Phosphorylation alters backbone conformational preferences of serine and threonine peptides.
about
Effects of phosphorylation on the intrinsic propensity of backbone conformations of serine/threonineEvolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites.Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P5 S3 during silicic acid condensation and silica decondensation.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacementsEvaluation of Long-Term Cryostorage of Brain Tissue Sections for Quantitative Histochemistry.
P2860
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P2860
Phosphorylation alters backbone conformational preferences of serine and threonine peptides.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年學術文章
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name
Phosphorylation alters backbon ...... serine and threonine peptides.
@en
Phosphorylation alters backbon ...... serine and threonine peptides.
@nl
type
label
Phosphorylation alters backbon ...... serine and threonine peptides.
@en
Phosphorylation alters backbon ...... serine and threonine peptides.
@nl
prefLabel
Phosphorylation alters backbon ...... serine and threonine peptides.
@en
Phosphorylation alters backbon ...... serine and threonine peptides.
@nl
P2093
P2860
P356
P1433
P1476
Phosphorylation alters backbon ...... serine and threonine peptides
@en
P2093
Geum-Sook Hwang
Su-Yeon Kim
Youngae Jung
P2860
P304
P356
10.1002/PROT.23148
P407
P50
P577
2011-08-30T00:00:00Z