| ¿µ¹® | protein | ÇÑ±Û | ´Ü¹éÁú |
|---|---|---|---|
| ¼³¸í | ź¼Ò, ¼ö¼Ò, »ê¼Ò, Áú¼Ò, ȲÀ» ÇÔÀ¯Çϰí ÀÖ´Â À¯±âÈÇÕ¹°·Î, ¸ðµç ¼¼Æ÷ÀÇ ¿øÇüÁúÀ» ÀÌ·ç°í ÀÖ´Â ±âº» ±¸¼º¹°ÁúÀÌ´Ù. ´Ü¹éÁúÀº ±× ´ÜÀ§ÀÎ ¾Æ¹Ì³ë»êµéÀÌ ÆéƼµå°áÇÕ¿¡ ÀÇÇØ °áÇյǾî ÀÖÀ¸¸ç, º¸Åë 20°³ÀÇ ¾Æ¹Ì³ë»êµéÀÌ ´Ù¸¥ ¼ø¼¿Í Á¶¼ºÀ» °¡Áö°í ¹è¿µÇ¾î, µ¶Æ¯ÇÑ ÇϳªÀÇ ´Ü¹éÁúÀ» Çü¼ºÇÏ°Ô µÈ´Ù. |
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| ¿µ¹® | receptor | ÇÑ±Û | ¼ö¿ëü |
|---|---|---|---|
| ¼³¸í | ¼¼Æ÷Áú³» ¶Ç´Â ¼¼Æ÷Ç¥¸é¿¡ Á¸ÀçÇÏ´Â ºÐÀÚ±¸Á¶·Î¼ ƯÀ̹°Áú°ú ¼±ÅÃÀûÀ¸·Î °áÇÕÇÏ¸ç °áÇÕ¿¡ ÀÇÇØ ƯÀÌÇÑ »ý¸®Àû ÀÛ¿ëÀ» ³ªÅ¸³½´Ù. ÆéƼµåÈ£¸£¸ó, ½Å°æÀü´Þ¹°Áú, Ç׿ø, º¸Ã¼, ¸é¿ª±Û·ÎºÒ¸°¿¡ ´ëÇÑ ¼¼Æ÷Ç¥¸é ¼ö¿ëü¿Í ½ºÅ×·ÎÀ̵忡 ´ëÇÑ ¼¼Æ÷Áú³» ¼ö¿ëü°¡ ÀÖ´Ù. |
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| ¿µ¹® | insulin | ÇÑ±Û | Àν¶¸° |
|---|---|---|---|
| ¼³¸í | ÀÌÀÚ ¶û°ÖÇѽº¼¶ÀÇ B¼¼Æ÷°¡ ÇÕ¼º-ºÐºñÇϴ ȣ¸£¸ó ´Ü¹éÁú, Æ÷µµ´çÀ» ±Û¸®ÄÚ°ÕÀ¸·Î ¹Ù²Ù´Â È£¸£¸ó´Ü¹éÁú·Î, ºÐÀÚ·®Àº 5,807ÀÌ´Ù. Ç÷ÁßÀÇ ´ç³óµµ »ó½ÂÀ¸·Î ÀÎÇÏ¿© ºÐºñ°¡ ÃËÁøµÈ´Ù. ±ÙÀ°-Áö¹æÁ¶Á÷-°£ µî Ç¥Àû¼¼Æ÷ÀÇ ¼ö¿ëü ´Ü¹éÁú°ú °áÇÕÇÏ¿© Á¤º¸¸¦ ¼¼Æ÷³»·Î Àü´ÞÇÔÀ¸·Î½á Ç÷¾× Áß¿¡¼ ´ç, ÁöÁú, ¾Æ¹Ì³ë»ê ´ë»ç¸¦ Á¶ÀýÇÑ´Ù. ´çÀÇ Á¶Á÷¿¡ ¹Þ¾Æµå¸®´Â °ÍÀ» ÃËÁøÇÏ¿© Ç÷´çÀ» ÀúÇϽÃŲ´Ù. »ý¼º-ºÐºñ·® ÀúÇÏ, Á¶Á÷¼¼Æ÷ÀÇ ¼ö¿ëü ºÎÁ·Àº °íÇ÷´çÀÇ ¿øÀÎÀÌ µÈ´Ù. ¶ÇÇÑ ¾Æ¹Ì³ë»êÀÇ Èí¼ö¿Í ´Ü¹éÁú, Áö¹æÀÇ ÇÕ¼ºÀ» ÃËÁøÇϸç Áö¹æºÐÇØ´Â ¾ïÁ¦ÇÑ´Ù. Àν¶¸°Àº ÀÌÀÚȰ¼º¼ººÐÀÇ ¾àǰÀ¸·Î¼ ´ç´¢º´ ¹× ±âŸ ÁúȯÀÇ Ä¡·á¿¡ »ç¿ëµÈ´Ù. Àν¶¸°À̶ó´Â ¸íĪÀº ¼¶À̶õ ¶æÀÇ ¶óƾ¾îÀÎ insula¿¡¼ ¿¬À¯ÇÑ´Ù. 1921³â ij³ª´ÙÀÇ ÀÇ»ç F.G. ¹êÆÃ°ú C.H. º£½ºÆ®¿¡ ÀÇÇÏ¿© óÀ½À¸·Î ÀÌÀÚ¿¡¼ äÃëµÇ¾ú°í, ±× ÈÄ Àν¶¸°ÀÇ °áÁ¤À» ¾ò°Ô µÇ¾ú´Ù. F. »ý°Å¿¡ ÀÇÇØ¼ ¼ÒÀÇ Àν¶¸°ÀÇ ±¸Á¶°¡ ¹àÇôÁ³´Âµ¥(1955), À̰ÍÀº ´Ü¹éÁú Áß¿¡¼´Â ÃÖÃÊ·Î ±¸Á¶½ÄÀÌ ¹àÇôÁø °ÍÀÌ´Ù. Æ÷µµ´çÀ¸·ÎºÎÅÍ ±Û¸®ÄÚ°ÕÀÇ »ý¼º, Æ÷µµ´çÀÇ »êÈ ¹× Áö¹æÀ¸·ÎÀÇ ÀüÈ µîÀ» ÃËÁøÇÏ´Â ÀÛ¿ëÀÌ ÀÖ´Ù. µû¶ó¼ Àν¶¸°ÀÇ ¼ö¿ë¾×À» ÁÖ»çÇϸé Ç÷´çÀÌ ÀúÇÏÇϹǷΠ´ç´¢º´ÀÇ Ä¡·á¿¡ ¾²ÀδÙ. ¶Ç Àν¶¸°À» ÇÇÇÏ¿¡ ´ë·® ÁÖ»çÇϸé È¥¼ö¿¡ ºüÁö´Â °ÍÀ» ÀÌ¿ëÇÏ¿© Á¤½Åº´ Ä¡·á¿¡ Àν¶¸°¼îÅ©¿ä¹ýÀ¸·Î¼ ¾²ÀδÙ. |
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| ¿µ¹® | IDDM(Insulin-Dependent Diabetes Mellitus) | ÇÑ±Û | Àν¶¸°ÀÇÁ¸´ç´¢º´ |
|---|---|---|---|
| ¼³¸í | IDDMÀº ´ç´¢º´ÀÇ Ä¡·á¿¡ ¹Ýµå½Ã Àν¶¸°ÀÌ ÇÊ¿äÇÑ °æ¿ì¸¦ ¸»ÇÑ´Ù. ÁÖ·Î ¿øÀÎÀÌ ÀÌÀÚ¿¡ ÀÖ´Â Àν¶¸°À» ºÐºñÇÏ´Â ¼¼Æ÷ÀÇ ÆÄ±«À̸ç ÀÌ·Î ÀÎÇØ¼ ´ç´¢º´ÀÇ Ä¡·áÁ¦·Î ¾²ÀÌ´Â Àν¶¸°ÀÇ ºÐºñ¸¦ ÃËÁøÇÏ´Â ¾à¹°ÀÌ ÀÌ IDDM¿¡¼´Â ¾²ÀÏ ¼ö°¡ ¾ø°í ¿ÀÁ÷ Àν¶¸°¸¸ÀÌ Ä¡·áÁ¦·Î ¾µ ¼ö°¡ ÀÖ´Ù. ÀüÇüÀûÀÎ Àν¶¸° ÀÇÁ¸Çü ´ç´¢º´Àº ¼Ò¾Æ¿¡¼ ÈçÈ÷ ¹ß»ýÇϰí Àν¶¸° ºÐºñ¼¼Æ÷ÀÇ ÆÄ±«¿¡ ÀÇÇØ¼ Àν¶¸° ºÐºñ´ÉÀº °ÅÀÇ ¾ø´Ù. |
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| IRS | immunoreactive secretion; infrared spectrophotometry; insulin receptor species; insulin receptor sub... |
|---|---|
| RAR | rapidly adapting receptor; rat insulin receptor; retinoic acid receptor; right arm reclining; right ... |
| INSRR | insulin receptor-related receptor |
| IRR | insulin receptor-related receptor; intrarenal reflux |
| CRP | chronic relapsing pancreatitis; corneal-retinal potential; coronary rehabilitation program; C-reacti... |
| IRR | Insulin receptor- related receptor |
|---|---|
| HIR | Human insulin receptor |
| IR | Insulin Receptor |
| IRS-1 | Insulin Receptor Substrat-1 |
| IRS | Insulin Receptor Substrate |
IGF-II : insulin like growth factor-IIÀÇ ¾àÀÚ. ¸¹Àº Àå±â¿Í Á¶Á÷¿¡ ÀÛ¿ëÇÏ¿© ´Ü¹é ÇÕ¼º°ú DNA, RNAÀÇ ÇÕ¼ºÀ» Áõ°¡½ÃÄÑ ¼¼Æ÷ÀÇ ¼ö¿Í ¾çÀ» Áõ°¡
| insulin receptor substrate-1 protein | <chemical> Amino acid sequence given in first source; a 180 kD protein that contains multiple phosphorylated tyrosine residues after insulin stimulation; human and rat forms (hirs-1 and irs-1) are homologous Synonym: insulin receptor substrate-1-like protein, irs-1 protein, irs-1 gene product, hirs-1 protein, hirs-1 gene product, insulin receptor substrate 1, insulin receptor substrate-1 (05 Dec 1998) |
|---|
| insulin receptor protein-tyrosine kinase | <enzyme> A catalytic protein-tyrosine kinase domain found on the cytoplasmic beta-portion of the insulin receptor. Registry number: EC 2.7.1.- (12 Dec 1998) |
|---|---|
| insulin receptor | Areas on the outer part of a cell that allow the cell to join or bind with insulin that is in the blood. When the cell and insulin bind together, the cell can take glucose (sugar) from the blood and use it for energy. (09 Oct 1997) |
| insulin-like growth-factor binding protein 1 | One of the six homologous proteins that specifically bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions. The function of this protein is not completely defined. However, several studies demonstrate that it inhibits igf binding to cell surface receptors and thereby inhibits igf-mediated mitogenic and cell metabolic actions. (proc soc exp biol med 1993;204(1):4-29) (12 Dec 1998) |
| insulin-like growth factor-binding protein 2 | One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level. (12 Dec 1998) |
| insulin-like growth factor binding protein 3 | One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level. (12 Dec 1998) |
| insulin like growth-factor-binding protein 4 | One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level. (12 Dec 1998) |
| insulin-like growth-factor-binding-protein 5 | One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level. (12 Dec 1998) |
| insulin-like-growth-factor-binding protein 6 | One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level. (12 Dec 1998) |
| cAMP receptor protein | catabolite (gene) activator protein |
| receptor protein | An intracellular protein (or protein fraction) that has a high specific affinity for binding a known stimulus to cellular activity, such as a steroid hormone or adenosine 3',5'-cyclic phosphate. (05 Mar 2000) |
| receptor protein-tyrosine kinase | <enzyme> A catalytic protein-tyrosine kinase domain found on the cytoplasmic beta-portion of receptors. Many growth and differentiation factor receptors contain this domain. It is critical for the signal transduction pathways required for mitogenesis, transformation, and cell differentiation. Registry number: EC 2.7.1.- (12 Dec 1998) |
| Cek4 receptor protein-tyrosine kinase | <enzyme> Isolated from mouse and chicken. Registry number: EC 2.7.1.- Synonym: cek4 protein, cek4 eph receptor, eph receptor cek4 (26 Jun 1999) |
| G-protein coupled receptor | <cell biology> Cell surface receptors that are coupled to G-proteins (GTP-binding protein). G-protein coupled receptors are thought to have seven membrane spanning domains and have been divided into 2 subclasses: those in which the binding site is in the extracellular domain for example receptors for glycoprotein hormones, such as thyroid stimulating hormone (TSH) and follicle-stimulating hormone (FSH) and those in which the ligand binding site is likely to be in the plane of the 7 transmembrane domains for example rhodopsin and receptors for small neurotransmitters and hormones for example muscarinic acetylcholine receptor. (18 Nov 1997) |
| cyclic AMP receptor protein | A transcriptional regulator in prokaryotes which, when activated by binding cyclic AMP, acts at several promoters. Cyclic AMP receptor protein was originally identified as a catabolite gene activator protein. It was subsequently shown to regulate several functions unrelated to catabolism, and to be both a negative and a positive regulator of transcription. Cell surface cyclic AMP receptors are not included (cyclic AMP receptors), nor are the eukaryotic cytoplasmic cyclic AMP receptor proteins, which are the regulatory subunits of cyclic AMP-dependent protein kinases. (12 Dec 1998) |
| TGF-beta receptor protein kinase | <enzyme> Belongs to the receptor-type serine-threonine kinase subfamily; from chick embryo, related to type II receptor for tgf-beta; 502 aa residues, mw 56,766 da; aa sequence given in first source Registry number: EC 2.7.1.- Synonym: tgf-beta rpk, rpk-1, rpk-2 (26 Jun 1999) |
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