Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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Forced degradation of recombinant monoclonal antibodies: A practical guide.Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions

P2860

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P2860

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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http://www.wikidata.org/entity/Q50508037

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

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2017年學術文章

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2017年學術文章

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name

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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type

Item

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Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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prefLabel

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

@en

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

@nl

P1476

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™

@en

P2093

Alexander Benet

http://www.w3.org/2001/XMLSchema#string

Anna Schwendeman

http://www.w3.org/2001/XMLSchema#string

Brandon T Ruotolo

http://www.w3.org/2001/XMLSchema#string

Eric Carlson

http://www.w3.org/2001/XMLSchema#string

Jukyung Kang

http://www.w3.org/2001/XMLSchema#string

Karthik Pisupati

http://www.w3.org/2001/XMLSchema#string

Michael Ford

http://www.w3.org/2001/XMLSchema#string

Sergei Saveliev

http://www.w3.org/2001/XMLSchema#string

Solomon Okbazghi

http://www.w3.org/2001/XMLSchema#string

Steven P Schwendeman

http://www.w3.org/2001/XMLSchema#string

P2860

Charge variants in IgG1: Isolation, characterization, in vitro binding properties and pharmacokinetics in rats

Lookup peaks: a hybrid of de novo sequencing and database search for protein identification by tandem mass spectrometry

Aggregation of human recombinant monoclonal antibodies influences the capacity of dendritic cells to stimulate adaptive T-cell responses in vitro

Post-translational modifications differentially affect IgG1 conformation and receptor binding.

Physicochemical characterization of Remsima.

Immunogenicity of different stressed IgG monoclonal antibody formulations in immune tolerant transgenic mice.

Mammalian cell protein expression for biopharmaceutical production.

Forced degradation of therapeutic proteins.

The challenge of indication extrapolation for infliximab biosimilars.

Post-translational structural modifications of immunoglobulin G and their effect on biological activity.

P304

1197-1209

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P31

scholarly article

P356

10.1080/19420862.2017.1347741

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Yuwei Tian

K Ilker Sen

P577

2017-08-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28787231

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P932

5627586

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Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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P2860

P2860

Biosimilarity under stress: A forced degradation study of Remicade® and Remsima™.

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932