(Q44540221)

English

Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: observations from molecular dynamics simulations

scientific article published on 12 November 2012

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scholarly article

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Europe PubMed Central

PubMed publication ID

4 December 2017

Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: observations from molecular dynamics simulations (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

1 reference

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author name string

Xiaoling Wang

1

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Sandeep Kumar

2

1 reference

Europe PubMed Central

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4 December 2017

Patrick M Buck

3

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Europe PubMed Central

PubMed publication ID

4 December 2017

Satish K Singh

4

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Europe PubMed Central

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4 December 2017

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publication date

12 November 2012

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Europe PubMed Central

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4 December 2017

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Europe PubMed Central

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4 December 2017

81

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Europe PubMed Central

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4 December 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

443-460

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Introduction to current and future protein therapeutics: a protein engineering perspective

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Potent antibody therapeutics by design

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Antibody structure, instability, and formulation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

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Stability of protein pharmaceuticals: an update

1 reference

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Aggregation in protein-based biotherapeutics: computational studies and tools to identify aggregation-prone regions

1 reference

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Impact of product-related factors on immunogenicity of biotherapeutics

1 reference

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21 January 2018

The impact of glycosylation on the biological function and structure of human immunoglobulins.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Dynamic fluctuations of protein-carbohydrate interactions promote protein aggregation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

The impact of glycosylation on monoclonal antibody conformation and stability

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Marketing approval of mogamulizumab: a triumph for glyco-engineering

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

When binding is enough: nonactivating antibody formats.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Refined structure of an intact IgG2a monoclonal antibody

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

The Protein Data Bank

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Design of therapeutic proteins with enhanced stability.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

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Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Scalable molecular dynamics with NAMD

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

GLYCAM06: a generalizable biomolecular force field. Carbohydrates

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Construction, MD Simulation, and Hydrodynamic Validation of an All-Atom Model of a Monoclonal IgG Antibody

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Aggregation-prone motifs in human immunoglobulin G.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Disulfide scrambling in IgG2 monoclonal antibodies: insights from molecular dynamics simulations

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Antibody-antigen interactions: contact analysis and binding site topography.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

VMD: visual molecular dynamics

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

The interpretation of protein structures: Estimation of static accessibility

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Structure of the cross-beta spine of amyloid-like fibrils

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

The structural biology of protein aggregation diseases: Fundamental questions and some answers

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Bacterial inclusion bodies contain amyloid-like structure

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Exploring the sequence determinants of amyloid structure using position-specific scoring matrices

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Physiological responses to protein aggregates: fibrinolysis, coagulation and inflammation (new roles for old factors).

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Oxidized and aggregated recombinant human interferon beta is immunogenic in human interferon beta transgenic mice

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Potential aggregation-prone regions in complementarity-determining regions of antibodies and their contribution towards antigen recognition: a computational analysis

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Protein sequences encode safeguards against aggregation.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Simulations as analytical tools to understand protein aggregation and predict amyloid conformation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Structure of an intermediate state in protein folding and aggregation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Coarse-grained models for protein aggregation.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Coarse-grained simulations of protein aggregation.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Structural and thermodynamic investigations on the aggregation and folding of acylphosphatase by molecular dynamics simulations and solvation free energy analysis.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Immunoglobulin kappa light chain and its amyloidogenic mutants: a molecular dynamics study

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Intrinsic disorder modulates protein self-assembly and aggregation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Characterizing intermolecular interactions that initiate native-like protein aggregation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Rationalization of poor solubility of TGF-β3 using MD simulation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Simulations of human lysozyme: probing the conformations triggering amyloidosis

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Beta edge strands in protein structure prediction and aggregation.

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Engineered human antibody constant domains with increased stability

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Shortened engineered human antibody CH2 domains: increased stability and binding to the human neonatal Fc receptor

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability

1 reference

https://api.crossref.org/works/10.1002%2FPROT.24202

21 January 2018

Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants

1 reference

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21 January 2018

A Role for Protein Misfolding in Immunogenicity of Biopharmaceuticals

1 reference

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21 January 2018

Identifiers

10.1002/PROT.24202

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

ResearchGate publication ID

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