Mammalian cell protein expression for biopharmaceutical production

J Zhu - Biotechnology advances, 2012 - Elsevier
Mammalian cell expression has become the dominant recombinant protein production
system for clinical applications because of its capacity for post-translational modification and …

Optimal and consistent protein glycosylation in mammalian cell culture

P Hossler, SF Khattak, ZJ Li - Glycobiology, 2009 - academic.oup.com
In the biopharmaceutical industry, mammalian cell culture systems, especially Chinese
hamster ovary (CHO) cells, are predominantly used for the production of therapeutic …

Synthetic biology goes cell-free

A Tinafar, K Jaenes, K Pardee - BMC biology, 2019 - Springer
Cell-free systems (CFS) have recently evolved into key platforms for synthetic biology
applications. Many synthetic biology tools have traditionally relied on cell-based systems …

Glycosylation: heterogeneity and the 3D structure of proteins

PM Rudd, RA Dwek - Critical reviews in biochemistry and …, 1997 - Taylor & Francis
Glycoproteins generally exist as populations of glycosylated variants (glycoforms) of a single
polypeptide. Although the same glycosylation machinery is available to all proteins that …

Getting the glycosylation right: implications for the biotechnology industry

N Jenkins, RB Parekh, DC James - Nature biotechnology, 1996 - nature.com
Glycosylation is the most extensive of all the posttranslational modifications, and has
important functions in the secretion, antigenicity and clearance of glycoproteins. In recent …

The past, present and future of cell-free protein synthesis

F Katzen, G Chang, W Kudlicki - Trends in biotechnology, 2005 - cell.com
Recent technical advances have revitalized cell-free expression systems to meet the
increasing demands for protein synthesis. Cell-free systems offer several advantages over …

Definition of the bacterial N‐glycosylation site consensus sequence

M Kowarik, NM Young, S Numao, BL Schulz… - The EMBO …, 2006 - embopress.org
The Campylobacter jejuni pgl locus encodes an N‐linked protein glycosylation machinery
that can be functionally transferred into Escherichia coli. In this system, we analyzed the …

Co‐and post‐translational protein folding in the ER

L Ellgaard, N McCaul, A Chatsisvili, I Braakman - Traffic, 2016 - Wiley Online Library
The biophysical rules that govern folding of small, single‐domain proteins in dilute solutions
are now quite well understood. The mechanisms underlying co‐translational folding of …

The amino acid following an asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency

JL Mellquist, L Kasturi, SL Spitalnik… - Biochemistry, 1998 - ACS Publications
Many eukaryotic proteins are modified by Asn-linked (N-linked) glycosylation. The number
and position of oligosaccharides added to a protein by the enzyme …

The Amino Acid at the X Position of an Asn-X-Ser Sequon Is an Important Determinant of N-Linked Core-glycosylation Efficiency (∗)

SH Shakin-Eshleman, SL Spitalnik, L Kasturi - Journal of Biological …, 1996 - ASBMB
N-Linked glycosylation is a common form of protein processing that can profoundly affect
protein expression, structure, and function. N-Linked glycosylation generally occurs at the …