An improved secretion signal enhances the secretion of model proteins from Pichia pastoris

Secretory Overexpression of Bacillus thermocatenulatus Lipase in Saccharomyces cerevisiae Using Combinatorial Library Strategy

(2018) Shota Kajiwara et al.   Biotechnology Journal

Secretory Overexpression of Bacillus thermocatenulatus Lipase in Saccharomyces cerevisiae Using Combinatorial Library Strategy

(2018) Shota Kajiwara et al.   Biotechnology Journal

Structural characterization of the α-mating factor prepro-peptide for secretion of recombinant proteins in Pichia pastoris

(2017) Sabreen Chahal et al.   GENE

Cargo Capture and Bulk Flow in the Early Secretory Pathway

(2016) Charles Barlowe et al.   Annual Review of Cell and Developmental Biology

Droplet digital PCR-aided screening and characterization ofPichia pastorismultiple gene copy strains

(2016) Elena Cámara et al.   BIOTECHNOLOGY AND BIOENGINEERING

Codon optimization of Saccharomyces cerevisiae mating factor alpha prepro-leader to improve recombinant protein production in Pichia pastoris

(2016) Jungoh Ahn et al.   BIOTECHNOLOGY LETTERS

Refined Pichia pastoris reference genome sequence

(2016) Lukas Sturmberger et al.   JOURNAL OF BIOTECHNOLOGY

Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris

(2015) Verena Puxbaum et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Cultivation strategies to enhance productivity of Pichia pastoris: A review

(2015) V. Looser et al.   BIOTECHNOLOGY ADVANCES

In-silico determination of Pichia pastoris signal peptides for extracellular recombinant protein production

(2015) Aslan Massahi et al.   JOURNAL OF THEORETICAL BIOLOGY

Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production

(2014) Mudassar Ahmad et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting

(2014) Ivy Fitzgerald et al.   Microbial Cell Factories

Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo

(2014) Sebastian Pechmann et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A Network of Cytosolic Factors Targets SRP-Independent Proteins to the Endoplasmic Reticulum

(2013) Tslil Ast et al.   CELL

Pichia pastoris: protein production host and model organism for biomedical research

(2013) Brigitte Gasser et al.   Future Microbiology

The effect of α-mating factor secretion signal mutations on recombinant protein expression in Pichia pastoris

(2013) Geoff P. Lin-Cereghino et al.   GENE

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

(2013) C. K. Barlowe et al.   GENETICS

Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics

(2012) José Luis Corchero et al.   BIOTECHNOLOGY ADVANCES

Protein Translocation across the Rough Endoplasmic Reticulum

(2012) E. C. Mandon et al.   Cold Spring Harbor Perspectives in Biology

Protein Secretion and the Endoplasmic Reticulum

(2012) A. M. Benham   Cold Spring Harbor Perspectives in Biology

N-Terminal Acetylation Inhibits Protein Targeting to the Endoplasmic Reticulum

(2011) Gabriella M. A. Forte et al.   PLOS BIOLOGY

Protein Sorting Receptors in the Early Secretory Pathway

(2010) Julia Dancourt et al.   Annual Review of Biochemistry

A Rapidly Maturing Far-Red Derivative of DsRed-Express2 for Whole-Cell Labeling

(2009) Rita L. Strack et al.   BIOCHEMISTRY

Methods for detection and characterization of lipases: A comprehensive review

(2009) Fariha Hasan et al.   BIOTECHNOLOGY ADVANCES

Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies inSaccharomyces cerevisiae

(2009) J. Andy Rakestraw et al.   BIOTECHNOLOGY AND BIOENGINEERING

Sec61p Is Required for ERAD-L

(2008) Martin Willer et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris

(2008) Hans Marx et al.   Microbial Cell Factories