NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2.
about
Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductaseMembrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientationsThe complete general secretory pathway in gram-negative bacteriaPredicting the orientation of eukaryotic membrane-spanning proteins.Topogenesis of membrane proteins: determinants and dynamics.Identification of cytochrome P450 2C2 protein complexes in mouse liver.Decoding signals for membrane protein assembly using alkaline phosphatase fusions.The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization.Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IVMultiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain.Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge.Mobility of cytochrome P450 in the endoplasmic reticulum membrane.Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain.Heads or tails--what determines the orientation of proteins in the membrane.Efficient assembly of functional cytochrome P450 2C2 requires a spacer sequence between the N-terminal signal anchor and catalytic domains.Function and membrane topology of wild-type and mutated cytochrome P-450c21The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane.The cytoplasmic and N-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum.Solution structure and topology of the N-terminal membrane anchor domain of a microsomal cytochrome P450: prostaglandin I2 synthase.The 'positive-inside rule' applies to thylakoid membrane proteins.Endoplasmic reticulum retention determinants in the transmembrane and linker domains of cytochrome P450 2C1.
P2860
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P2860
NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2.
description
1989 nî lūn-bûn
@nan
1989 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@ast
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@en
type
label
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@ast
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@en
prefLabel
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@ast
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@en
P2860
P356
P1476
NH2-terminal substitutions of ...... of rabbit cytochrome P450IIC2.
@en
P2093
E Szczesna-Skorupa
P2860
P304
P356
10.1083/JCB.108.4.1237
P407
P577
1989-04-01T00:00:00Z