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  • peripheral linear enhancement
    ¸»ÃÊ ¼±Çü Á¶¿µÁõ°­
  • peripheral lymphoid organs
    ¸»Ãʸ²ÇÁ°è ±â°ü.
  • peripheral lymphoid system
    ¸»Ãʸ²ÇÁ°è
  • peripheral microcystoid degeneration
    ÁÖº¯¼Ò³¶Æ÷º¯¼º
  • peripheral motor neuron
    ¸»Ãʿ¼º ½Å°æ¼¼Æ÷(¡­ê¡ÔÑàõãêÌèá¬øà).
  • peripheral motor neuron
    ¸»Ãʿ¼º ½Å°æ¼¼Æ÷(¡­ê¡ÔÑàõãêÌèá¬øà).
  • peripheral nerve
    ¸»ÃʽŰæ(ØÇ ãêÌè).
  • peripheral nerve
    ¸»ÃʽŰæ(ØÇôþãêÌè)
  • peripheral nerve block
    ¸»ÃʽŰæÂ÷´Ü.
  • peripheral nerve stimulator
    ¸»ÃʽŰæÀÚ±ØÀåÄ¡(¡­ô§Ð½íûöÇ).
  • peripheral nerve system
    ¸»ÃʽŰæ°è(¡­Í§).
  • peripheral nerve,axonal degeneration
    Ãà»èº¯¼º(õîÞþܨàõ)
  • peripheral nerve,compression
    ¾Ð¹Ú(äâÚÞ), °¡¾Ð(Ê¥äâ)
  • peripheral nervous system
    ¸»ÃʽŰæ°è
  • peripheral nervous system
    ¸»ÃʽŰæ°èÅë, ¸»ÃʽŰæ°è(ØÇ ãêÌèͧ).
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anti-PNM Ab anti-peripheral nerve myelin antibody
ASPVD atherosclerotic peripheral vascular disease
BZRP benzodiazepine receptor peripheral [type]
CSPINE corticosteroid use, seropositive RA, peripheral joint destruction, involvement of cervical nerves, n...
FPR false-positive rate; finger peripheral resistance; fluorescence photobleaching recovery; N-formylpep...
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IGFBPs Insulin-like growth factors and their binding proteins
KIFs Kinesin superfamily proteins
LMWP Low Molecular Weight Proteins
MIP-1 Macrophage inflammatory proteins-1
MP Membrane proteins
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 13 ÆäÀÌÁö: 4
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  • peripheral rim enhancement
    Å׵θ® Á¶¿µ Áõ°­
  • peripheral scotoma
    ÁÖº¯ ¾ÏÁ¡
    ÁÖ½ÃÁ¡¿¡¼­ ¸Ö¸® ¶³¾îÁö°í ½Ã¾ß ÁÖº¯À¸·Î ÇâÇÑ ½Ã°¢ ÀúÇÏ ºÎ.
  • peripheral sensation
    ¸»ÃÊ °¨°¢
  • peripheral sensory nerve
    ¸»ÃÊ °¨°¢ ½Å°æ
  • peripheral structure
    ¸»ÃÊ Á¶Á÷
  • peripheral sympathetic process
    ¸»ÃÊ ±³°¨ °úÁ¤
  • peripheral tabes
    ¸»Ãʼº ô¼ö·Î
  • peripheral tissue
    ¸»ÃÊ Á¶Á÷
  • peripheral vascular disease
    ¸»ÃÊÇ÷°ü Áúȯ
  • peripheral vascular system
    ¸»ÃÊÇ÷°ü°è
  • peripheral vein nutritional support
    ¸»ÃÊÁ¤¸Æ ¿µ¾ç ÁöÁö ¿ä¹ý
    Áï°¢ÀûÀÎ ÁöÁö ¿ä¹ýÀÌ ÇÊ¿äÇÏÁö¸¸ °æ±¸ ¿µ¾çÀÌ °¡´ÉÇϱâ±îÁö 1-2Á־ȿ¡ ÀÓ»óÀûÀÎ »óÅÂÀÇ Çâ»óÀÌ ±â´ëµÇ´Â ºñ±â´É¼º À§ Àå°üÀ» °¡Áø ȯÀÚ¿¡¼­ °¡Àå ÈçÈ÷ »ç¿ëµÈ´Ù. ¸»ÃÊÁ¤¸Æ ¿µ¾ç ÁöÁö ¿ä¹ýÀº Á¤¸Æ¼±À» ÅëÇØ Åõ¿©µÈ´Ù. ¿ë¾×Àº Ç×»ó Áö¹æ°ú Æ÷µµ´ç°ú ÇÔ²² ÀûÀýÇÑ ºñ´Ü¹éÁú ¿­·®À» °ø±ÞÇϱâ À§ÇÑ ¾Æ´Ï³ë»êÀ» Æ÷ÇÔÇÑ´Ù. ½É°¢ÇÑ ÇÕº´ÁõÀº µå¹°Áö¸¸ Á¤¸Æ¼±ÀÇ Ä§À±°ú Á¤¸Æ¿°ÀÇ ºóµµ°¡ ³ô´Ù.
  • peripheral vision
    ÁÖº¯ ½Ã
  • peripheral vocal cord paralysis
    ¸»Ãʼº ¼º´ë ¸¶ºñ
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bone morphogenetic proteins Non-collagenous factors, believed to be proteins, that occur in demineralised bone and stimulate osteogenesis. They can induce new bone formation in ectopic sites and thus have potential use in bone repair.
(12 Dec 1998)
calmodulin-binding proteins Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including f-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium atpases.
(12 Dec 1998)
capping proteins Proteins that bind to one end of actin filaments, preventing both addition and loss of actin monomers.
(05 Mar 2000)
vegetable proteins Proteins which are present in or isolated from vegetables or vegetable products used as food. The concept is distinguished from plant proteins which refers to non-dietary proteins from plants.
(12 Dec 1998)
ras proteins Small GTP-binding proteins encoded by ras genes (genes, ras) that play a critical role in normal cellular growth, differentiation, and development, and have the potential for malignant transformation. Two of the major ras proteins include the normal cellular form, proto-oncogene protein p21(ras), and the malignant form, oncogene protein p21(ras).
(12 Dec 1998)
recombinant fusion proteins Proteins that are the result of genetic engineering. A regulatory part or promoter of one or more genes is combined with a structural gene. The fusion protein is formed after transcription and translation of the fused gene. This type of fusion protein is used in the study of gene regulation or structure-activity relationships. They might also be used clinically as targeted toxins (immunotoxins).
(12 Dec 1998)
recombinant proteins Proteins prepared by recombinant DNA technology.
(12 Dec 1998)
carrier proteins Transport proteins that carry specific substances in the blood or across cell membranes.
(12 Dec 1998)
matrix proteins Proteins of the outer layer of the cell wall of gram-negative bacteria.
(18 Nov 1997)
viral core proteins Proteins found mainly in icosahedral DNA and RNA viruses. They consist of proteins directly associated with the nucleic acid inside the nucleocapsid.
(12 Dec 1998)
viral envelope proteins Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.
(12 Dec 1998)
viral fusion proteins Proteins, usually glycoproteins, found in the viral envelopes of a variety of viruses. They promote cell membrane fusion and thereby may function in the uptake of the virus by cells.
(12 Dec 1998)
viral matrix proteins Proteins associated with the inner surface of the lipid bilayer of the viral envelope. These proteins have been implicated in control of viral transcription and may possibly serve as the "glue" that binds the nucleocapsid to the appropriate membrane site during viral budding from the host cell.
(12 Dec 1998)
viral nonstructural proteins Viral proteins that are coded by nonstructural genes and usually have an unknown function. Some of these proteins may play structural roles within the infected cell during replication or act in virus regulation.
(12 Dec 1998)
viral proteins Proteins found in any species of virus.
(12 Dec 1998)
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