RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism.
about
Formation of cystine slipknots in dimeric proteinsConformational plasticity of proNGFKinetic and thermodynamic studies reveal chemokine homologues CC11 and CC24 with an almost identical tertiary structure have different folding pathways.A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.Threading a peptide through a peptide: protein loops, rotaxanes, and knots.The pro-peptide of proNGF: structure formation and intramolecular association with NGF.
P2860
RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@en
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@nl
type
label
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@en
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@nl
prefLabel
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@en
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@nl
P2093
P2860
P356
P1433
P1476
RhNGF slow unfolding is not du ...... knot loop-threading mechanism.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560050811
P577
1996-08-01T00:00:00Z