¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"parathyroid hormone-related peptide"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • peptide
    ÆéŸÀ̵å.
  • peptide antibiotics
    ÆÕƼµåÇ×»ýÁ¦
  • peptide bond
    ÆÕƼµå°áÇÕ
  • peptide bond
    ÆéŸÀ̵å°áÇÕ.
  • peptide hormone
    ÆéƼµåÈ£¸£¸ó.
  • peptide linkage
    ÆéƼµå°áÇÕ
  • procollagen III peptide
    ÇÁ·ÎÄݶó°Õ III ÆéƼµå
  • signal peptide
    ½ÅÈ£ÆéƼµå
  • trypsinogen activation peptide(TAP)
  • urinary gonadotropin fragment/peptide
    ¿äÁß¼º¼±ÀÚ±ØÈ£¸£¸óºÐÀý/ÆéƼµå
  • vasoactive intestinal (poly)peptide
    Ç÷°üÀۿ뼺 ÀåÆéƼµå
  • bud of inferior parathyroid gland
    ¾Æ·¡ºÎ°©»ó»ù½Ï
  • bud of superior parathyroid gland
    À§ºÎ°©»ó»ù½Ï
  • cell of parathyroid gland
    ºÎ°©»ó»ù¼¼Æ÷
  • inferior parathyroid gland
    ¾Æ·¡ºÎ°©»ó»ù
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 9 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • peptide map
    ÆéŸÀ̵å Áöµµ(ò¢Óñ)
  • peptide synthetase
    ÆéŸÀÌµå ½ÅÅ×Å×À̽º
  • phosphate acceptor peptide
    Àλê¼ö¿ë(×òß«áôé») ÆéŸÀ̵å
  • signal peptide
    ½ÅÈ£(ãáûÜ)ÆéŸÀ̵å
  • S peptide
    S ÆéŸÀ̵å
  • spore peptide
    Æ÷ÀÚ(øàí­)
  • streptogenin peptide
    ½ºÆ®·¾ÅäÁ¦´Ñ ÆéŸÀ̵å
  • tryptic peptide
    Æ®¸³½ÅºÐÇØ(ÝÂú°) ÆéŸÀ̵å
  • vasoactive intestinal peptide
    Ç÷°ü ÀÛµ¿¼º(úìηíÂÔÑàõ) Àå(íó)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
C-Peptide Connecting Peptide
ERP early receptor potential; effective refractory period; elodoisin-related peptide; endoscopic retrogr...
VIP vasoactive intestinal peptide; vasoinhibitory peptide; venous impedance plethysmography; ventricular...
PTH ParaThyroid Hormone
PTH-rP ParaThyroid Hormone related Protein
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
iPTH D-intact parathyroid hormone
hPTH Human parathyroid hormone
PT Parathyroid
PTH Parathyroid
PTE Parathyroid Extract
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 13 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • endogenous opiate peptide
    ³»Àμº ¾ÆÆí ÆéŸÀ̵å, ³»À缺 ¿ÀÇÇ¿¡ÀÌÆ® ÆÕŸÀ̵å, ³»À缺 ¾ÆÆí¾ç ÆéŸÀ̵å
  • multiple biologically active peptide fragment
    ´Ù¹ß¼º »ý¹°ÇÐÀû Ȱ¼º ÆéŸÀÌµå ºÐÀý
  • non-peptide transmitter
    ºñÆéƼµå Àü´Þ ¹°Áú
  • opioid peptide
    ¾ÆÆí¾ç ÆéƼµå, ¾ÆÆí¾ç ÆéŸÀ̵å
  • peptide
    ÆéŸÀ̵å, ÆéƼµå
    °¡¼öºÐÇØ¿¡ ÀÇÇÏ¿© À̺ÐÀÚ ÀÌ»óÀÇ ¾Æ¹Ì³ë»êÀ» ¸¸µå´Â ÀúºÐÀÚ È­ÇÕ¹°·Î¼­, ÀÎÁ¢ ¾Æ¹Ì³ë»êÀÇ NH2±â¿Í COOH±â·ÎºÎÅÍ Å»¼ö °áÇÕÀ» ÅëÇÏ¿© Çü¼ºµÈ´Ù.
  • peptide E
    ÆéƼµå E
  • peptide hormone
    ÆéƼµå È£¸£¸ó
  • precursor peptide
    Àü±¸ ÆéƼµå
  • proenkephalin peptide
    ÇÁ·Î ¿£ÄÉÆÈ¸° ÆéƼµå
  • proenkephalin-derived peptide
    ÇÁ·Î¿£ÄÉÆÈ¸° À¯·¡ ÆéƼµå
  • signal peptide
    ½ÅÈ£ ÆéƼµå
  • simple-chain peptide

    simplex (´Ü¼ø

  • single peptide
    ´ÜÀÏ ÆéŸÀ̵å
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
antibiotics, peptide Antibiotics whose structure contains one or more peptides, usually cyclic. They are generally effective against gram-positive bacteria and act by inhibiting peptidoglycan synthesis in bacterial cell walls.
(12 Dec 1998)
atrial natriuretic peptide <hormone> This cardiac hormone (28 amino acid residues) regulates salt and water balance in body fluids and blood pressure, it has potential as a medication to treat heart and kidney failure and the buildup of excess fluid in tissue.
(09 Oct 1997)
bradykinin-potentiating peptide <chemical> 2-l-tryptophan-3-de-l-leucine-4-de-l-proline-8-l-glutamine bradykinin potentiator b. A synthetic nonapeptide with the sequence pyr-trp-pro-arg-pro-gln-ile-pro-pro, which is identical to that of the peptide from the venom of the snake, bothrops jararaca. It acts as an inhibitor of kininase II and angiotensin I and has been proposed as an antihypertensive agent.
Pharmacological action: angiotensin-converting enzyme inhibitors, antihypertensive agents.
Chemical name: Bradykinin potentiator B, 2-L-tryptophan-3-de-L-leucine-4-de-L-proline-8-L-glutamine-
(12 Dec 1998)
brain natriuretic peptide <hormone, protein> Brain peptide that induces diuresis, related to atrial natriuretic peptide.
(18 Nov 1997)
calcitonin gene-related peptide <protein> A second product transcribed from the calcitonin gene. Calcitonin gene related peptide is found in a number of tissues including nervous tissue. It is a vasodilator that may participate in the cutaneous triple response.
It is a neuropeptide of 37 amino acids with structural homology to salmon calcitonin. Co-localises with substance P in neurons. It occurs as a result of alternative processing of mRNA from the calcitonin gene.
The neuropeptide is widely distributed in neural tissue of the brain, gut, perivascular nerves, and other tissue. The peptide produces multiple biological effects and has both circulatory and neurotransmitter modes of action. In particular, it is a potent endogenous vasodilator.
Intracerebral administration leads to a rise in noradrenergic sympathetic outflow, a rise in blood pressure and a fall in gastric secretion.
Acronym: CGRP
(05 May 2002)
vasoactive intestinal peptide <gastroenterology, protein> Peptide of 28 amino acids, originally isolated from porcine intestine, but later found in the central nervous system where it acts as a neuropeptide and is released by specific interneurons. May also affect behaviour of cells of the immune system.
Acronym: VIP
(05 Jan 1998)
gastrin-releasing peptide <hormone> A regulatory peptide (27 amino acids) thought to be the mammalian equivalent of bombesin. It elicits gastrin release and regulates gastric acid secretion and motor function.
It causes bronchoconstriction and vasodilation in the respiratory tract and stimulates the growth and mitogenesis of cells in culture. Once released from nerves in the antrum of the stomach, the neuropeptide stimulates release of gastrin from the g cells.
Chemical name: Gastrin-releasing peptide
(12 Dec 1998)
receptors, calcitonin gene-related peptide Cell surface proteins that bind calcitonin gene-related peptide (cgrp) with high affinity and trigger intracellular changes which influence the behaviour of cells. Cgrp receptors are present in both the central nervous system and the periphery and are not the same as calcitonin receptors.
(12 Dec 1998)
receptors, invertebrate peptide Cell surface receptors for invertebrate peptide hormones or neuropeptides.
(12 Dec 1998)
receptors, peptide Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behaviour of cells.
(12 Dec 1998)
receptors, vasoactive intestinal peptide Cell surface proteins that bind vasoactive intestinal peptide (vip) with high affinity and trigger intracellular changes which influence the behaviour of cells.
(12 Dec 1998)
glutaminyl-peptide cyclotransferase <enzyme> Catalyses the formation of 5-oxoprolyl-trna and nh3 from l-glutaminyl-trna; also acts on glutaminyl peptides
Registry number: EC 2.3.2.5
Synonym: glutaminyl cyclase, glutaminylpeptide cyclase, glutamine cyclotransferase, glutaminyl-trna cyclotransferase
(26 Jun 1999)
peptide <biochemistry> A compound of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
(27 Sep 1997)
peptide antibiotic lactonase <enzyme> Peptide lactone and water gives linear peptide
Registry number: EC 3.1.1.-
(26 Jun 1999)
peptide bond The amide linkage between the carboxyl group of one amino acid and the amino group of another. The linkage does not allow free rotation and can occur in cis or trans configuration, the latter the most common in natural peptides, except for links to the amino group of proline, which are always cis.
(18 Nov 1997)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
ÅëÇÕ°Ë»ö ¿Ï·á