Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
about
Characterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinoprilThe N Domain of Human Angiotensin-I-converting Enzyme: THE ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407Molecular and Thermodynamic Mechanisms of the Chloride-dependent Human Angiotensin-I-converting Enzyme (ACE)Angiotensin I-converting enzyme Gln1069Arg mutation impairs trafficking to the cell surface resulting in selective denaturation of the C-domainInhibition mechanism and model of an angiotensin I-converting enzyme (ACE)-inhibitory hexapeptide from yeast (Saccharomyces cerevisiae)Comparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.Angiotensin I-converting enzyme inhibitors are allosteric enhancers of kinin B1 and B2 receptor function.Inhibitor and substrate binding by angiotensin-converting enzyme: quantum mechanical/molecular mechanical molecular dynamics studies.Functional regulation of sugar assimilation by N-glycan-specific interaction of pancreatic α-amylase with glycoproteins of duodenal brush border membraneAngiotensin-I converting enzyme (ACE): structure, biological roles, and molecular basis for chloride ion dependence.The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme.Insight into the interactive residues between two domains of human somatic Angiotensin-converting enzyme and Angiotensin II by MM-PBSA calculation and steered molecular dynamics simulation.Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method
P2860
Q27660250-CDF318D4-8AD1-4DBD-9377-F9008636E4C0Q27664390-C6C94F66-CF5F-4340-927C-375EDA2B8D99Q27680735-1E056F9A-93FF-450E-BA87-E45405EDFDA9Q28473818-FF2D2AE4-A759-4033-843A-BEED8AC987ECQ28483656-D4574372-1DCB-4DE4-9D27-210A98B7BE24Q30379469-0287435D-1A3C-4C21-872B-FB68405ED6A9Q33623829-B525B0C2-B6A3-40BB-8810-3AA52B3132D1Q35167293-EE551C14-A9D4-4D2A-ADB1-1F5D8206A2E2Q36080467-D3C60296-BAD6-4181-B3AA-E4218AD23F60Q38247932-4EAA571E-13E4-4A59-A6F5-C6F5FBAB7C2CQ38820520-378B3F50-347D-4C9B-A551-EA41A023F365Q39949282-38C2641E-3A39-45B5-9A56-0FE8D0801F51Q41591227-3EACC9C6-7017-4040-9C40-9987AC20BD12Q57911637-18CFBF0E-90F7-4E15-A89D-9C91047B73A4
P2860
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@ast
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@en
type
label
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@ast
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@en
prefLabel
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@ast
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@en
P2093
P2860
P356
P1433
P1476
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement.
@en
P2093
B Trevor Sewell
Edward D Sturrock
Hazel R Corradi
Jean M Watermeyer
K Ravi Acharya
Ramanathan Natesh
Sylva L Schwager
P2860
P304
12654-12663
P356
10.1021/BI061146Z
P407
P577
2006-10-01T00:00:00Z