Affinity modification of E1-form of Na+, K+-ATPase revealed Asp-710 in the catalytic site.
about
cDNA cloning, expression and chromosomal localization of the human sarco/endoplasmic reticulum Ca(2+)-ATPase 3 geneCloning and characterization of the entire cDNA encoded by ATP1AL1--a member of the human Na,K/H,K-ATPase gene familyFamily of human Na+,K+-ATPase genes Structure of the gene for the catalytic subunit (αIII-form) and its relationship with structural features of the proteinMolecular characterization and expression of the (Na+ + K+)-ATPase alpha-subunit in Drosophila melanogaster.Low temperature molecular adaptation of the skeletal muscle sarco(endo)plasmic reticulum Ca2+-ATPase 1 (SERCA 1) in the wood frog (Rana sylvatica).Molecular and biochemical characterization of the Dio-9-resistant pma1-1 mutation of the H(+)-ATPase from Saccharomyces cerevisiae.Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.The sodium pump. Its molecular properties and mechanics of ion transport.The KDP ATPase of Escherichia coli.cDNA cloning of possible mammalian homologs of the yeast secretory pathway Ca(2+)-transporting ATPase.Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domainsChemical modification as an approach to elucidation of sodium pump structure-function relations.Advances in Na+,K+-ATPase studies: from protein to gene and back to protein.Introducing Wilson disease mutations into the zinc-transporting P-type ATPase of Escherichia coli. The mutation P634L in the 'hinge' motif (GDGXNDXP) perturbs the formation of the E2P state.Photoinactivation of fluorescein isothiocyanate-modified Na,K-ATPase by 2'(3')-O-(2,4,6-trinitrophenyl)8-azidoadenosine 5'-diphosphate. Abolition of E1 and E2 partial reactions by sequential block of high and low affinity nucleotide sites.
P2860
Q24324213-5B0444CD-2DF8-44A5-9BD8-1CC753ABD62BQ28609361-BBEF2030-A43B-4069-BEF2-B1461A8921DDQ29308501-621D0547-DCEE-401D-812A-6527F0B00856Q30448506-793310FF-937A-40A4-8A32-85729F3F79C1Q31484910-A1AE9E3E-C9E8-4EF7-9EE7-89DC1942BA42Q33870155-440983F8-6DC5-4463-ACF1-30D083732C5AQ34018696-76D83527-E4E6-4FDA-A9BF-C3CB5F1D6CA3Q34655307-9AB62556-8D47-4128-B076-38C06A9CD2D6Q35185920-D35E4824-93F7-438D-BDCE-CD8F70670599Q35186118-E3E58C4E-7356-47B9-A525-FBBB810A37D3Q36569774-19AF44CD-1DDF-466E-9A8C-1B088B555EB6Q37871851-11252033-3FF6-4F5F-8976-56BE3701224CQ38298381-7B9F7D74-90BF-4488-B60F-0E3C6214596DQ43902851-8798DA6C-DCDA-4400-8747-2F2A194923BDQ48034678-2EBF1C88-964A-42D4-A80F-08797FDA978C
P2860
Affinity modification of E1-form of Na+, K+-ATPase revealed Asp-710 in the catalytic site.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
1987年學術文章
@zh
1987年學術文章
@zh-hant
name
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@en
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@nl
type
label
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@en
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@nl
prefLabel
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@en
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@nl
P2093
P2860
P1433
P1476
Affinity modification of E1-fo ...... Asp-710 in the catalytic site.
@en
P2093
Dzhandzhugazyan KN
Dzhandzugazyan KN=Dzhadzhugazyan KN
Lutsenko SV
Modyanov NN
Mustayev AA
Ovchinnikov YuA
P2860
P304
P356
10.1016/0014-5793(87)81253-X
P407
P577
1987-06-01T00:00:00Z