Optimized signal peptides for the development of high expressing CHO cell lines

L Kober, C Zehe, J Bode - Biotechnology and bioengineering, 2013 - Wiley Online Library
Recombinant biotherapeutic proteins such as monoclonal antibodies are mostly produced in
Chinese hamster ovary (CHO) cells and pharmaceutical companies are interested in an …

Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process

MH Saier Jr, PK Werner, M Müller - Microbiological reviews, 1989 - Am Soc Microbiol
334 SAIER ET AL. ally similar (see sections III and V). Cleavage of amino-terminal signal
sequences by signal peptidases occurs with similar specificities (89, 184, 220, 322); the …

Targeting of proteins into the eukaryotic secretory pathway: signal peptide structure/function relationships

SF Nothwehr, JI Gordon - Bioessays, 1990 - Wiley Online Library
Much progress has been made in recent years regarding the mechanisms of targeting of
secretory proteins to, and across, the endoplasmic reticulum (ER) membrane. Many of the …

Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore

KS Crowley, S Liao, VE Worrell, GD Reinhart… - Cell, 1994 - cell.com
The environment of secretory proteins undergoing translocation across the ER membrane
was determlned by Incorporating fluorescent probes Into nascent chains during translatlon …

The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation

KS Crowley, GD Reinhart, AE Johnson - Cell, 1993 - cell.com
The signal sequence is in an aqueous milieu at an early stage in the translocation of a
nascent secretory protein across the endoplasmic reticulum membrane. This was …

The efficiency of protein compartmentalization into the secretory pathway

CG Levine, D Mitra, A Sharma, CL Smith… - Molecular biology of …, 2005 - Am Soc Cell Biol
Numerous proteins targeted for the secretory pathway are increasingly implicated in
functional or pathological roles at alternative cellular destinations. The parameters that allow …

Flanking signal and mature peptide residues influence signal peptide cleavage

KH Choo, S Ranganathan - BMC bioinformatics, 2008 - Springer
Abstract Background Signal peptides (SPs) mediate the targeting of secretory precursor
proteins to the correct subcellular compartments in prokaryotes and eukaryotes. Identifying …

Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide

EL Snapp, N McCaul, M Quandte, Z Cabartova… - elife, 2017 - elifesciences.org
Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the
endoplasmic reticulum (ER) by its signal peptide during synthesis. Proper gp160 folding in …

[HTML][HTML] N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression.

SH Shakin-Eshleman, AT Remaley… - Journal of Biological …, 1992 - Elsevier
Many eukaryotic proteins are modified by N-linked glycosylation, a process in which
oligosaccharides are added to asparagine residues in the sequon Asn-X-Ser/Thr. However …

Long-lived signal peptide of lymphocytic choriomeningitis virus glycoprotein pGP-C

M Froeschke, M Basler, M Groettrup… - Journal of Biological …, 2003 - ASBMB
Signal peptides (SPs) direct nascent secretory and membrane proteins to the membrane of
the endoplasmic reticulum. They are usually cleaved from the nascent polypeptide by signal …