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Greg A. Lazar

Researcher at Genentech

Publications -  12
Citations -  704

Greg A. Lazar is an academic researcher from Genentech. The author has contributed to research in topics: Cell surface receptor & Agonist. The author has an hindex of 7, co-authored 12 publications receiving 494 citations.

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Next generation antibody drugs: pursuit of the 'high-hanging fruit'.

TL;DR: This Review focuses on emerging and novel mechanisms of action of antibodies and innovative targeting strategies that could extend their therapeutic applications, including antibody–drug conjugates, bispecific antibodies and antibody engineering to facilitate more effective delivery.
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An in vitro FcRn- dependent transcytosis assay as a screening tool for predictive assessment of nonspecific clearance of antibody therapeutics in humans

TL;DR: The results strongly support the utility of this assay as a cost-effective and animal-sparing screening tool for evaluation of mAb-based drug candidates during lead selection, optimization, and process development for desired pharmacokinetic properties.
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Attachment Site Cysteine Thiol pKa Is a Key Driver for Site-Dependent Stability of THIOMAB Antibody–Drug Conjugates

TL;DR: Evidence is provided that the site-dependent stability of cys-engineered antibody-drug conjugates may be explained by interactions between the engineered cysteine and the local protein environment that serves to modulate the side-chain thiol pKa.
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Novel Interface for High-Throughput Analysis of Biotherapeutics by Electrospray Mass Spectrometry.

TL;DR: The SampleStream platform is compatible with both native and denaturing electrospray, operates with a throughput up to 15 sec/sample, provides extensive concentration of dilute samples, and affords similar sensitivity to comparable liquid chromatographic methods.
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Susceptibility of Antibody CDR Residues to Chemical Modifications Can Be Revealed Prior to Antibody Humanization and Aid in the Lead Selection Process

TL;DR: A streamlined developability assessment process for therapeutic antibodies from lead discovery to clinical development by comparing the stability of all sequence motifs by mass spectrometric peptide mapping between the rodent parental antibody and the final humanized antibody and observed a linear correlation.