Optimized signal peptides for the development of high expressing CHO cell lines
about
Engineering Translation in Mammalian Cell Factories to Increase Protein Yield: The Unexpected Use of Long Non-Coding SINEUP RNAsOptimization of heavy chain and light chain signal peptides for high level expression of therapeutic antibodies in CHO cellsExploring Strong Interactions in Proteins with Quantum Chemistry and Examples of Their Applications in Drug DesignBiochemical Characterization of Human Anti-Hepatitis B Monoclonal Antibody Produced in the Microalgae Phaeodactylum tricornutumDirect production of itaconic acid from liquefied corn starch by genetically engineered Aspergillus terreus.Efficient Secretion of Recombinant Proteins from Rice Suspension-Cultured Cells Modulated by the Choice of Signal PeptideOvercoming the Refractory Expression of Secreted Recombinant Proteins in Mammalian Cells through Modification of the Signal Peptide and Adjacent Amino Acids.Identification and characterization of Toxoplasma gondii aspartic protease 1 as a novel vaccine candidate against toxoplasmosis.Cloning and expression of soluble vascular endothelial growth factors receptor-1 (sFlt-1) fragments in CHO-K1.Improved antibody production in Chinese hamster ovary cells by ATF4 overexpressionRecombinant production of the antibody fragment D1.3 scFv with different Bacillus strains.Phosphatidylethanolamine binding protein 4 (PEBP4) is a secreted protein and has multiple functions.Over-expression of secreted proteins from mammalian cell lines.Expression of recombinant antibodies.The present state of the art in expression, production and characterization of monoclonal antibodies.New Mammalian Expression Systems.Speciated High-Density Lipoprotein Biogenesis and Functionality.A control strategy to investigate the relationship between specific productivity and high-mannose glycoforms in CHO cells.FBN30 in wild Anopheles gambiae functions as a pathogen recognition molecule against clinically circulating Plasmodium falciparum in malaria endemic areas in Kenya.Fine mapping the MHC region identified four independent variants modifying susceptibility to chronic hepatitis B in Han Chinese.Local and transient gene expression primes the liver to resist cancer metastasis.Cell-free synthesis of functional antibodies using a coupled in vitro transcription-translation system based on CHO cell lysatesEfficient and inexpensive transient expression of multispecific multivalent antibodies in Expi293 cells.High-yield production of "difficult-to-express" proteins in a continuous exchange cell-free system based on CHO cell lysates.Modifications of a signal sequence for antibody secretion from insect cells.The emerging role of systems biology for engineering protein production in CHO cells.Alga-Made Anti-Hepatitis B Antibody Binds to Human Fcγ Receptors.Impact of Signal Peptides on Furin-2A Mediated Monoclonal Antibody Secretion in CHO Cells.Comparison of secretory signal peptides for heterologous protein expression in microalgae: Expanding the secretion portfolio for Chlamydomonas reinhardtii.N-terminal or signal peptide sequence engineering prevents truncation of human monoclonal antibody light chains.Strategies and Considerations for Improving Expression of "Difficult to Express" Proteins in CHO Cells.Endoplasmic reticulum-directed recombinant mRNA displays subcellular localization equal to endogenous mRNA during transient expression in CHO cells.Electrostatic engineering of the interface between heavy and light chains promotes antibody Fab fragment production.Engineering a stable CHO cell line for the expression of a MERS-coronavirus vaccine antigen.A rationally designed fully human EGFRvIII:CD3-targeted bispecific antibody redirects human T cells to treat patient-derived intracerebral malignant glioma.
P2860
Q28071440-B9CE86FD-F87B-443A-A0E6-978F0A6778B9Q28543595-61A6A430-D366-47BE-89CA-80B814C6F35CQ28547761-1798151A-975D-407D-962D-E36FB909AC28Q28550050-57C9FBCD-3956-4E85-95B2-9F17EA93BE28Q34091469-D48B61D9-C56A-43EC-B13F-D1506F7B1F04Q35810240-7801967E-6B75-4CFD-98B0-78071C25B95FQ36022211-BB1DE2D8-5171-4D28-B650-D21F56849F09Q36952854-34A8BFBE-F057-44C3-887B-E8A31F8612E5Q37233487-23B9B357-0F57-4FED-ACA2-B3E5965D8EDCQ37369571-4AF0D3FD-554F-4BFE-A5C1-BC3A15F20D98Q37602484-3896C67A-A30C-470A-9D5A-08EDA41B5277Q37679775-02324C92-9F8C-4D33-8236-27E548117C67Q37734441-F490C304-997A-422E-BF6A-F26F0D1CF325Q38126016-8E7F20C9-8CB9-4133-B944-BFC45BF749CDQ38572163-829AB854-FE58-43EB-840B-EA7D7D1543B5Q38701179-19B2AD3B-585D-441E-AD41-5EF193F1A696Q38785650-930200EB-6FC0-4FF6-BF2F-3533EA7BA6D7Q38791462-6EC5CC0C-35A7-4E1F-B19D-45756C9C24C0Q40089062-2B30E773-30A4-4095-A5F3-4C958B41C678Q40105875-ACE8C046-C8C3-413F-BF59-9626CE709E75Q41028280-5BADE3D7-7E51-4E79-AAD5-7D829A78BD8BQ41697029-B9A1DAB5-82B0-407C-9CDC-CF0318C0E95AQ41711395-F734A68F-7502-4665-B620-AD8935367E05Q41718299-236880D3-9636-4AEE-9181-3B50AE5373FBQ41986713-1E107C25-A8F6-4DBB-8F58-AD5B71C3E854Q46453776-0C22F8C2-BBC5-430E-955F-722F4054F5A8Q47341896-B946FBA3-0D1F-49FD-8BD0-29CA53120A5FQ48094732-B81C4085-76FA-4FE5-BAC0-1ECD5360B6BCQ48097183-A58D0956-BD18-42A3-8170-BC47862976F5Q48335716-4E699EB1-9ED1-494B-AFBB-6F499A5CF76FQ50880151-E990BD59-0C31-4BBE-BA46-4D0AF809FA3BQ51510933-08374C55-0831-4123-9770-54EC47FE26F4Q51531891-DB296E46-F075-42FD-AD59-D69FDC53FF26Q51730564-8868E74F-9DA0-4B0F-8896-883B2C692E06Q52716114-918975F6-C0FC-4ADD-B8ED-863C049FA31B
P2860
Optimized signal peptides for the development of high expressing CHO cell lines
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Optimized signal peptides for the development of high expressing CHO cell lines
@ast
Optimized signal peptides for the development of high expressing CHO cell lines
@en
Optimized signal peptides for the development of high expressing CHO cell lines
@nl
type
label
Optimized signal peptides for the development of high expressing CHO cell lines
@ast
Optimized signal peptides for the development of high expressing CHO cell lines
@en
Optimized signal peptides for the development of high expressing CHO cell lines
@nl
prefLabel
Optimized signal peptides for the development of high expressing CHO cell lines
@ast
Optimized signal peptides for the development of high expressing CHO cell lines
@en
Optimized signal peptides for the development of high expressing CHO cell lines
@nl
P2093
P2860
P3181
P356
P1476
Optimized signal peptides for the development of high expressing CHO cell lines
@en
P2093
Christoph Zehe
Juergen Bode
Lars Kober
P2860
P304
P3181
P356
10.1002/BIT.24776
P577
2013-01-17T00:00:00Z