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"Glial Cell Line-Derived Neurotrophic Factor Receptors"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • racial factor
    ÀÎÁ¾¿äÀÎ
  • realization factor
    ½ÇÇöÀÎÀÚ
  • recruitment factor
    µ¿¿øÀÎÀÚ
  • reducing factor
    ȯ¿øÀÎÀÚ
  • reinforcing factor
    °­È­¿äÀÎ
  • relaxing factor
    ÀÌ¿ÏÀÎÀÚ
  • radiation weighting factor
    ¹æ»ç¼±°¡Áß°è¼ö
  • resistance factor
    ³»¼ºÀÎÀÚ, ÀúÇ×ÀÎÀÚ
  • resistance transfer factor
    ³»¼ºÀü´ÞÀÎÀÚ
  • reticuloendothelial depressant factor
    ±×¹°³»Çǰè¾ïÁ¦ÀÎÀÚ, ¸Á»ó³»Çǰè¾ïÁ¦ÀÎÀÚ
  • rheumatoid factor
    ·ù¸¶Æ¼½ºÀÎÀÚ
  • risk factor
    À§ÇèÀÎÀÚ
  • roentgen-to-rad conversion factor
    ·ÛÆ®°Õ´ë·¡µåº¯È¯°è¼ö
  • somatotropin release inhibiting factor
    ¼ºÀåÈ£¸£¸óºÐºñ¾ïÁ¦ÀÎÀÚ
  • spreading factor
    È®»êÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ
  • stroma factor
    ¹öÆÀÁúÀÎÀÚ
  • sunprotective factor
    Àϱ¤º¸È£Áö¼ö
  • testis-determining factor
    °íȯ°áÁ¤ÀÎÀÚ
  • therapeutic gain factor
    Ä¡·áÀ̵æ°è¼ö
  • thyrotrophin releasing factor
    ¹æÆÐ»ùÀÚ±ØÈ£¸£¸óÀ¯¸®ÀÎÀÚ, °©»ó»ùÀÚ±ØÈ£¸£¸óÀ¯¸®ÀÎÀÚ
  • time-dose factor
    ½Ã°£¼±·®ÀÎÀÚ
  • tissue factor
    Á¶Á÷ÀÎÀÚ
  • transfer factor
    Àü´ÞÀÎÀÚ
  • transforming growth factor
    Àüȯ¼ºÀåÀÎÀÚ
  • transmission factor
    Åõ°ú°è¼ö
  • tumor angiogenesis factor
    Á¾¾çÇ÷°üÇü¼ºÀÎÀÚ
  • tumor necrosis factor
    Á¾¾ç±«»çÀÎÀÚ
  • vascular endothelial growth factor
    Ç÷°ü³»ÇǼºÀåÀÎÀÚ
  • vascular permeability factor
    Ç÷°üÅõ°úÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • growth factor
    ¼ºÀå ÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ(à÷íþì×í­).
  • growth factor
    Áõ½ÄÀÎÀÚ
  • growth factor
    ¼ºÀå ÀÎÀÚ(à÷íþ ì×í­)
  • growth hormone-releasing factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®ÀÎÀÚ<--¹æÃâÀÎÀÚ>
  • growth promoting factor
    ¼ºÀåÃËÁøÀÎÀÚ(à÷íþõµòäì×í­), ¹ßÀ°ÃËÁø¹°Áú(Û¡ëÀõµòäÚªòõ)
  • hageman factor
    ÇϰԸ¸ ÀÎÀÚ, Hageman ÀÎÀÚ
  • hematopoietic growth factor
    Á¶Ç÷¼ºÀåÀÎÀÚ
  • hemorrhagic diathesis,clotting factor abnormalities
    ÀÀ°íÀÎÀÚ ÀÌ»ó
  • hepatocyte growth factor
    °£¼¼Æ÷¼ºÀåÀÎÀÚ
  • histamine sensitizing factor =HSF
    È÷½ºÅ¸¹Î°¨ÀÛÀÎÀÚ(¡­ÊïíÂì×í­).
  • homologous restriction factor
    µ¿Á¾Á¦ÇÑÀÎÀÚ
  • hyperglycemic glycogenolytic factor
    °íÇ÷´ç¼º ´ç¿øºÐÇØ(¼º) ÀÎÀÚ.
  • hypothalamic releasing factor
    ½Ã»óÇϺÎÀ¯¸®ÀÎÀÚ(ë¤×ãì×í­).
  • hypothalamic releasing factor
    ½Ã»óÇϺιæÃâÀÎÀÚ.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • cooperative factor
    Çùµ¿ÀÎÀÚ.
  • cord factor
    ±Õ»öÀÎÀÚ
  • cord factor
    ÄÚ¿Àµå ÀÎÀÚ(¡­ì×í­)
  • cord factor
    ÄÚ¿ÀµåÀÎÀÚ(¡­ì×í­).
  • coronary risk factor
    °ü(»ó)(µ¿¸Æ)ÁúȯÀ§Çè¿äÀÎ.
  • corticotropin-releasing factor =CRF
    ºÎ½ÅÇÇÁú ÀÚ±ØÈ£¸£¸ó ¹æÃâÀÎÀÚ(Üù ãìù«òõô§Ð½¡­Û¯õóì×í­).
  • cothromboplastin factor VII
    ÄÚÆ®·Òº¸ÇÃ¶ó½ºÆ¾.
  • coupling factor
    ¹è¿ìÀÎÀÚ.
  • covering factor
    ÇǺ¹ÀÎÀÚ(¡­ì×í­).
  • cytotoxic factor
    ¼¼Æ÷ µ¶¼º ÀÎÀÚ
  • decay-accelerating factor
    ºÐÇØÃËÁøÀÎÀÚ
  • decay-accelerating factor (DAF)
    ºØ±«ÃËÁøÀÎÀÚ
  • decay-accelerating factor(daf)
    Decay-accelerating factor(DAF)
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢À¯¹ßÀÎÀÚ.
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • Columnar epithelial cell
    ¿øÁÖ»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ¿øÁÖ»óÇǼ¼Æ÷
  • Columnar cell
    ¿øÁÖ¼¼Æ÷
    [¿¾ ¿ë¾î] ¿øÁÖ¼¼Æ÷
  • Type II hair cell
    ¿øÁÖÅм¼Æ÷
    [¿¾ ¿ë¾î] ÀüÆÄ¿¬Á¢¼¼Æ÷
  • Secretory cell of pyloric gland
    À§³¯¹®»ù¼¼Æ÷
    [¿¾ ¿ë¾î] À¯¹®¼±¼¼Æ÷
  • Secretory cell of cardiac gland
    À§µé¹®»ù¼¼Æ÷
    [¿¾ ¿ë¾î] ºÐ¹®¼±¼¼Æ÷
  • Gastrointestinal endocrine cell
    À§Ã¢ÀÚ³»ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] À§Ã¢ÀÚ³»ºÐºñ¼¼Æ÷
  • Synovial cell
    À±È°¼¼Æ÷
    [¿¾ ¿ë¾î] Ȱ¸·¼¼Æ÷
  • Principal cell
    À¸¶ä¼¼Æ÷
    [¿¾ ¿ë¾î] ÁÖ¼¼Æ÷
  • Pancreatic endocrine cell
    ÀÌÀÚ³»ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] ÃéÀå³»ºÐºñ¼¼Æ÷
  • Pancreatic acinar cell
    ÀÌÀڿܺкñ¼¼Æ÷
    [¿¾ ¿ë¾î] ÃéÀå¼±¼¼Æ÷
  • Cuboidal epithelial cell
    ÀÔ¹æ»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ÀÔ¹æ»óÇǼ¼Æ÷
  • Cuboidal cell
    ÀԹ漼Æ÷
    [¿¾ ¿ë¾î] ÀԹ漼Æ÷
  • Small cell part
    ÀÛÀº¼¼Æ÷ºÎºÐ
    [¿¾ ¿ë¾î] ¼Ò¼¼Æ÷ºÎ
  • Mucous cell
    Á¡¾×¼¼Æ÷
    [¿¾ ¿ë¾î] Á¡¾×¼¼Æ÷
  • Spermatogenic cell
    Á¤Àڹ߻ý¼¼Æ÷
    [¿¾ ¿ë¾î] Á¤Àڹ߻ý¼¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • antineuritic factor
    Ç׽Ű漺ÀÎÀÚ(ù÷ãêÌèàõì×í­)
  • antinuclear factor
    Ç×ÇÙÀÎÀÚ(ù÷ú·ì×í­)
  • antipellagra factor
    Ç×(ù÷)Æç¶ó±×¶ó ÀÎÀÚ(ì×í­)
  • antipeptic ulcer factor
    Ç×(ù÷)±Ë¾ç(Ï÷åË) ÀÎÀÚ(ì×í­)
  • antipernicious anemia factor
    Ç×(ù÷)¾Ç¼ººóÇ÷(äÂàõÞ¸úì) ÀÎÀÚ(ì×í­)
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ(ù÷ÎÕúìÜ»ì×í­)
  • antisigma factor
    Ç×(ù÷)½Ã±×¸¶ ÀÎÀÚ(ì×í­)
  • antispecificity factor
    Çׯ¯À̼º ÀÎÀÚ(ù÷÷åì¶àõì×í­)
  • antisterility factor
    Ç׺ÒÀÓ ÀÎÀÚ(ù÷ÝÕìõì×í­)
  • antitermination factor
    Ç×Á¾·á ÀÎÀÚ(ù÷ðûÖõì×í­)
  • antixerophthalmic factor
    Ç׾ȱ¸ °ÇÁ¶Áõ ÀÎÀÚ(ù÷äÑϹËëðÏñøì×í­)
  • Arrenius factor
    ¾Æ·¹´Ï¿ì½º ÀÎÀÚ(ì×í­)
  • asymmetry factor
    ºñ±¸»ó ÀÎÀÚ (ުϹßÒì×í­)
  • atrial natriuretic factor
    ½É¹æ(ãýÛ®) ³ªÆ®·ý¹è¼³ÀÎÀÚ(ÛÉàÜì×í­)
  • bacteriocin factor
    "¹ÚÅ׸®¿À½Å ÀÎÀÚ(ì×í­), »ì±ÕÀÎÀÚ(߯жì×í­)"
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
MCF macrophage chemotactic factor; median cleft face; medium corpuscular fragility; microcomplement fixa...
TRF T-cell replacing factor; thyrotropin-releasing factor; tubular rejection fraction
FDC factor-dependent cell [line]; follicular dendritic cell
ADCC cell Antibody Dependent Cellular(= Cell-Mediated) Cytotoxicity cell
HCG, hCG Human Chorionic Gonadotropin; »ç¶÷À¶¸ð¼º¼º¼±ÀÚ±ØÈ£¸£¸ó
  1. Placental Glycoprotein Hormone
&nbs...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
PTBR Peripheral-type benzodiazepine receptors
PR Progestin receptors
PRL-R Prolactin receptors
PAR Protease activated receptors
RACK Receptors for activated C kinase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • resistance factor
    ³»¼º ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
  • rheumsid factor
    ·ù¸¶Æ¼½º¾ç ÀÎÀÚ
  • risk factor
    À§Çè ¿äÀÎ, À§Çè ¿ä¼Ò, À§Çè ÀÎÀÚ
    °³ÀÎÀ̳ª ´Üü°¡ ÁúȯÀ̳ª Àå¾Ö¿¡ °É¸®±â ½±°Ô ÇÏ´Â ¿øÀÎÀÌ µÇ´Â ¿ä¼Ò·Î¼­ ¹Î°¨ÇÑ »ç¶÷µé¿¡¼­ ¹ß»ý ºóµµ¿Í Á¤µµ¸¦ Áõ°¡½ÃŲ´Ù.
  • safety factor
    ¾ÈÀü·ü
    ½Å°æ ¼¶À¯³ª ±Ù¼¶À¯ÀÇ ÈïºÐ Á¤µµ¿¡ À־ ÀÌ¹Ì ÈïºÐÇÑ °÷¿¡¼­, ¾ÆÁ÷ ÈïºÐÇϰí ÀÖÁö ¾ÊÀº ºÎºÐÀ¸·Î Àü·ù°¡ È帧À¸·Î½á ÈïºÐÀÌ ÀüµµÇϴµ¥, ÀÌ Àü·ù°¡ ½ÇÁ¦·Î ÈïºÐ½Ã۴µ¥ ÇÊ¿äÇÑ Àü·ù°ª.
  • self-associated rheumatoid factor complex

    self-care (ÀÚ°¡ Ä¡·á

  • sex factor
    ¼º ÀÎÀÚ
  • situational factor
    »óȲ ¿äÀÎ
  • socioeconomic factor
    »çȸ °æÁ¦Àû ¿äÀÎ
  • somatic factor
    ü¼º ¿äÀÎ
  • spreading factor
    È®»ê ÀÎÀÚ
  • systemic etiologic factor
    Àü½ÅÀû ¿øÀÎ ¿ä¼Ò
  • transfer factor
    Àü´Þ ÀÎÀÚ, ÀüÀÌ ¿äÀÎ
  • tumor necrosis factor
    Á¾¾ç ±«»ç ÀÎÀÚ
    TNF. Á¾¾ç¿¡ °ü°èÇϰí ÀÖ´Â ¸é¿ª°èÀÇ ¼¼Æ÷ÀÎ Á¾¾ç ħÀ±¼º ¸²ÇÁ±¸
  • tumor necrotizing factor
    Á¾¾ç ±«»ç ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
receptors, interleukin-6 <chemical> Receptors present on t cells, mitogen-activated B-cells, peripheral monocytes, and some macrophage- and B-cell-derived tumour cell types. The receptor is a strongly glycosylated protein of 80 kD and a length of 468 amino acids.
Pharmacological action: growth inhibitors.
(12 Dec 1998)
receptors, invertebrate peptide Cell surface receptors for invertebrate peptide hormones or neuropeptides.
(12 Dec 1998)
receptors, kainic acid Cell surface proteins that bind glutamate and directly gate ion channels. Kainic acid receptors were originally discriminated from other glutamate receptors by their affinity for the agonist kainic acid. Activation of kainic acid receptors is generally excitatory to cells. Subtypes have been cloned, and for some the traditional distinction from ampa receptors may not apply.
(12 Dec 1998)
receptors, laminin Glycoprotein molecules on the surface of cells that react with or bind to laminin whose function allows the binding of epithelial cells to the basement membrane. The molecular weight of this high-affinity receptor is 67 kD.
(12 Dec 1998)
receptors, ldl Receptors on the plasma membrane of nonhepatic cells that specifically bind ldl. The receptors are localised in specialised regions called coated pits. Hypercholesteraemia is caused by an allelic genetic defect of three types: 1) receptors do not bind to ldl; 2) there is reduced binding of ldl; and 3) there is normal binding but no internalization of ldl. In consequence, entry of cholesterol esters into the cell is impaired and the intracellular feedback by cholesterol on 3-hydroxy-3-methylglutaryl CoA reductase is lacking.
(12 Dec 1998)
receptors, leukocyte-adhesion Family of proteins associated with the capacity of leukocytes, including lymphocytes, monocytes, and neutrophils, to adhere to each other and to certain substrata, e.g., the c3bi component of complement. Members of this family are the lymphocyte function-associated antigen-1 (lfa-1), the macrophage-1 antigen (mac-1), and the antigen p150,95 or p150,95 leukocyte adhesion protein. They all share a common beta-subunit which is the CD18 antigen. All three of the above antigens are absent in inherited leukocyte-adhesion deficiency syndrome, which is characterised by recurrent bacterial infections, impaired pus formation, and wound healing as well as abnormalities in a wide spectrum of adherence-dependent functions of granulocytes, monocytes, and lymphoid cells.
(12 Dec 1998)
receptors, leukotriene Cell-surface receptors that bind leukotrienes with high affinity and trigger intracellular changes influencing the behaviour of cells. The leukotriene receptor subtypes have been tentatively named according to their affinities for the endogenous leukotrienes ltb4, ltc4, ltd4, and lte4.
(12 Dec 1998)
receptors, leukotriene b4 A class of cell surface leukotriene receptors with a preference for leukotriene b4. Leukotriene b4 receptor activation influences chemotaxis, chemokinesis, adherence, enzyme release, oxidative bursts, and degranulation in polymorphonuclear leukocytes. There are at least two subtypes of these receptors. Some actions are mediated through the inositol phosphate and diacylglycerol second messenger systems.
(12 Dec 1998)
receptors, lh Those protein complexes or molecular sites on the surfaces and cytoplasm of gonadal cells that bind luteinizing or chorionic gonadotropic hormones and thereby cause the gonadal cells to synthesise and secrete sex steroids. The hormone-receptor complex is internalised from the plasma membrane and initiates steroid synthesis.
(12 Dec 1998)
receptors, lhrh Receptors with a 6-kD protein on the surfaces of cells that secrete lh or fsh, usually in the adenohypophysis. Lhrh binds to these receptors, is endocytosed with the receptor and, in the cell, triggers the release of lh or fsh by the cell. These receptors are also found in rat gonads. Inhibin prevents the binding of gnrh to its receptors.
(12 Dec 1998)
receptors, lipoprotein Cell surface proteins that bind lipoproteins with high affinity. Lipoprotein receptors in the liver and peripheral tissues mediate the regulation of plasma and cellular cholesterol metabolism and concentration. The receptors generally recognise the apolipoproteins of the lipoprotein complex, and binding is often a trigger for endocytosis.
(12 Dec 1998)
receptors, lymphocyte homing Cell surface glycoproteins on lymphocytes and other leukocytes that mediate adhesion to specialised blood vessels called high endothelial venules. Several different classes of lymphocyte homing receptors have been identified, and they appear to target different surface molecules (addressins) on high endothelial venules in different tissues. The adhesion plays a crucial role in the trafficking of lymphocytes.
(12 Dec 1998)
receptors, metabotropic glutamate Cell surface proteins that bind glutamate and act through g-proteins to influence second messenger systems. Several types of metabotropic glutamate receptors have been cloned. They differ in pharmacology, distribution, and mechanisms of action.
(12 Dec 1998)
receptors, mineralocorticoid Cytoplasmic proteins that specifically bind mineralocorticoids and mediate their cellular effects. The receptor with its bound ligand acts in the nucleus to induce transcription of specific segments of DNA. Mineralocorticoids were named for their actions on extracellular electrolyte concentrations. The most important example is aldosterone.
(12 Dec 1998)
receptors, mitogen Glycoprotein molecules on the surface of b- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
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    ÇѱÛ
    ÇÑÀÚ
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    ÇÑÀÚ
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KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 9
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