AbstractSecretory signal peptides from individual prokaryotic and eukaryotic species have been analyzed, and the lengths and amino acid compositions of the positively charged amino-terminal region, the central hydrophobic region, and the carboxy-terminal cleavage-region have been compared. We find distinct differences between species in all three regions. Implications for protein secretion in foreign hosts are discussed
AbstractProcessing of human lysozyme with artificially designed signal sequences was examined in an ...
Background and aims: Signal peptides are central to biological processes in that they direct protein...
Targeting signals direct proteins to their extra- or intracellular destination such as the plasma me...
AbstractSecretory signal peptides from individual prokaryotic and eukaryotic species have been analy...
Can orthologous proteins differ in terms of their ability to be secreted? To answer this question, w...
ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until no...
Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experim...
The correct delivery of noncytoplasmic proteins to locations both within and outside the cell depend...
Exported prokaryotic proteins typically contain an amino-terminal extension called the signal peptid...
Abstract The secretion of biotechnologically or pharmaceutically relevant recombinant proteins into ...
We have developed a new method for identification of signal peptides and their cleavage sites based ...
Over the last 5 years proteogenomics (using mass spectroscopy to identify proteins predicted from ge...
Oligonucleotide-directed mutagenesis was employed to investigate the role of the hydrophilic segment...
The definition of a typical sec-dependent bacterial signal peptide contains a positive charge at the...
The passage of proteins across biological membranes via the general secretory (Sec) pathway is a uni...
AbstractProcessing of human lysozyme with artificially designed signal sequences was examined in an ...
Background and aims: Signal peptides are central to biological processes in that they direct protein...
Targeting signals direct proteins to their extra- or intracellular destination such as the plasma me...
AbstractSecretory signal peptides from individual prokaryotic and eukaryotic species have been analy...
Can orthologous proteins differ in terms of their ability to be secreted? To answer this question, w...
ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until no...
Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experim...
The correct delivery of noncytoplasmic proteins to locations both within and outside the cell depend...
Exported prokaryotic proteins typically contain an amino-terminal extension called the signal peptid...
Abstract The secretion of biotechnologically or pharmaceutically relevant recombinant proteins into ...
We have developed a new method for identification of signal peptides and their cleavage sites based ...
Over the last 5 years proteogenomics (using mass spectroscopy to identify proteins predicted from ge...
Oligonucleotide-directed mutagenesis was employed to investigate the role of the hydrophilic segment...
The definition of a typical sec-dependent bacterial signal peptide contains a positive charge at the...
The passage of proteins across biological membranes via the general secretory (Sec) pathway is a uni...
AbstractProcessing of human lysozyme with artificially designed signal sequences was examined in an ...
Background and aims: Signal peptides are central to biological processes in that they direct protein...
Targeting signals direct proteins to their extra- or intracellular destination such as the plasma me...