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"Membrane Fusion Proteins"¿¡ ´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
  • membrane stabilizer
    ¸·¾ÈÁ¤Á¦
  • membrane-derived oligosaccharide
    ¼¼Æ÷¸·À¯·¡¼Ò´ç·ù, ¼¼Æ÷¸·À¯·¡¿Ã¸®°í´ç·ù
  • neovascular membrane
    ½Å»ýÇ÷°ü¸·
  • nictitating membrane
    ±ô¹ÚÀÓ¸·, ¼ø¸·(âëØ¯)
  • nuclear membrane
    ÇÙ¸·
  • olfactory membrane
    Èİ¢Á¡¸·
  • oncospheral membrane
    ¿©¼¸°¥°í¸®À¯Ã渷, À°±¸À¯Ã渷
  • oronasal membrane
    ÀÔÄÚ¸·, ±¸ºñ¸·
  • oropharyngeal membrane
    ÀÔÀεθ·, ±¸Àεθ·
  • obturator membrane
    Æó¼â¸·
  • otolithic membrane
    ÆòÇü¸ð·¡¸·, À̼®¸·
  • ovular membrane
    ³­È²¸·
  • placental membrane
    Źݸ·
  • plasma membrane
    ÇüÁú¸·
  • platelet demarcation membrane
    Ç÷¼ÒÆÇ±¸È¹¸·
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  • ¿µ¹®
    ÇѱÛ
  • membrane stabilizer
    ¸·¾ÈÁ¤Á¦
  • membrane transport
    ¸·¿î¹Ý
  • membrane control protein
    ¸·Á¶Àý´Ü¹é
  • membrane-derived oligosaccharide
    ¼¼Æ÷¸·À¯·¡¼Ò´ç·ù
  • mucous membrane
    Á¡¸·, Á¡¸·Ãþ
  • neovascular membrane
    ½Å»ýÇ÷°ü¸·
  • nictitating membrane
    ±ô¹Ú´«²¨Ç®
  • nuclear membrane
    ÇÙ¸·
  • obturator membrane
    Æó¼â¸·
  • olfactory membrane
    Èİ¢Á¡¸·
  • oncospheral membrane
    ¿©¼¸°¥°í¸®À¯Ã渷, À°±¸À¯Ã渷
  • oronasal membrane
    ÀÔÄÚ»çÀ̸·
  • oropharyngeal membrane
    ÀÔÀεθ·
  • otolithic membrane
    ÆòÇü¸ð·¡¸·
  • ovular membrane
    (¢¡vitelline membrane) ³­È²¸·
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  • ¿µ¹®
    ÇѱÛ
  • placental membrane
    Źݸ·(¡­Ø¯).
  • plamsa membrane
    ¿øÇüÁú¸·(ê«û¡òõد)
  • plasma membrane
    ÇüÁú¸·
  • plasma membrane
    ¿øÇüÁú¸·(ê«û¡òõد), ¼¼Æ÷ÇüÁú¸·(á¬øàû¡òõد).
  • plasma membrane
    ÇüÁú¸·
  • plasma membrane
    ¿øÇüÁú¸·
  • plasma membrane
    ¿øÇüÁú¸·(ê«û¡òõد), ¼¼Æ÷ÇüÁú¸·(á¬øàû¡òõد).
  • plasma membrane of erythrocyte
    ÀûÇ÷±¸ÇüÁú¸·
  • platelet demarcation membrane
    Ç÷¼ÒÆÇ±¸È¹¸·(¡­Ï¡üñد).
  • platelet demarcation membrane
    Ç÷¼ÒÆÇ
  • pleuropericardial membrane
    °¡½¿¸·½ÉÀ帷¸·
  • pleuropericardial membrane
    È丷½É¸·(ýØØ¯ãýد)
  • pleuroperitoneal membrane
    °¡½¿¸·º¹¸·¸·
  • posterior atlanto-occipital membrane
    µÚȯÃßÈĵθ·, ÈÄȯÃßÈĵθ·(ý­ü»õÐý­Ô騝)
  • posterior atlanto-occipital membrane
    µÚ°í¸®µÚÅë¼ö¸·
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  • ¿µ¹®
    ÇѱÛ
  • artificial membrane
    Àΰø¸·(Àΰø¸·).
  • atlanto-occipital membrane
    ȯÃßÈĵθ· (ü»õÐý­Ô騝).
  • bacterial cell membrane
    ¼¼±Õ¼¼Æ÷¸·
  • basal membrane of semicircular canal
    ¹Ý±Ô°ü±âÀú¸·, ¹Ý°í¸®°ü¹Ù´Ú¸·
  • basal membrane of semicircular duct
    ¹Ý°í¸®°ü¹Ù´Ú¸·, ¹Ý±Ô°ü±âÀú¸·(ÚâЮηÐñî¼?
  • basal membrane of semicircular duct
    ¹Ý°í¸®°ü¹Ù´Ú¸·
  • basement membrane
    ±âÀú¸·(¡­Ø¯)
  • basement membrane
    ¹Ù´Ú¸·
  • basement membrane antigen
    ±âÀú¸· Ç׿ø
  • basement membrane dystrophy
    ±âÀú¸·ÀÌ¿µ¾ç(Áõ)
  • basement membrane zone
    ±âÀú¸·(Ðñî¼Ø¯) ´ë(Óá)
  • basement membrane= basal laminar
    ±âÀú¸·(Ðñî¼Ø¯)
  • basilar membrane
    ±âÀú¸·
  • basilar membrane
    ¹Ù´ÚÆÇ
  • basolateral membrane
    ±âÀúÃø¸·(Ðñî¼ö°Ø¯)
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    ÇѱÛ
  • Bowman`s membrane
    ¾Õ°æ°èÆÇ
    [¿¾ ¿ë¾î] Àü°æ°èÆÇ(Bowman¸·)
  • Anterior atlanto-occipital membrane
    ¾Õ°í¸®µÚÅë¼ö¸·
    [¿¾ ¿ë¾î] ÀüȯÃßÈĵθ·
  • Continuous basement membrane
    ¿¬¼Ó¹Ù´Ú¸·
    [¿¾ ¿ë¾î] ¿¬¼Ó¼º±âÀú¸·
  • Presynaptic membrane
    ¿¬Á¢ÀÌÀü¸·
    [¿¾ ¿ë¾î] ¿¬Á¢Àü¸·
  • Postsynaptic membrane
    ¿¬Á¢ÀÌÈĸ·
    [¿¾ ¿ë¾î] ¿¬Á¢Èĸ·
  • Fold of postsynaptic membrane
    ¿¬Á¢ÀÌÈĸ·ÁÖ¸§
    [¿¾ ¿ë¾î] ÈÄ¿¬Á¢ÁÖ¸§
  • Superior synovial membrane
    À§À±È°¸·
    [¿¾ ¿ë¾î] »óȰ¾×¸·
  • Vitreous membrane
    À¯¸®Ã¼¸·
    [¿¾ ¿ë¾î] ÃÊÀÚü¸·
  • Synovial membrane [Synovial layer]
    À±È°¸·
    [¿¾ ¿ë¾î] Ȱ¾×¸·
  • Oropharyngeal membrane
    ÀÔÀεθ·
    [¿¾ ¿ë¾î] ±¸°­Àεθ·
  • Oropharyngeal[Buccopharyngeal] membrane
    ÀÔÀεθ·
    [¿¾ ¿ë¾î] ±¸°­Àεθ·
  • Oronasal membrane
    ÀÔÄÚ»çÀ̸·
    [¿¾ ¿ë¾î] ±¸ºñ¸·
  • Plasma membrane of erythrocyte
    ÀûÇ÷±¸ÇüÁú¸·
    [¿¾ ¿ë¾î] ÀûÇ÷±¸ÇüÁú¸·
  • Mucous membrane
    Á¡¸·Ãþ
    [¿¾ ¿ë¾î] Á¡¸·
  • Crural interosseous membrane
    Á¾¾Æ¸®»À»çÀ̸·
    [¿¾ ¿ë¾î] ÇÏÅð°ñ°£¸·
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TBM total body mass; tracheobronchiomegaly; trophoblastic basement membrane; tuberculous meningitis; tub...
TM technology management; tectorial membrane; temperature by mouth; temporalis muscle; temporomandibula...
BM   1) Bone Marrow
  2) Basement Membrane
  3) Bench-Mark; ¼öÁØ ±âÇ¥...
BMZ Basement Membrane Zone
ECMO Extra-Corporeal Membrane Oxygenation
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 6
FnBP Fibronectin binding proteins
Hsp Heat shock or stress proteins
hsp Heat stress proteins
HMG High mobility group proteins
HABP Hyaluronan-binding proteins
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 6
viral tail proteins Proteins found in the tail sections of DNA and RNA viruses. It is believed that these proteins play a role in directing chain folding and assembly of polypeptide chains.
(12 Dec 1998)
cell cycle proteins Proteins that control the cell division cycle. This family of proteins includes a wide variety of classes, including cyclin-dependent kinases, mitogen-activated kinases, cyclins, and phosphoprotein phosphatases (phosphoprotein phosphatase) as well as their putative substrates such as chromatin-associated proteins, cytoskeletal proteins, and transcription factors.
(12 Dec 1998)
glue proteins, drosophila Glycosylated proteins which are part of the salivary glue that drosophila larvae secrete as a means of fixing themselves to an external substrate for the duration of the pre-pupal and pupal period. The proteins which consist of at least eight polypeptides are encoded in the third larval instar by the sgs-3, sgs-4, sgs-7 and sgs-8 genes.
(12 Dec 1998)
repressor proteins Proteins which are normally bound to the operator locus of an operon, thereby preventing transcription of the structural genes. In enzyme induction, the substrate of the inducible enzyme binds to the repressor protein, causing its release from the operator and freeing the structural genes for transcription. In enzyme repression, the end product of the enzyme sequence binds to the free repressor protein, the resulting complex then binds to the operator and prevents transcription of the structural genes.
(12 Dec 1998)
cerebrospinal fluid proteins Proteins in the cerebrospinal fluid, normally albumin and globulin present in the ratio of 8 to 1. Increases in protein levels are of diagnostic value in neurological diseases. (brain and bannister's clinical neurology, 7th ed, p221)
(12 Dec 1998)
retroviridae proteins Proteins from the family retroviridae. The most frequently encountered member of this family is the rous sarcoma virus protein.
(12 Dec 1998)
retroviridae proteins, oncogenic Retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukaemias, lymphomas, and mammary carcinomas. Not all retroviral proteins are oncogenic.
(12 Dec 1998)
chimeric proteins Proteins in individuals that are derived from genetically different zygotes.
(12 Dec 1998)
peripheral proteins Pathways that can be easily removed from a biomembrane (e.g., by altering the pH or the ionic strength).
Synonym: extrinsic proteins.
(05 Mar 2000)
periplasmic binding proteins Transport proteins located within the periplasmic space. Some act as receptors for bacterial chemotaxis, interacting with MCPs. Their mode of action is unclear.
(18 Nov 1997)
ribosomal proteins Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.
(12 Dec 1998)
growth associated proteins <growth factor> Group of developmentally regulated polypeptides thought to be critical for the formation of neural circuitry. The acidic membrane phosphoprotein GAP 43 is synthesised and transported down regenerating and developing axons, pp46 localised in growth cone membranes during embryogenesis, B 50 in mature presynaptic membranes in the regulation of phosphotidylinositol turnover and F1 in the hippocampus during long-term potentiation, are now all known to be the same protein.
(18 Nov 1997)
RNA-binding proteins Proteins which bind to RNA molecules. Certain structure motifs are common to several of the proteins, such as arginine (arg)-rich tracts, typically consisting of alternating arg-asp, arg-ser, or arg-gly residues. These proteins also tend to have a common ribonucleotide sequence domain.
(12 Dec 1998)
cholesterol ester transport proteins A protein that transports cholesterol esters from HDL to VLDL and LDL; a deficiency of this protein is associated with elevated HDL cholesterol.
(05 Mar 2000)
chromosomal proteins, non-histone Nucleoproteins which in contrast to histones are acid insoluble. They are involved in chromosomal functions; e.g. They bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens.
(12 Dec 1998)
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