Protein synthesis is a dynamic process that tunes the cellular proteome in response to internal and external demands. Metabolic labeling approaches identify the general proteomic response but cannot visualize specific newly synthesized proteins within cells. Here we describe a technique that couples noncanonical amino acid tagging or puromycylation with the proximity ligation assay to visualize specific newly synthesized proteins and monitor their origin, redistribution and turnover in situ
The proteome undergoes complex changes in response to disease, drug treatment, and normal cellular s...
We describe fluorescence labeling of newly synthesized proteins in Escherichia coli cells by means o...
Newly synthesized cellular proteins can be tagged with a variety of metabolic labels that distinguis...
Protein synthesis is a dynamic process that tunes the cellular proteome in response to internal and ...
The non-canonical amino acid labeling techniques BONCAT (bioorthogonal non-canonical amino acid tagg...
Protein translation has been implicated in different forms of synaptic plasticity, but direct in sit...
Modern proteomic methods enable efficient identification of the hundreds or thousands of proteins pr...
Proteins can be rendered susceptible to bio-orthogonal chemistries through metabolic labeling with a...
Proteins in living cells can be made receptive to bioorthogonal chemistries through metabolic labeli...
The non-canonical amino acid labeling techniques BONCAT (bioorthogonal non-canonical amino acid tagg...
Fluorescent labeling of proteins by genetically encoded fluorescent protein tags has enabled an enha...
Measuring the synthesis of new proteins in the context of a much greater number of pre-existing prot...
Summary: Selective identification of newly synthesized proteins is challenging because all proteins,...
Here we describe the application of a new click chemistry method for fluorescent tracking of protein...
AbstractUnderstanding the expression of known and unknown gene products represents one of the key ch...
The proteome undergoes complex changes in response to disease, drug treatment, and normal cellular s...
We describe fluorescence labeling of newly synthesized proteins in Escherichia coli cells by means o...
Newly synthesized cellular proteins can be tagged with a variety of metabolic labels that distinguis...
Protein synthesis is a dynamic process that tunes the cellular proteome in response to internal and ...
The non-canonical amino acid labeling techniques BONCAT (bioorthogonal non-canonical amino acid tagg...
Protein translation has been implicated in different forms of synaptic plasticity, but direct in sit...
Modern proteomic methods enable efficient identification of the hundreds or thousands of proteins pr...
Proteins can be rendered susceptible to bio-orthogonal chemistries through metabolic labeling with a...
Proteins in living cells can be made receptive to bioorthogonal chemistries through metabolic labeli...
The non-canonical amino acid labeling techniques BONCAT (bioorthogonal non-canonical amino acid tagg...
Fluorescent labeling of proteins by genetically encoded fluorescent protein tags has enabled an enha...
Measuring the synthesis of new proteins in the context of a much greater number of pre-existing prot...
Summary: Selective identification of newly synthesized proteins is challenging because all proteins,...
Here we describe the application of a new click chemistry method for fluorescent tracking of protein...
AbstractUnderstanding the expression of known and unknown gene products represents one of the key ch...
The proteome undergoes complex changes in response to disease, drug treatment, and normal cellular s...
We describe fluorescence labeling of newly synthesized proteins in Escherichia coli cells by means o...
Newly synthesized cellular proteins can be tagged with a variety of metabolic labels that distinguis...