Geneva, Switzerland

Claudio Soto-Jara


Average Co-Inventor Count = 1.8

ph-index = 3

Forward Citations = 68(Granted Patents)


Location History:

  • New York, NY (US) (1999)
  • Geneva, CH (2002 - 2004)

Company Filing History:


Years Active: 1999-2004

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3 patents (USPTO):Explore Patents

Title: Claudio Soto-Jara: Innovator in Amyloid Research

Introduction

Claudio Soto-Jara is a prominent inventor based in Geneva, Switzerland. He has made significant contributions to the field of amyloid research, particularly in the development of peptide analogs that target amyloid formation. With a total of 3 patents, his work is crucial in the fight against neurodegenerative diseases such as Alzheimer's.

Latest Patents

Soto-Jara's latest patents include innovative peptide analogs that inhibit the formation of β-pleated sheets in amyloid β-peptide. This invention provides pharmaceutical compositions that can be used therapeutically to treat Alzheimer's Disease. Another notable patent involves novel peptides that interact with hydrophobic β-sheet forming clusters of amino acid residues, effectively blocking the abnormal folding of proteins into amyloid-like deposits. These methods are essential for preventing, treating, or detecting disorders associated with amyloid-like fibril deposits.

Career Highlights

Throughout his career, Claudio Soto-Jara has worked with esteemed institutions such as New York University and Axonyx, Inc. His research has been pivotal in advancing our understanding of protein folding and its implications for various diseases.

Collaborations

Soto-Jara has collaborated with notable colleagues, including Marc Henrik Baumann and Blas Frangione. Their combined expertise has furthered the impact of his research in the scientific community.

Conclusion

Claudio Soto-Jara's innovative work in peptide analogs and amyloid research positions him as a key figure in the ongoing battle against neurodegenerative diseases. His contributions are vital for developing effective treatments and understanding the complexities of protein folding.

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