M. Bahler's research while affiliated with The Rockefeller University and other places
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Publication (1)
Synapsin I is a neuron-specific phosphoprotein that is concentrated in the presynaptic nerve terminal in association with the cytoplasmic surface of synaptic vesicles. It has been demonstrated to bundle F-actin in a phosphorylation-dependent manner in vitro, a property consistent with its proposed role in linking synaptic vesicles to the cytoskelet...
Citations
... Proline endopeptidase, for example, can carry out non-specific cleavage at other amino acids [42]. Therefore, we instead turned to the chemical degradation literature and found the following chemical cleavage candidates: 2-nitro-5-thiocyanatobenzoic acid (NTCB) has been widely used to cyanlyate and cleave proteins N-terminal of cysteine [43][44][45][46][47]; 5-5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) also cleaves proteins N-terminal of cysteine, though less efficiently than NTCB [44,46]; N-chlorosuccinimide (NCS) cleaves C-terminal of tryptophan, usually at acidic pH with urea, as the efficiency becomes much lower at neutral and alkaline pH (acidic conditions are known to affect the aggregation state of Aβ, so this was felt to be less optimal [44,48]); iodosobenzoic acid also cleaves C-terminal of tryptophan at acidic pH [49]; hydroxylamine cleaves between asparagine and glycine, but its efficiency is typically low. ...
