Alteration of NH2-terminal residues of nerve growth factor affects activity and Trk binding without affecting stability or conformation.
about
Design and nuclear magnetic resonance (NMR) structure determination of the second extracellular immunoglobulin tyrosine kinase A (TrkAIg2) domain construct for binding site elucidation in drug discovery.Mutational studies of conserved residues in the dimer interface of nerve growth factorCharacterization of the recombinant extracellular domain of the neurotrophin receptor TrkA and its interaction with nerve growth factor (NGF)Two restricted sites on the surface of the nerve growth factor molecule independently determine specific TrkA receptor binding and activation.Identification of critical residues within the conserved and specificity patches of nerve growth factor leading to survival or differentiationConformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor.Comparison of nerve growth factor receptor binding models using heterodimeric muteins.The role of the nerve growth factor carboxyl terminus in receptor binding and conformational stability.RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism.Nerve growth factor-induced glutamate release is via p75 receptor, ceramide, and Ca(2+) from ryanodine receptor in developing cerebellar neurons.Deacetylation of p53 after nerve growth factor treatment in PC12 cells as a post-translational modification mechanism of neurotrophin-induced tumor suppressor activation.The nerve growth factor precursor proNGF exhibits neurotrophic activity but is less active than mature nerve growth factor.Distinction between differentiation, cell cycle, and apoptosis signals in PC12 cells by the nerve growth factor mutant delta9/13, which is selective for the p75 neurotrophin receptor.Solution Structure and Internal Motion of a Bioactive Peptide Derived from Nerve Growth FactorIndividual and Combined Effects of TrkA and p75NTRNerve Growth Factor Receptors
P2860
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P2860
Alteration of NH2-terminal residues of nerve growth factor affects activity and Trk binding without affecting stability or conformation.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Alteration of NH2-terminal res ...... ing stability or conformation.
@en
type
label
Alteration of NH2-terminal res ...... ing stability or conformation.
@en
prefLabel
Alteration of NH2-terminal res ...... ing stability or conformation.
@en
P2093
P2860
P356
P1476
Alteration of NH2-terminal res ...... ing stability or conformation.
@en
P2093
P2860
P304
P356
10.1074/JBC.270.11.6278
P407
P577
1995-03-01T00:00:00Z