Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
about
Targeting the molecular chaperone SlyD to inhibit bacterial growth with a small molecule.Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases.Novel polysaccharide binding to the N-terminal tail of galectin-3 is likely modulated by proline isomerization.Structural insight into proline / isomerization of unfolded proteins catalyzed by the trigger factor chaperone
P2860
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@ast
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@en
type
label
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@ast
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@en
prefLabel
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@ast
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@en
P2093
P2860
P50
P1433
P1476
Molecular insights into substr ...... peptidyl-prolyl isomerase SlyD
@en
P2093
Kristofer Modig
Pär Nordlund
Ulrich Weininger
P2860
P2888
P356
10.1186/S12915-016-0300-3
P577
2016-09-23T00:00:00Z
P6179
1012272646