Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.
about
NMR structures of membrane proteins in phospholipid bilayersStructural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium TransportThe alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.Discovery and structural characterization of a phospholamban-binding cyclic peptide and design of novel inhibitors of phospholamban.Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pumpStructural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.Effects of PKA phosphorylation on the conformation of the Na,K-ATPase regulatory protein FXYD1.High-yield expression of isotopically labeled peptides for use in NMR studies.
P2860
Q27006900-424C6317-148C-4301-A76A-DD8E843433ACQ27680562-C7C5E130-1B65-4526-BB74-80E0B189F58DQ30984765-14106522-F063-42E2-A1BA-638414E7DDFFQ34266350-AFE1C1E6-4952-47B0-A123-E12BD9A160C4Q35063543-EC24CE32-896F-44A6-8A0E-213CAF9DA288Q37275638-C46D31D4-8FDD-426C-BC19-66650F481099Q37422859-B14B778D-ADF8-43F7-AFAF-923388FBC454Q42222367-9ED8CEC2-CBEE-4DC7-9DB5-BC1600B1F5B4
P2860
Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Structure of the 1-36 N-termin ...... orylated at Ser-16 and Thr-17.
@en
type
label
Structure of the 1-36 N-termin ...... orylated at Ser-16 and Thr-17.
@en
prefLabel
Structure of the 1-36 N-termin ...... orylated at Ser-16 and Thr-17.
@en
P2860
P1433
P1476
Structure of the 1-36 N-termin ...... orylated at Ser-16 and Thr-17.
@en
P2093
Arto Annila
Piero Pollesello
P2860
P304
P356
10.1016/S0006-3495(02)75184-9
P407
P577
2002-07-01T00:00:00Z