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"membrane 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
  • fenestrated elastic membrane
    ⟷¸·
  • fertilization membrane
    ¼öÁ¤¸·
  • fetal membrane
    žƸ·
  • fibroelastic membrane
    ¼¶À¯Åº·Â¸·
  • fibrous membrane
    ¼¶À¯¸·
  • glassy membrane
    À¯¸®Áú¸·
  • glial limiting membrane
    ¾Æ±³°æ°è¸·, ±³¼¼Æ÷°æ°è¸·
  • hemoendothelial membrane
    Ç÷¾×³»ÇǸ·
  • hyaline membrane
    À¯¸®Áú¸·
  • hyaline membrane disease
    À¯¸®Áú¸·º´
  • hyaloid membrane
    À¯¸®Ã¼¸·
  • ion-exchange membrane
    À̿±³È¯¸·
  • iridopupillary membrane
    ȫ䵿°ø¸·
  • intercostal membrane
    °¥ºñ»çÀ̸·, ´Á°£¸·
  • interosseous membrane
    »À»çÀ̸·, °ñ°£¸·
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • elastic membrane
    ź·Â¸·
  • enamel membrane
    »ç±âÁú¸·
  • excitable membrane
    ÈïºÐ¸·
  • exocoelomic membrane
    ü°­¹Û¸·
  • extracorporeal membrane oxygenation
    ü¿Ü¸·Çü»ê¼Ò¼·Ãë
  • membrane equilibrium
    ¸·ÆòÇü
  • fenestrated elastic membrane
    ⟷¸·
  • fertilization membrane
    ¼öÁ¤¸·
  • fibroelastic membrane
    ¼¶À¯Åº·Â¸·
  • fibrous membrane
    ¼¶À¯¸·
  • membrane filter
    ¸·°Å¸£°³, ¸·ÇÊÅÍ
  • glassy membrane
    À¯¸®¸·
  • glial limiting membrane
    ¾Æ±³°æ°è¸·
  • hemochorial membrane
    Ç÷¾×À¶¸ð¸·
  • hemodichorial membrane
    Ç÷¾×µÎ°ãÀ¶¸ð¸·
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • glomerular membrane
    »ç±¸Ã¼¸·(¡­Ø¯).
  • glomerular membrane
    »ç±¸Ã¼¸·.
  • hemochorial membrane
    Ç÷¾×À¶¸ð¸·
  • hemodichorial membrane
    Ç÷¾×µÎ°ãÀ¶¸ð¸·
  • hemoendothelial membrane
    Ç÷¾×³»ÇÇ»çÀ̸·
  • hemomonochorial membrane
    Ç÷¾×Ȭ°ãÀ¶¸ð¸·
  • hemotrichorial membrane
    Ç÷¾×¼¼°ãÀ¶¸ð¸·
  • homogeneous membrane
    ±ÕÁú¸·(гòõد) ŹÝÀ¶¸ð¸¦ ½Î°í ÀÖ´Â °Í .
  • hyaloid membrane
    À¯¸®Ã¼¸·, ÃÊÀÚü¸·(õ¦í­ô÷د).
  • hyaloid membrane
    À¯¸®Ã¼¸·
  • hyothyroid membrane
    °©»ó¼³°ñ¸·, ¼³°ñ°©»ó¸·(àßÍéË£ßÒØ¯).
  • hyothyroid membrane
    °©»ó¼³°ñ¸·, ¼³°ñ°©»ó¸·
  • inferior synovial membrane
    ¾Æ·¡À±È°¸·
  • injuries of the tympanic membrane
    °í¸·¼Õ»ó
  • inner acrosomal membrane
    ¼Ó÷´Üü¸·
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • basilar membrane
    ¹Ù´ÚÆÇ
  • basolateral membrane
    ±âÀúÃø¸·(Ðñî¼ö°Ø¯)
  • bowmans membrane
    ¾Õ°æ°èÆÇ
  • branches to tympanic membrane
    °í¸·°¡Áö
  • bruchs membrane
    ¹Ù´Úº¹ÇÕÃþ
  • bucconasal membrane
    ±¸ºñ¸·
  • buccopharyngeal membrane
    ÇùÀεθ·(úúìÖÔ騝).
  • cell membrane
    ¼¼Æ÷¸·
  • cell membrane
    ¼¼Æ÷¸·(á¬øàØ¯)
  • cell membrane
    ¼¼Æ÷¸·
  • cell membrane permeability
    ¼¼Æ÷¸·Åõ°ú¼º(á¬øàØ¯÷âΦàõ).
  • cellular membrane
    ¼¼Æ÷¼º¸·
  • cellulose membrane
    ¼¿·ê·Î½º¸·
  • chorioallantoic membrane
    À¶¸ð¿ä¸·
  • chorioallantoic membrane
    À¶¸ð¸·¿ä¸·.
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • Posterior atlanto-occipital membrane
    µÚ°í¸®µÚÅë¼ö¸·
    [¿¾ ¿ë¾î] ÈÄȯÃßÈĵθ·
  • Stapedial membrane
    µîÀÚ¸·
    [¿¾ ¿ë¾î] µî°ñ¸·
  • External intercostal membrane
    ¹Ù±ù°¥ºñ»çÀ̸·
    [¿¾ ¿ë¾î] ³úÃø°£¸·
  • External intercostal membrane
    ¹Ù±ù°¥ºñ»çÀ̸·
    [¿¾ ¿ë¾î] ¿Ü´Á°£¸·
  • Outer limiting membrane
    ¹Ù±ù°æ°èÃþ
    [¿¾ ¿ë¾î] ¿Ü°æ°èÃþ
  • External mitochondrial membrane
    ¹Ù±ù»ç¸³Ã¼¸·
    [¿¾ ¿ë¾î] »ç¸³Ã¼¿Ü¸·
  • External glial limiting membrane
    ¹Ù±ù¾Æ±³°æ°è¸·
    [¿¾ ¿ë¾î] ¿Ü±³°æ°è¸·
  • External acrosomal membrane
    ¹Ù±ù÷´Üü¸·
    [¿¾ ¿ë¾î] ÷´Üü¿Ü¸·
  • Outer acrosomal membrane
    ¹Ù±ù÷´Üü¸·
    [¿¾ ¿ë¾î] ¿Ü÷´Üü¸·
  • External elastic membrane
    ¹Ù±ùź·Â¸·
    [¿¾ ¿ë¾î] ¿Üź·Â¸·
  • External nuclear membrane
    ¹Ù±ùÇÙ¸·
    [¿¾ ¿ë¾î] ¿ÜÇÙ¸·
  • Basement membrane
    ¹Ù´Ú¸·
    [¿¾ ¿ë¾î] ±âÀú¸·
  • Bruch`s membrane
    ¹Ù´Úº¹ÇÕÃþ
    [¿¾ ¿ë¾î] ±âÀúº¹ÇÕü
  • Basilar membrane
    ¹Ù´ÚÆÇ
    [¿¾ ¿ë¾î] ±âÀúÆÇ
  • Basilar membrane
    ¹Ù´ÚÆÇ
    [¿¾ ¿ë¾î] ³ª¼±¸·
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  • ¿µ¹®
    ÇѱÛ
  • membrane fluidity
    ¸·À¯µ¿¼º(د׵ÔÑàõ)
  • membrane hydrolysis
    ¸·°¡¼öºÐÇØ(دʥâ©ÝÂú°)
  • membrane mimetic chemistry
    À¯»ç(×¾ÞÄ) ¸·È­ÇÐ(دûùùÊ)
  • membrane osmometer
    ¸·»ïÅõ°è(د߶÷âͪ)
  • membrane resistance
    ¸·ÀúÇ×(دî½ù÷)
  • membrane potential
    ¸·ÀüÀ§(دï³êÈ)
  • membrane structure
    ¸·±¸Á¶(دϰðã)
  • membrane transport
    ¸·À̵¿(دì¹ÔÑ)
  • membrane trigger hypothesis
    ¸·À¯¹ß¼³(دë¯Û¡àã)
  • mucous membrane
    Á¡¾×¸·(ïÄäûد)
  • outer membrane
    ¿Ü¸·(èâØ¯)
  • permselective membrane
    ¼±ÅÃÅõ°ú¸·(àÔ÷É÷âΦد)
  • plasma membrane
    ¿øÇüÁú¸·(ê«û¡òõد)
  • precipitation membrane
    ħÀü¸·(öØîþد)
  • protoplast membrane
    ¿øÇüÁúü¸·(د)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
PBM peak bone mass; peripheral basement membrane; peripheral blood mononuclear [cell]; placental basemen...
PHM peptide histidine methionine; peptidylglycine alpha-hydroxylating monooxygenase; posterior hyaloid m...
PM after death (Lat. post mortem); after noon [Lat. post meridiem]; mean pressure; pacemaker; pantomogr...
SM Master of Science; sadomasochism; self-monitoring; silicon microphysiometer; simple mastectomy; skim...
TBM total body mass; tracheobronchiomegaly; trophoblastic basement membrane; tuberculous meningitis; tub...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
ECM Extracellular matrix proteins
FnBP Fibronectin binding proteins
Hsp Heat shock or stress proteins
hsp Heat stress proteins
HMG High mobility group proteins
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • membrane protein
    ¸· ´Ü¹éÁú
  • membrane stabilizing
    ¸· ¾ÈÁ¤¼ºÀÇ
  • membrane type
    ¸·Çü
  • mucous membrane congestion
    Á¡¸· ÃæÇ÷
  • mucous membrane of palate
    ±¸°³ Á¡¸·
  • nasal mucous membrane
    ÄÚ Á¡¸·, ºñ Á¡¸·
  • neovascular membrane
    ½Å»ý Ç÷°ü ¸·
  • neuronal cell membrane
    ´º¿ì·± ¼¼Æ÷¸·
  • nictitating membrane
    ±ô¹Ú ´«²¨Ç®, ´« ±ô¹Ú¸·
  • nitrocellulose membrane
    ´ÏÆ®·Î ¼¿·ê·Î½º ¸·
  • oropharyngeal membrane
    ÀÔ Àεθ·
  • otolithic membrane
    ÆòÇü ¸ð·¡¸·
  • palatine membrane
    ±¸°³¸·
  • peri-implant membrane
    À̽Ű ÁÖÀ§¸·
  • pericolic membrane syndrome
    °áÀåÁÖÀ§ Á¡¸· ÁõÈıº
    °áÀå ÁÖÀ§¸·ÀÇ ¾Ð·ÂÀ¸·Î ¸¸¼º Ãæ¼ö¿°°ú À¯»çÇÑ Áõ»óÀÌ ³ªÅ¸³ª´Â ÁúȯÀÌ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
viral regulatory proteins Proteins which regulate the rate of transcription of viral structural genes.
(12 Dec 1998)
viral structural proteins Viral proteins that do not regulate transcription. They are coded by viral structural genes and include nucleocapsid core proteins (gag proteins), enzymes (pol proteins), and membrane components (env proteins). Transcription of viral structural genes is regulated by viral regulatory proteins.
(12 Dec 1998)
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)
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