Massachusetts Institute of Technology

Novartis Ag

Glykos Finland Oy

Novartis Pharma Ag

Bernhard Helk

Bernhardt Levy Trout

Veysel Kayser

Naresh Chennamsetty

Vladimir Voynov

Neeraj Jagdish Agrawal

Jari Natunen

Markku Saloheimo

Anne Kanerva

Juhani Saarinen

Ann Westerholm-Parvinen

Anne Huuskonen

Christopher Landowski

Jukka Hiltunen

Annamari Heiskanen

Christian Ostermeier

Benjamin Patrick Sommer

Ramon Wahl

Georg Schmidt

Eero Mustalahti

Anne Leppänen

Heidi Salminen

Provided herein are high-throughput methods for identifying a candidate antibody based on viscosity of the candiate antibody.

Computer-implemented methods of determining protein viscosity

The present disclosure relates to compositions and methods useful for the production of recombinant glycoproteins in filamentous fungal cells, such ascells, wherein at least 90% (mol %), preferably at least 95% of the total neutral N-glycans of said produced recombinant glycoprotein are mammalian-like N-glycans. More specifically, the invention provides a filamentous fungal cell comprising i. one or more mutations that reduces or eliminates one or more endogenous protease activity compared to a parental filamentous fungal cell which does not have said mutation(s); ii. a polynucleotide encoding a heterologous catalytic subunit of oligosaccharyl transferase; iii. a recombinant polynucleotide for increasing &#x3b1;1, 2 mannosidase activity;and, iv. a recombinant polynucleotide encoding said heterologous glycoprotein.

Production of glycoproteins with mammalian-like N-glycans in filamentous fungi

The present disclosure relates to methods and computational tools based, at least in part, on computer simulations that identify hot-spot amino acid residues and binding-region amino acid residues of a protein.

Methods to identify amino acid residues involved in macromolecular binding and uses therefor

The present invention provides methods and computational tools based, at least in part, on computer simulations that identify macromolecule binding regions and aggregation prone regions of a protein. Substitutions may then be made in these aggregation prone regions to engineer proteins with enhanced stability and/or a reduced propensity for aggregation. Similarly, substitutions may then be made in these macromolecule binding regions to engineer proteins with altered binding affinity for the macromolecule.

Methods to identify macromolecule binding and aggregation prone regions in proteins and uses therefor

The present disclosure relates to immunoglobulins with reduced aggregation and compositions, methods of generating such immunoglobulins with computational tools and methods of using such immunoglobulins particularly in the treatment and prevention of disease.

Immunoglobulins with reduced aggregation

The present disclosure relates to immunoglobulins and immunoglobulin conjugates with reduced oligomerization and efficient labeling and compositions, methods of generating such immunoglobulins and immunoglobulin conjugates and methods of using such immunoglobulin conjugates particularly in the treatment and prevention of disease.

Methods for identification of sites for IgG conjugation

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Basel, Switzerland

Bernhard Helk