¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"cytochrome"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
À̰ÍÀ» ¿øÇϼ̽À´Ï±î?
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 2
UQCRC ubiquinol-cytochrome C reductase core
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
CYP1A1 Cytochrome P-450 1A1
CYP2C11 Cytochrome P-450 2C11
CYP2D6 Cytochrome P-450 2D6
CYP2E1 Cytochrome P-450 2E1
CYP 3A Cytochrome P-450 3A
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
cytochrome c2 reductase <enzyme> An enzyme catalyzing the reduction of 2 ferricytochrome c2 to 2 ferrocytochrome c2 at the expense of NADPH.
Synonym: cytochrome c2 reductase.
(05 Mar 2000)
cytochrome c3 hydrogenase A hydrogenase enzyme catalyzing reduction of 2ferricytochrome c3 by H2 to 2ferrocytochrome c3 and 2H+.
(05 Mar 2000)
cytochrome C553 peroxidase <enzyme> A haem group of cytochrome-c peroxidase (EC 1.11.1.5); catalytically active in both the oxidised and half-reduced states; from nitrosomonas europaea; partial amino acid sequence given in first source
Registry number: EC 1.11.1.-
(26 Jun 1999)
cytochrome cd cytochrome oxidase (Pseudomonas)
cytochrome d <chemical> Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin.
Chemical name: Cytochrome d
(12 Dec 1998)
cytochrome oxidase <enzyme> Terminal enzyme of the electron transport chain that accepts electrons from (i.e. Oxidizes) cytochrome C and transfers electrons to molecular oxygen.
(18 Nov 1997)
cytochrome p-450 <biochemistry> Enzymes of the electron transport chain that are pigmented by virtue of their haem prosthetic groups.
They are highly conserved isozymes which are key components of the mixed-function oxidase system responsible for the biotransformation of many foreign compounds to mutagens and carcinogens.
Most mammals have several distantly related phenobarbital-inducible gene subfamilies.
(21 Jun 2000)
cytochrome p-450 cyp11b2 <enzyme> A multifunctional enzyme that catalyses the conversion of corticosterone to 18-hydroxycorticosterone and the subsequent conversion of 18-hydroxycorticosterone to aldosterone.
Registry number: EC 1.14.99.-
(12 Dec 1998)
cytochrome p-450 cyp1a1 <enzyme> A cytochrome p-450 enzyme capable of activating procarcinogenic polycyclic hydrocarbons and halogenated aromatic hydrocarbons into mutagenic compounds. Ethoxyresorufin acts as a substrate for cyp1a1 and measurement of ethoxyresorufin o-deethylase provides a more direct method of detection for this enzyme.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp1a2 <enzyme> A polycyclic aromatic hydrocarbon-inducible cytochrome which is of significant clinical interest due to the large number of drug interactions associated with induction and inhibition of theophylline. Caffeine is considered to be a model substrate for this enzyme. It also metabolises theophylline and antipyrene. Environmental factors including cigarette smoking, charbroiled meat, cruciferous vegetables, and a number of drugs including phenytoin, phenobarbital, and omeprazole produce increases in cyp1a2 activity.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp2b1 <enzyme> A major cytochrome p-450 enzyme which is inducible by phenobarbital in both the liver and small intestine. It is active in the metabolism of compounds like pentoxyresorufin, testosterone, and androstenedione. Cyp2b1 also mediates the activation of cyclophosphamide and ifosfamide to mutagens.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp2d6 <enzyme> A polymorphic enzyme that catalyses the hydroxylation of debrisoquine. It also metabolises several antidepressants and neuroleptics. This enzyme is deficient in up to 10 percent of the population.
Registry number: EC 1.14.99.-
(12 Dec 1998)
cytochrome p-450 cyp2e1 <enzyme> A polymorphic enzyme that activates carcinogenic n-nitrosamines, benzene, urethane, and other low molecular weight compounds. It is inducible by ethanol and metabilises alcohol. Experimentally, it is used to study the effects of ethanol usage and withdrawal via enzyme markers such as n-nitrosodimethylamine demethylase.
Registry number: EC 1.5.99.-
(12 Dec 1998)
cytochrome P-450 oxidase <enzyme> Oxidises NADPH with formation of hydrogen peroxide
Registry number: EC 1.6.2.-
Synonym: NADPH-p450 reductase, NADPH-cytochrome p450 reductase, cytochrome p450 reductase, cpra gene product
(26 Jun 1999)
cytochrome P-450-dependent digitoxin 12beta-hydroxylase <enzyme> Isolated from digitalis lantata cell cultures
Registry number: EC 1.14.99.-
Synonym: digitoxin 12beta-hydroxylase
(26 Jun 1999)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 2
  • Cytochrome P-450 CYP1A1 - »õâ A liver microsomal cytochrome P-450 monooxygenase capable of biotransforming xenobiotics such as polycyclic hydrocarbons and halogenated aromatic hydrocarbons into carcinogenic or mutagenic compounds. They have been found in mammals and fish. This enzyme, encoded by CYP1A1 gene, can be measured by using ethoxyresorufin as a substrate for the ethoxyresorufin O-deethylase activity.
    Synonyms : 7-Ethoxyresorufin O-Deethylase, CYP 1A1, CYP1A1 Protein, Cytochrome P450 IA1, Ethoxyresorufin Dealkylase, Ethylresorufin O-Deethylase, Cytochrome P 450 CYP1A1
  • Cytochrome P-450 CYP1A2 - »õâ A cytochrome P-450 monooxygenase that can be induced by polycyclic aromatic xenobiotics in the liver of human and several animal species. This enzyme is of significant clinical interest due to the large number of drug interactions associated with its induction and its metabolism of THEOPHYLLINE. Caffeine is considered to be a model substrate for this enzyme. CYP1A2 activity can also be increased by environmental factors such as cigarette smoking, charbroiled meat, cruciferous vegetables, and a number of drugs including phenytoin, phenobarbital, and omeprazole.
    Synonyms : CYP 1A2, Caffeine Demethylase, Cytochrome P-450 LM(4), Cytochrome P-450 LM4, Cytochrome P-450d, Cytochrome P450 1A2, CYP1A2, Cytochrome P-450, Cytochrome P 450 CYP1A2, Cytochrome P 450d, Demethylase, Caffeine, O-Dealkylase, Phenacetin, Phenacetin O Dealkylase
  • Cytochrome P-450 CYP27A1 - »õâ An NAPH-dependent cytochrome P450 enzyme that catalyzes the oxidation of the side chain of sterol intermediates such as the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha, 12-alpha-triol. Cytochrome P-450 CYP27A1 is a mitochondrial enzyme; however microsomal-derived homologs of the enzyme have been identified and are included under this heading.
    Synonyms : 5-beta-Cholestane-3-alpha, 7-alpha, 12-alpha-triol 27-Hydroxylase, C27-Steroid 26-Hydroxylase, Cholestanetriol 26-Monooxygenase, Cytochrome P-450 CYP2R1, Cytochrome P-450 Steroid 27-Hydroxylase, Cytochrome P-450 Sterol 26-Hydroxylase, Cytochrome P450 2R1
  • Cytochrome P-450 CYP2B1 - »õâ A major cytochrome P-450 enzyme which is inducible by PHENOBARBITAL in both the LIVER and SMALL INTESTINE. It is active in the metabolism of compounds like pentoxyresorufin, TESTOSTERONE, and ANDROSTENEDIONE. This enzyme, encoded by CYP2B1 gene, also mediates the activation of CYCLOPHOSPHAMIDE and IFOSFAMIDE to MUTAGENS.
    Synonyms : 7-Benzyloxyresorufin O-Dealkylase, 7-Pentylresorufin O-Depentylase, CYP 2B1, Cytochrome P450 2B1, 7 Benzyloxyresorufin O Dealkylase, 7 Pentylresorufin O Depentylase, Benzyloxyresorufin O Dealkylase, Cytochrome P 450 CYP2B1, O-Dealkylase, Pentoxyresorufin
  • Cytochrome P-450 CYP2D6 - »õâ A cytochrome P450 enzyme that catalyzes the hydroxylation of many drugs and environmental chemicals, such as DEBRISOQUINE; ADRENERGIC RECEPTOR ANTAGONISTS; and TRICYCLIC ANTIDEPRESSANTS. This enzyme is deficient in up to 10 percent of the Caucasian population.
    Synonyms : CYP 2D6, Cytochrome P450 2D6, Debrisoquine 4-Monooxygenase, Imipramine 2-Hydroxylase, Sparteine Monooxygenase, 2-Hydroxylase, Imipramine, 4-Hydroxylase, Debrisoquine, 4-Monooxygenase, Debrisoquine, CYP2D6, Cytochrome P-450, Cytochrome P 450 CYP2D6
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
cytochrome P-450 an enzyme that plays an important role in the metabolism of drugs and toxins in the liver. It also plays a role in the synthesis (formation) of steroid hormones in the adrenal cortex.
Ãâó: www.nutrabio.com/Definitions/definitions_c.htm
cytochrome A type of protein whose function is to carry electrons or protons (hydrogen ions) by virtue of the reversible charging/discharging of an iron atom or iron/sulfur atoms in the center of the protein. Cytrochromes are central molecules of electron transport in the process known as oxidative phosphorylation. The "chrome" means color, and these cytochromes are divided into four groups. (a, b, c, d) according to their ability to absorb or transmit certain colors of light.
Ãâó: aspin.asu.edu/geneinfo/glos-c.htm
cytochrome P450 a system that metabolizes drugs and other foreign substances in the liver by means of enzymes (eg, CYP3A4) that inhibit or promote metabolic reactions.
Ãâó: www.aegis.com/pubs/beta/1999/be990414.html
cytochrome P-450 This is a haem-containing protein which takes part in the phase I reactions of xenobiotics during biotransformation processes.
Ãâó: www.bio.hw.ac.uk/edintox/glossall.htm
cytochrome A type of enzyme.
Ãâó: www.third-plateau.org/faq/dxm_glossary.shtml
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
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °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
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °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 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