Sarepta Therapeutics, Inc.

Agritope, Inc.

Epitope Limited

The United States of America, As Represented by the Secretary, Department of Health and Human Services

University System of Maryland

Orasure Technologies, Inc.

Progeria Research Foundation, Inc.

Other

The Scripps Research Institute

Avi Biopharma, Inc.

Murdoch University

Richard K. Bestwick

Adolph J. Ferro

Lyle R. Brown

Richard Keith Bestwick

Adolph J Ferro

Ryszard M Kole

Jill Anne Kellogg

Diane Elizabeth Frank

Patrick L Iversen

Frederick Joseph Schnell

Pamela Gail Marrone

Dwight D Weller

Denise Carol Manker

Francis S Collins

Andrew S Goldstein

David A Stein

Desmond Rito Jimenez

Sherry Darlene Heins

Helena V Mathews

Leslie B Gordon

Baozhong Cai

Mitchell Martini

Katie Thomas

Kan Cao

Ross Shimabuku

Michael R Erdos

George J Vandemark

Vijaya K Mokkapati

Lyle R Brown

Gunnar J Hanson

Stephen Donald Wilton

Sue Fletcher

Hemant Kumar Roy

Bao Zhong Cai

Benjamin Neuman

Michael Buchmeier

Judit Monis

Fred Joseph Schnell

Antisense molecules capable of binding to a selected target site in the human dystrophin gene to induce exon 44 skipping are described.

Exon skipping compositions for treating muscular dystrophy

Provided are LMNA-targeted antisense oligonucleotides for reducing expression of one or more aberrantly spliced LMNA mRNA isoforms that encode progerin.

Oligonucleotide analogues targeting human LMNA

Antisense oligomers complementary to a selected target site in the human dystrophin gene to induce exon 52 skipping are described.

Exon skipping oligomer conjugates for muscular dystrophy

Provided herein are processes for preparing an oligomer (e.g., a morpholino oligomer). The synthetic processes described herein may be advantageous to scaling up oligomer synthesis while maintaining overall yield and purity of a synthesized oligomer.

Processes for preparing oligomers

The present disclosure relates to antisense oligomers and related compositions and methods for inducing exon inclusion as a treatment for glycogen storage disease type II (GSD-II) (also known as Pompe disease, glycogenosis II, acid maltase deficiency (AMD), acid alpha-glucosidase deficiency, and lysosomal alpha-glucosidase deficiency), and more specifically relates to inducing inclusion of exon 2 and thereby restoring levels of enzymatically active acid alpha-glucosidase (GAA) protein encoded by the GAA gene.

Antisense-induced exon2 inclusion in acid alpha-glucosidase

The present disclosure relates to antisense oligomers and related compositions and methods for decreasing the expression of functional human myostatin and methods for treating muscular dystrophy and related disorders and more specifically relates to inducing exclusion of myostatin exon 2 and thereby reducing the levels of myostatin protein.

Antisense-induced exon exclusion in myostatin

Provided herein are processes for preparing an oligomer (e.g., a morpholino oligomer). The synthetic processes described herein may be advantageous to scaling up oligomersynthesis while maintaining overall yield and purity of a synthesized oligomer.

Growing community of inventors

Corvallis, OR, United States of America

Richard Keith Bestwick