¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"proton pumping ATPase"¿¡ ´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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • shielding proton
    Â÷Æó¾çÀÚ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 14 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • proton density weighted image
    ¾çÀÚ ¹Ðµµ °­Á¶ ¿µ»ó
  • proton density weighting
    ¾çÀÚ °­Á¶
  • proton electron dipole dipole interaction
    ¾çÀÚ ÀüÀÚ ½Ö±ØÀÚ ½Ö±ØÀÚ »óÈ£¹ÝÀÀ
  • proton flow
    ¾çÀÚ À¯µ¿
  • proton flow abnormality
    ¾çÀÚ À¯µ¿ ÀÌ»ó
  • proton flow deficit
    ¾çÀÚ À¯µ¿ °áÇÌ
  • proton radiation therapy
    ¾çÀÚ¼±Ä¡·á
  • proton relaxation
    ¾çÀÚ ÀÌ¿Ï
  • proton relaxation enhancement
    ¾çÀÚ ÀÌ¿Ï Áõ°­
  • proton shift
    ¾ç¼ºÀÚÀ̵¿(åÕàõí­ì¹ÔÑ).
  • pseudodiastole in high intensity proton flow
    °í°­µµ ¾çÀÚ À¯µ¿¿¡¼­ À§À̿ϱâ
  • recoil proton
    ¹Ýµµ¾çÀÚ
  • replaceable proton
    ´ëü¾çÀÚ
  • shielding proton
    Â÷Æó ¾çÀÚ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • proton translocating ATP synthase
    ¾ç¼ºÀÚ(åÕàõí­) ÀüÀÌ ATP ½ÅÅ×À̽º
  • proton translocation
    ¾ç¼ºÀÚ(åÕàõí­) ÀüÀÌ(ï®ì¹)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • proton flow
    ¾çÀÚÀ¯µ¿
  • proton flow abnormality
    ¾çÀÚÀ¯µ¿ÀÌ»ó
  • proton flow deficit
    ¾çÀÚÀ¯µ¿°áÇÌ
  • proton MR spectroscopy
    ¾çÀÚÀÚ±â°ø¸íºÐ±¤¼ú
  • proton relaxation
    ¾çÀÚÀÌ¿Ï
  • proton relaxation enhancement
    ¾çÀÚÀÌ¿ÏÁõ°­
  • pseudodiastole in high intensity proton flow
    °í°­µµ¾çÀÚÀ¯µ¿¿¡¼­ À§À̿ϱâ
  • shielding proton
    Â÷Æó¾çÀÚ
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
PIXE particle-induced x-ray emission; proton-induced x-ray emission
PMF platelet membrane fluidity; progressive massive fibrosis; proton motive force; pterygomaxillary foss...
pmf proton motive force
PMR patient meta-record; perinatal mortality rate; periodic medical review; physical medicine and rehabi...
PRE photoreacting enzyme; physician's report of examination; pigmented retinal epithelium; preplacement ...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
PD Proton density
PMR Proton magnetic resonance
PMF Proton motive force
PRR proton relaxation rate
PRF proton resonance frequency
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
cadmium translocating ATPase <enzyme> Cadmium-efflux atpase; e1,e2-translocating atpase is a generic name which includes all cation-transport atpases; do not confuse with lysine decarboxylase cada
Registry number: EC 3.6.1.-
Synonym: cada atpase, cd-e1,e2-translocating atpase
(26 Jun 1999)
calcium ATPase <enzyme> Usually used of the calcium pumping ATPase present in high concentration as an integral membrane protein of the sarcoplasmic reticulum of muscle.
This pump lowers the cytoplasmic calcium level and causes contraction to stop. Normal function of the pump seems to require a local phospholipid environment from which cholesterol is excluded.
(18 Nov 1997)
calcium magnesium-atpase <enzyme> An enzyme that catalyses the hydrolysis of ATP and is activated by millimolar concentrations of either calcium or magnesium. Unlike calcium-transporting atpase it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate.
Registry number: EC 3.6.1.-
(12 Dec 1998)
calcium-transporting atpase <enzyme> An enzyme found in the sarcoplasmic reticulum vesicle membrane. During the relaxation of skeletal muscles and muscle rich in mitochondria, this enzyme catalyses the active transport of calcium into the sarcoplasmic reticulum vesicles from the sarcoplasm. It requires micromolar concentrations of calcium and utilises mgatp as a substrate.
Chemical name: ATP phosphohydrolase (Calcium-transporting)
Registry number: EC 3.6.1.38
(12 Dec 1998)
vacuolar ATPase <enzyme> From eukaryotic endomembrane systems, including vacuoles, lysosomes, golgi apparatus, chromaffin granules and coated vesicles. One of three major classes of ion transport ATPase, characterised by a multi subunit structure and a lack of a phosphorylated intermediate.
Found in archaebacteria but not eubacteria, in the intracellular acidic vacuoles and in some proton pumping epithelia (e.g. Intercalated cells of kidney). A complex enzyme encoded by several genes, involved in ion translocation but does not act via phosphorylated enzyme intermediate
See: P-type ATPase.
Registry number: EC 3.6.1.-
Synonym: atpase, v-type, atpase, vacuolar, vacuolar atpase, v-atpase, vacuolar h+-atpase, vacuolar membrane h(+)-atpase, vha55 gene product, vma16 gene product
(26 Jun 1999)
vacuolar calcium ATPase <enzyme> Isolated from saccharomyces cerevisiae; genbank u36603
Registry number: EC 3.6.1.-
Synonym: h(+)-ca(2+)-atpase, vacuolar
(26 Jun 1999)
Rad3 ATPase-DNA helicase <enzyme> Can unwind duplex regions as short as 11 base pairs in a partially duplex circular DNA substrate; on partially duplex linear substrates, the enzyme has a strict 5'--3' polarity with respect to the single strand to which it binds; nicked circular DNA is not utilised; from saccharomyces cerevisiae
Registry number: EC 3.6.1.-
Synonym: rad3 protein
(26 Jun 1999)
magnesium-bicarbonate ATPase <enzyme> Aspect of EC 3.6.1.3
Registry number: EC 3.6.1.-
Synonym: mg-hco3-atpase, atpase, magnesium-bicarbonate
(26 Jun 1999)
VAT ATPase <enzyme> A member of the cdc48/p97 family of atpases; isolated from thermoplasma acidophilum; genbank u78072; do confuse with vat protein
Registry number: EC 3.6.1.-
Synonym: vcp-like atpase, thermoplasma, vat gene product, thermoplasma
(26 Jun 1999)
V-type ATPase <enzyme> From eukaryotic endomembrane systems, including vacuoles, lysosomes, golgi apparatus, chromaffin granules and coated vesicles. One of three major classes of ion transport ATPase, characterised by a multi subunit structure and a lack of a phosphorylated intermediate.
Found in archaebacteria but not eubacteria, in the intracellular acidic vacuoles and in some proton pumping epithelia (e.g. Intercalated cells of kidney). A complex enzyme encoded by several genes, involved in ion translocation but does not act via phosphorylated enzyme intermediate
See: P-type ATPase.
Registry number: EC 3.6.1.-
Synonym: atpase, v-type, atpase, vacuolar, vacuolar atpase, v-atpase, vacuolar h+-atpase, vacuolar membrane h(+)-atpase, vha55 gene product, vma16 gene product
(26 Jun 1999)
RNA-dependent ATPase <enzyme> Requires single-stranded polynucleotide as cofactor
Registry number: EC 3.6.1.-
Synonym: atpase, RNA-dependent
(26 Jun 1999)
CopA ATPase <enzyme> A p-type cation-transporting atpase involved in copper homeostasis in enterococcus hirae; exhibits sequence similarity to copb (atpase) and human mc1 protein; 727 amino acids, mw 87 kD
Registry number: EC 3.6.1.-
(26 Jun 1999)
CopB ATPase <enzyme> A p-type cation-transporting atpase involved in copper homeostasis in enterococcus hirae; exhibits sequence similarity to copa (atpase) and human mc1 protein; 745 amino acids, mw 93 kD
Registry number: EC 3.6.1.-
(26 Jun 1999)
myosin atpase <enzyme> An enzyme that catalyses the hydrolysis of myosin ATP in the presence of actin to form myosin ADP and orthophosphate. This reaction is the immediate source of free energy that drives muscle contraction. In the absence of actin, myosin atpase activity is low and requires calcium ions.
Chemical name: Myosin ATP phosphohydrolase (actin-translocating)
Registry number: EC 3.6.1.32
(12 Dec 1998)
S-(dinitrophenyl)glutathione ATPase <enzyme> Anionic conjugates of bilirubin and bile acids stimulate the hydrolysis of the above enzyme of human erythrocyte; also found in other tissue
Registry number: EC 3.6.1.-
Synonym: dnp-sg-atpase
(26 Jun 1999)
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 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
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 ¸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