Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.

Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.

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http://www.wikidata.org/entity/Q41933274
The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopyBactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragmentArginine residues are more effective than lysine residues in eliciting the cellular uptake of onconase.NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimeticsIntercellular adhesion molecule-1 expression in activated eosinophils is associated with mucosal remodeling in nasal polyps.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans
P2860

Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.

Item
http://www.wikidata.org/entity/Q41933274
description
2006 nî lūn-bûn
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2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
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@zh-mo
2006年論文
@zh-tw
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@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.
@en
type
label
Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.
@en
prefLabel
Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
Thermal unfolding of eosinophil cationic protein/ribonuclease 3: a nonreversible process
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932