¼Ò½ÇâÀÚº´Áõ
  • foreign protein
    ÀÌÁ¾´Ü¹é
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ
  • globular protein
    ±¸»ó´Ü¹é
  • protein granule
    ´Ü¹éÁú°ú¸³
  • heat-shock protein
    ¿­Ãæ°Ý´Ü¹é
  • heterologous protein
    ÀÌÁ¾´Ü¹é
  • iron binding protein
    ö°áÇմܹéÁú
  • protein bound iodine
    ´Ü¹éÁú°áÇÕ¿ä¿Àµå
  • mitogen-activated protein kinase
    ºÐ¿­Á¦È°¼º´Ü¹éŰ³ª¾ÆÁ¦
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • G protein
    G ´Ü¹é(Ó±ÛÜ)
  • G-myeloma protein
    ¸é¿ª±Û·ÎºÒ¸° G-°ñ¼öÁ¾´Ü¹éÁú
  • Heat shock protein
    ¿­¼ï´Ü¹éÁú
  • Integral membrane protein
    ÅëÇÕ(÷Öùê) ¸·´Ü¹é(Ø­Ó±ÛÜ)
  • M protein
    M´Ü¹éÁú
  • M protein
    M´Ü¹é.
  • NPN= non protein nitrogen
    ºñ´Ü¹éÁú¼Ò.
  • POMP (principal outer membrane protein)
    ÁÖ¿ä¿Ü¸·´Ü¹éÁú
  • PPD (purified protein derivatives)
    ÇÇÇǵð, Á¤Á¦´Ü¹éÁú·ù(À¯µµÃ¼)
  • PPD(Purified protein derivative) test
    PPD °Ë»ç.
  • Reiters protein
    ¶óÀÌÅÍ ¸Åµ¶Áø´Ü¿ë´Ü¹éÁú
  • S100 protein
    S100 ´Ü¹éÁú
  • actin-binding protein
    ¾×ƾ °áÇմܹé(¡­Ì¿ùêÓ±ÛÜ)
  • activated protein C inhibitor
    Ȱ¼ºÈ­´Ü¹éÁú C ¾ïÁ¦Á¦
  • activated protein C resistance
    Ȱ¼ºÈ­C´Ü¹é³»¼º
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • anion exchange protein
    À½À̿ ±³È¯ ´Ü¹é(ÎßüµÓ±ÛÜ)
  • antifreeze protein
    Ç×µ¿°á´Ü¹éÁú(ù÷ÔÐÌ¿ Ó±ÛÜòõ).
  • bacterial cell protein
    ±Õü´Ü¹é(Áú).
  • bactericidal permeability increasing protein(bpip)
    Bactericidal permeability increasing protein
  • bence-jones protein
    º¥½º-Á¸½º ´Ü¹é(¡­Ó±ÛÜ)
  • blood protein
    Ç÷¾×´Ü¹é(¡­Ó±ÛÜ).
  • body protein
    ü´Ü¹é(Áú)(ô÷Ó±ÛÜòõ).
  • c-Jun protein
    ¾¾-ÁØ ´Ü¹é(Ó±ÛÜ)
  • calcium-binding protein
    Ä®½· °áÇմܹé(Ì¿ùêÓ±ÛÜ)
  • cap binding protein
    ĸ°áÇմܹéÁú
  • carrier protein
    ¿î¹Ý´Ü¹éÁú
  • carrier protein
    ¿î¹Ý´Ü¹é(¡­Ó±ÛÜ)
  • catabolite activating protein
    ÀÌÈ­»ê¹° Ȱ¼ºÈ­´Ü¹éÁú
  • cellular retinol-binding protein
    ¼¼Æ÷³» ·¹Æ¼³î °áÇմܹé
  • chromatographic protein separation
    Å©·Î¸¶Åä±×·¡Çǹý ´Ü¹éºÐ¸®
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  • ¿µ¹®
    ÇѱÛ
  • A protein
    A ´Ü¹éÁú(Ó±ÛÜòõ)
  • azo-dye protein
    ¾ÆÁ¶»ö¼Ò ´Ü¹éÁú(ßäáÈÓ±ÛÜòõ)
  • Bence-Jones protein
    º¥½º-Á¸½º ´Ü¹éÁú(Ó±ÛÜòõ)
  • binding protein
    °áÇմܹéÁú(Ì¿ùêÓ±ÛÜòõ)
  • binding protein transport system
    °áÇÕ ´Ü¹éÁú ¼ö¼Û(Ì¿ùêÓ±ÛÜòõâÃáê) ½Ã½ºÅÛ
  • biotin carboxyl carrier protein
    ¹ÙÀÌ¿Àƾ Ä«¸£º¹½Ç ¿î¹Ý´Ü¹éÁú(ê¡ÚæÓ±ÛÜòõ)
  • blue copper protein
    ûµ¿ ´Ü¹éÁú(ôìÔÞÓ±ÛÜòõ)
  • blue protein
    û´Ü¹éÁú(ôìÓ±ÛÜòõ)
  • B protein
    B ´Ü¹éÁú(Ó±ÛÜòõ)
  • Ca2+-dependent regulatory protein
    Ca2+-ÀÇÁ¸(ëîðí) Á¶Àý´Ü¹éÁú(ðàï½Ó±ÛÜòõ)
  • calcium-dependent regulatory protein
    Ä®½·ÀÇÁ¸ Á¶Àý´Ü¹éÁú(ëîðíðàï½Ó±ÛÜòõ)
  • cAMP-dependent protein kinase
    cAMPÀÇÁ¸(ëîðí) ´Ü¹éÁú(Ó±ÛÜòõ) Ȱ¼ºÈ­È¿¼Ò(üÀàõûùý£áÈ)
  • carboxyl carrier protein
    Ä«¸£º¹½Ç ¿î¹Ý´Ü¹éÁú(ê¡ÚæÓ±ÛÜòõ)
  • carrier protein
    ¿î¹Ýü´Ü¹éÁú(ê¡Úæô÷Ó±ÛÜòõ)
  • catabolite activator protein
    īŸº¼¶óÀÌÆ® Ȱ¼ºÈ­ ´Ü¹éÁú(üÀàõûùÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
V-ONC viral oncogene
MAP malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ...
MBP major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl...
RP radial pulse; radiopharmaceutical; rapid processing [of film]; Raynaud phenomenon; reactive protein;...
ABP actin-binding protein; ambulatory blood pressure; American Board of Pedodontics; American Board of P...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
r-protein Ribosomal protein
SSB-protein Single-stranded DNA-binding protein
G protein binding protein
M protein monoclonal protein
G protein nucleotide-binding protein
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • hepatic protein
    °£ ´Ü¹é, °£ ´Ü¹éÁú
    °£ÀÇ ´Ü¹éÁú.
  • high protein diet
    °í´Ü¹é ½ÄÀÌ
  • membrane protein
    ¸· ´Ü¹éÁú
  • myotonin-protein kinase
    ¹Ì¿ÀÅä´Ñ-´Ü¹é Ű³ªÁ¦
  • pathologic plasma protein
    º´Àû Ç÷Àå ´Ü¹é
  • penicillin binding protein
    Æä´Ï½Ç¸° °áÇÕ ´Ü¹éÁú
  • perturbation of protein
    ´Ü¹éÁú º¯ÅÂ
  • plasma protein
    Ç÷Àå ´Ü¹é, Ç÷Àå ´Ü¹éÁú
    1. Ç÷Àå¿¡ Á¸ÀçÇÏ´Â ¿©·¯ Á¾·ùÀÇ ´Ü¹éÁú. ¿î¹Ý ´Ü¹éÁú
  • plasma protein binding
    Ç÷Àå ´Ü¹é °áÇÕ
  • protein
    ´Ü¹éÁú
  • protein bound radioactive iodine
    PBRI
  • protein hydrolysate
    ´Ü¹é ¼öÇØ¹°
    ´Ü¹éÁúÀ» »ê, ¾ËÄ®¸®, È¿¼Ò µîÀ¸·Î ºÐÇØÇÏ¿© »ý±â´Â ¾Æ¹Ì ³ë»êÀÇ È¥ÇÕ¹°·Î, À̰ÍÀ¸·Î ¾ò¾îÁö´Â Á¦Àç´Â ¾Æ¹Ì³ë»ê ¼ººÐÀ¸·Î º¼ ¶§, ¿ø·¡ÀÇ ¹°Áú°ú ¿µ¾çÇÐÀûÀ¸·Î µî°¡·Î¼­, º¸ÅëÀÇ ½ÄÀ̼º ´Ü¹éÀ» ¼·ÃëÇÏÁö ¸øÇϴ ȯÀÚ¿ë ¶Ç´Â Æ¯º°½ÄÀ¸·Î »ç¿ëµÈ´Ù.
  • protein polysaccharide
    ´Ü¹é ´Ù´ç·ù
  • protein-drug complex
    ´Ü¹é-¾à¹° º¹ÇÕü
  • protein-losing gastroenteropathy
    ´Ü¹é »ó½Ç¼º À§ÀåÁõ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
proto-oncogene proteins c-erbb-2 Cellular proteins in the epidermal growth factor receptor family encoded by the c-erbb genes. These proteins are overexpressed in a significant portion of adenocarcinomas found at various sites, especially in the breast. Gene amplification appears to be the predominant method leading to overexpression.
(12 Dec 1998)
proto-oncogene proteins c-fos Cellular DNA-binding proteins encoded by the c-fos genes (genes, fos). They are involved in growth-related transcriptional control. C-fos combines with c-jun (proto-oncogene proteins c-jun) to form a c-fos/c-jun heterodimer (transcription factor ap-1) that binds to the tre (tpa-responsive element) in promoters of certain genes.
(12 Dec 1998)
proto-oncogene proteins c-jun Cellular DNA-binding proteins encoded by the c-jun genes (genes, jun). They are involved in growth-related transcriptional control. There appear to be three distinct functions: dimerization (with c-fos), DNA-binding, and transcriptional activation. Oncogenic transformation can take place by constitutive expression of c-jun.
(12 Dec 1998)
proto-oncogene proteins c-kit Tyrosine kinase membrane receptors which are the natural ligands for mast cell growth factor (steel factor). This interaction is crucial for the development of haematopoietic, gonadal, and pigment stem cells.
(12 Dec 1998)
proto-oncogene proteins c-met <enzyme> A transmembrane tyrosine kinase that is the receptor for hepatocyte growth factor (scatter factor). It consists of an extracellular alpha chain which is disulfide linked to the transmembrane beta chain. The cytoplasmic portion contains the catalytic domain and critical sites for the regulation of kinase activity.
Registry number: EC 2.7.11.-
(12 Dec 1998)
proto-oncogene proteins c-mos Cellular proteins encoded by the c-mos genes (genes, mos). They function in the cell cycle to maintain maturation-promoting factor in the active state and have protein-serine/threonine kinase activity. Oncogenic transformation can take place when c-mos proteins are expressed at the wrong time.
(12 Dec 1998)
proto-oncogene proteins c-myc Cellular DNA-binding proteins encoded by the c-myc genes. They are normally involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Elevated and deregulated (constitutive) expression of c-myc proteins can cause tumourigenesis.
(12 Dec 1998)
proto-oncogene proteins c-raf <enzyme> A class of serine-threonine kinases involved in cellular signal transduction. Included in this class are the proto-oncogene proteins mil and raf. Raf is a component of a signal transduction pathway leading to increased gene expression through the c-jun DNA binding site, ap1.
Registry number: EC 2.7.10.-
(12 Dec 1998)
dominant oncogene <genetics, molecular biology, oncology> A gene that stimulates cell proliferation and can drastically increase the risk of cancer development when present in a single copy.
(09 Oct 1997)
immortalising oncogene <molecular biology> A gene that upon transfectionenables a primary cell to grow indefinitely in culture.
(09 Oct 1997)
oncogene <molecular biology, oncology> Mutated and/or overexpressed version of a normal gene of animal cells (the proto-oncogene) that in a dominant fashion can release the cell from normal restraints on growth and thus alone or in concert with other changes, convert a cell into a tumour cell.
(18 Nov 1997)
oncogene proteins Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (oncogene proteins, fusion).
(12 Dec 1998)
oncogene proteins, fusion The translation products of the fusion between an oncogene and another gene. The latter may be of viral or cellular origin.
(12 Dec 1998)
oncogene proteins v-abl Transforming proteins encoded by the abl oncogenes. Oncogenic transformation of c-abl to v-abl occurs by insertional activation that results in deletions of specific n-terminal amino acids.
(12 Dec 1998)
oncogene proteins v-erba Transforming proteins encoded by erba oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erba, the thyroid hormone receptor (receptors, thyroid hormone) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. V-erba acts as a dominant repressor of c-erba, inducing transformation by disinhibiting proliferation.
(12 Dec 1998)
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