¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"serine endopeptidase"¿¡ ´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 : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • endopeptidase
    ÆéƼµå³»ºÎºÐÇØÈ¿¼Ò, ¿£µµÆéƼ´Ù¾ÆÁ¦
  • serine
    1. ¼¼¸° 2. ¼¼¸°Á¦
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • serine
    ¼¼¸°
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • endopeptidase
    ÆéƼµå³»ºÎºÐÇØÈ¿¼Ò, ¿£µµÆéƼ´Ù¾ÆÁ¦
  • serine
    ¼¼¸°
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • phosphatidyl serine
    Æ÷½ºÆÄƼµô¼¼¸°
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • phosphatidyl serine
    Æ÷½ºÆÄƼµô¼¼¸°
  • serine
    ¼¼¸°
  • endopeptidase
    ¿£µµÆéƼ´Ù¾ÆÁ¦
  • endopeptidase
    ¿£µµÆéƼµ¥À̽º.
  • endopeptidase
    ¿£µµÆéƼ´ÙÁ¦
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • endopeptidase
    ¿£µµÆéƼµ¥À̽º
  • phosphatidal serine
    Æ÷½ºÆÄƼ´Þ ¼¼¸°
  • serine
    ¼¼¸°
  • serine convention
    ¼¼¸° ¹æ½Ä(Û°ãÒ)
  • serine esterase
    ¼¼¸° ¿¡½ºÅÍ·¹À̽º
  • serine protease
    ¼¼¸° ÇÁ·ÎƼ¿¡À̽º
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
BBEP brush border endopeptidase
NEP negative expiratory pressure; nephrology; neutral endopeptidase; no evidence of pathology
CAAX [box] protein segment in which C is cysteine, A is usually but not always an aliphatic amino acid, and X i...
HFSP Hanukah factor serine protease
PS pacemaker syndrome; paired stimulation; paradoxical sleep; paraspinal; parasympathetic; Parkinson sy...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
NEP Neutral Endopeptidase
PEP Prolyl endopeptidase
Ser L-serine
L-SOP L-serine O-phosphate
SDH L-serine dehydratase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • endopeptidase
    ¿£µµÆéƼ´Ù¾ÆÁ¦
    ÆéŸÀ̵å¼âÀÇ ³»ºÎ¿¡ ÀÖ´Â ÆéŸÀÌµå °áÇÕÀ» óÀ½¿¡ °¡¼öºÐÇØÇÏ°í µ¿½Ã¿¡ ÆéŸÀ̵åÀÇ ¸»´Ü °áÇÕµµ °¡¼öºÐÇØÇÒ ¼ö ÀÖ´Â ´Ü¹é ºÐÇØ È¿¼Ò.
  • serine
    ¼¼¸°
    1. ´Ü¹éÁúÀ» ±¸¼ºÇÏ´Â ¾Æ¹Ì³ë»êÀÇ Çϳª. ´ë»çµÇ¾î ÇǸ£ºó»êÀ¸·Î µÈ´Ù. 2. õ¿¬À¸·Î Á¸ÀçÇÏ´Â ºñÇʼö ¾Æ¹Ì³ë»ê. C3H7NO3. ±Û¶óÀ̽ſ¡¼­ ÇÕ¼ºµÈ´Ù.
  • serine esterase
    ¼¼¸° ¿¡½ºÅ×¶ó¾ÆÁ¦
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
serine endopeptidase <enzyme> Proteolytic enzyme from pronase& maise
Registry number: EC 3.4.99.-
Synonym: serine endopeptidase, maise
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
IgA-specific serine endopeptidase <enzyme> Extracellular microbial enzymes whose only substrate is human IgA of the iga1 subclass; cleave the immunoglobulin at a specific internal prolyl-threonyl peptide bond in the heavy chain to yield intact faba and fca fragments; consider also EC 3.4.24.13
Registry number: EC 3.4.21.72
Synonym: immunoglobulin a(1) protease, iga1 protease, immunoglobulin a1 protease, IgA protease
(26 Jun 1999)
adenovirus endopeptidase <enzyme> Has been sequenced; high homology for enzymes from human, bovine, canine, murine and avian adenoviruses; see also record for avian adenovirus type 1 proteinase
Registry number: EC 3.4.22.-
Synonym: ad2 proteinase, can1 proteinase, mav1 proteinase, adenovirus proteinase ad2
(26 Jun 1999)
alanine endopeptidase <enzyme> From enterocyte brush border; cleaves between alanyl and alanyl-, leucyl-, or norleucyl- residues of synthetic peptides similar to metallic endopeptidases
Registry number: EC 3.4.24.-
(26 Jun 1999)
arginine endopeptidase <enzyme> Cleaves arginine at the carboxyl side in a peptide chain
Registry number: EC 3.4.21.-
Synonym: arginyl endopeptidase
(26 Jun 1999)
glutamyl endopeptidase <enzyme> Cleaves at the carboxyl side of glutamate and aspartate residues in proteins; see also glutamyl endopeptidase II from strep. Griseus (EC 3.4.21.82)
Registry number: EC 3.4.21.19
Synonym: staphylococcus v-8 protease, v-8 protease, protease v8, staph aureus sv8 protease, staphylococcal serine protease, glu-c protease, staphylococcal glu-c protease, endoproteinase glu-c, protease glu-c, glutamate-specific endopeptidase, endopeptidase glu-c
(26 Jun 1999)
glycyl endopeptidase <enzyme> Isoelectric pt greater than 11.1; molecular mass=24k; separable from papaya proteinase a by acid gel electrophoresis; from papaya plant carcica papaya; not inhibited by chicken cystatin
Registry number: EC 3.4.22.25
Synonym: papaya peptidase b, papaya proteinase b, papaya proteinase iv
(26 Jun 1999)
PepE endopeptidase <enzyme> Thiol-dependent endoprotease from lactobacillus helveticus; do not confuse with pepe protein, which is an aspartic proteinase from aspergillus niger; genbank u77050
Registry number: EC 3.4.-
Synonym: pepe gene product, lactobacillus
(26 Jun 1999)
peptide hormone inactivating endopeptidase <enzyme> From xenopus laevis; cleaves at xaa-phe, xaa-leu or xaa-ile bonds where xaa = ser, phe, tyr, his or gly in peptide hormones
Registry number: EC 3.4.24.-
Synonym: phie, xenopus
(26 Jun 1999)
procollagen C-endopeptidase <enzyme> Cleaves the carboxyl-terminal propeptides from type I pr; in 1996 determined to be identical to bone morphogenetic protein 1
Registry number: EC 3.4.24.19
Synonym: procollagen c-protease, type I procollagen carboxyl-terminal proteinase, c-proteinase, procollagen, procollagen endopeptidase (carboxy terminal splitting), procollagen c-proteinase, bone morphogenetic protein 1, bone morphogenic protein 1, bmp-1
(26 Jun 1999)
procollagen n-endopeptidase <enzyme> An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis.
Registry number: EC 3.4.24.14
(12 Dec 1998)
D-alanyl-L-alanine endopeptidase <enzyme> Acts on peptidoglycan
Registry number: EC 3.4.99.-
Synonym: d-ala-l-ala endopeptidase
(26 Jun 1999)
DD-carboxypeptidase-endopeptidase <enzyme> Hydrolyzes c-terminal d-ala-d-peptide, where second amino acid can vary
Registry number: EC 3.4.15.-
Synonym: dacf protein
(26 Jun 1999)
dynorphin-converting endopeptidase <enzyme> Enzyme from human cerebrospinal fluid; cleaves dynorphin a and b and neoendorphin at the arg(6)-arg(7) or arg(6)-lys(7) bonds
Registry number: EC 3.4.21.-
Synonym: dynorphin-neo-endorphin endopeptidase, dc-endopeptidase
(26 Jun 1999)
O-sialoglycoprotein endopeptidase <enzyme> Specific for o-sialoglycoproteins such as glycophorin a; amino acid sequence given in first source
Registry number: EC 3.4.24.57
Synonym: pht a1 glycoprotease, o-glycosylated glycoprotein protease, sialoglycoprotease, glycophorin a protease, glycophorin a glycoprotease, glycoprotease, pasteurella haemolytica a1
(26 Jun 1999)
tetralysine endopeptidase <enzyme> E coli enzyme cleaves tetralysine into 2 dilysine
Registry number: EC 3.4.99.-
(26 Jun 1999)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Serine Endopeptidases - »õâ Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. EC 3.4.21.
    Synonyms : Serine Protease, Serine Protein Hydrolases, Serine Proteinase, Endopeptidases, Serine, Hydrolases, Serine Protein, Protease, Serine, Proteases, Serine, Protein Hydrolases, Serine, Proteinase, Serine, Proteinases, Serine
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
serine endopeptidase [EC 3.4.21] any member of the group of endopeptidases containing at the active site a triad of serine, aspartate, and histidine residues involved in catalysis. Included are enzymes active in digestion, blood coagulation, immune reactions, and fertilization of the ovum. Called also serine protease or proteinase.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • 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: 1
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
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: 1
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: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á