Susanna E. Barrett

ORCID: 0000-0003-3149-6654
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About
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Research Areas
  • Advanced biosensing and bioanalysis techniques
  • CRISPR and Genetic Engineering
  • Biochemical and Structural Characterization
  • Microbial Natural Products and Biosynthesis
  • Glycosylation and Glycoproteins Research
  • DNA and Nucleic Acid Chemistry
  • RNA and protein synthesis mechanisms
  • Cancer Genomics and Diagnostics
  • Hepatitis B Virus Studies
  • Advanced Proteomics Techniques and Applications
  • Plant biochemistry and biosynthesis
  • Chemical Synthesis and Analysis
  • Machine Learning in Bioinformatics
  • interferon and immune responses
  • Cancer Research and Treatments
  • Antimicrobial Peptides and Activities
  • vaccines and immunoinformatics approaches
  • Molecular Biology Techniques and Applications
  • DNA Repair Mechanisms
  • Microbial Metabolism and Applications

University of Illinois Urbana-Champaign
2023-2024

Scripps College
2017-2020

Mitja M. Zdouc Kai Blin Nico L L Louwen Jorge C. Navarro-Muñoz Catarina Loureiro and 95 more Chantal D. Bader Constance B. Bailey Lena Barra Thomas Booth Kenan A. J. Bozhüyük José D. D. Cediel-Becerra Zachary Charlop–Powers Marc G. Chevrette Yit‐Heng Chooi Paul M. D’Agostino Tristan de Rond Elena Del Pup Katherine Duncan Wenjia Gu Novriyandi Hanif Eric J. N. Helfrich Matthew Jenner Yohei Katsuyama Aleksandra E. Korenskaia Daniel Krug Vincent Libis George Lund Shrikant Mantri Kalindi D. Morgan Charlotte Owen Chin‐Soon Phan Benjamin Philmus Zachary L. Reitz Serina L. Robinson Kumar Saurabh Singh Robin Teufel Yaojun Tong Fidele Tugizimana Dana Ulanová Jaclyn M. Winter César Aguilar Daniel Yuri Akiyama Suhad A. A. Al-Salihi Mohammad Alanjary Fabrizio Alberti Gajender Aleti Shumukh A. Alharthi Manuel Rojo Amr A. Arishi Hannah E. Augustijn Nicole E. Avalon J. Abraham Avelar‐Rivas Kyle K. Axt Hellen Bertoletti Barbieri Júlio César Jerônimo Barbosa Lucas Gabriel Barboza Segato Susanna E. Barrett Martin Baunach Christine Beemelmanns Dardan Beqaj Tim Berger Jordan Bernaldo-Agüero Sandra M Bettenbühl Vincent A. Bielinski Friederike Biermann Ricardo Moraes Borges Rainer Borriss Milena Breitenbach Kevin M. Bretscher Michael W Brigham Larissa Buedenbender Brodie W. Bulcock Carolina Cano‐Prieto João Capela Víctor J. Carrión Riley S. Carter Raquel Castelo‐Branco Gabriel Castro‐Falcón Fernanda O. Chagas Esteban Charria‐Girón Ayesha Ahmed Chaudhri Vasvi Chaudhry Hyukjae Choi Yukyung Choi Roya Choupannejad Jakub Chromy Melinda S Chue Donahey Jérôme Collemare Jack A. Connolly Kaitlin E. Creamer Max Crüsemann Arturo Colín-Cruz Andrés Cumsille Jean‐Félix Dallery Luis Caleb Damas-Ramos Tito Damiani Martinus de Kruijff Belén Martín Gerardo Della Sala Jelle Dillen

Abstract Specialized or secondary metabolites are small molecules of biological origin, often showing potent activities with applications in agriculture, engineering and medicine. Usually, the biosynthesis these natural products is governed by sets co-regulated physically clustered genes known as biosynthetic gene clusters (BGCs). To share information about BGCs a standardized machine-readable way, Minimum Information Biosynthetic Gene cluster (MIBiG) data standard repository was initiated...

10.1093/nar/gkae1115 article EN cc-by Nucleic Acids Research 2024-12-09

The RiPP precursor recognition element (RRE) is a conserved domain found in many prokaryotic ribosomally synthesized and post-translationally modified peptide (RiPP) biosynthetic gene clusters (BGCs). RREs bind with high specificity affinity to sequence within the N-terminal leader region of peptides. Lasso biosynthesis involves an RRE-dependent peptidase, which discretely encoded or fused RRE as di-domain protein. Here we leveraged thousands predicted BGCs define RRE:leader peptidase...

10.1021/acs.biochem.2c00700 article EN Biochemistry 2023-02-03

Abstract Ribosomally synthesized and post-translationally modified peptides (RiPPs) comprise a structurally functionally diverse group of natural products. Lasso represent one about 50 known molecular classes RiPPs, which display characteristic [1] rotaxane conformation formed by lasso cyclase. This unique, threaded endows with biological activities remarkable thermal proteolytic stability. The prediction peptide properties, such as substrate compatibility particular cyclase or desired...

10.1101/2024.10.25.620295 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-10-29

Abstract Chemical modifications can enhance the properties of DNA by imparting nuclease resistance and generating more‐diverse physical structures. However, native polymerases generally cannot synthesize significant lengths with modified nucleotide triphosphates. Previous efforts have identified a mutant polymerase I from Thermus aquaticus (SFM19) as capable synthesizing range short, 2′‐modified DNAs; however, it is limited in length products synthesize. Here, we rationally designed...

10.1002/cbic.201600701 article EN ChemBioChem 2017-02-04

DNA is a foundational tool in biotechnology and synthetic biology but limited by sensitivity to DNA-modifying enzymes. Recently, researchers have identified polymerases that can enzymatically synthesize long oligonucleotides of modified (M-DNA) are resistant Most applications require M-DNA be reverse transcribed, typically using RNA transcriptase, back into natural for sequence analysis or further manipulation. Here, we tested commercially available DNA-dependent their ability transcribe...

10.1021/acs.biochem.0c00494 article EN Biochemistry 2020-07-13

Modified‐DNA polymerases have been evolved that can synthesize long strands of modified oligonucleotides. The resulting DNA (M‐DNA) has many high‐value potential applications, such as clinical diagnostics and therapeutics. To fully apply M‐DNA, it must be reverse transcribed back into natural DNA. Previously, error prone transcriptases required for this step, then the to amplified in a separate amplification reaction. Using synthetic template with 2′F nucleotides, we tested panel...

10.1096/fasebj.2020.34.s1.00614 article EN The FASEB Journal 2020-04-01

Recently, several modified‐DNA (M‐DNA) polymerases have been identified which can synthesize long M‐DNAs. While these discoveries enabled new applications of M‐DNA, enzymes typically poor fidelity, possessing error rates orders magnitude worse than native enzymes. However, to date, efforts both quantify rate, as well experimental approaches towards understanding the origin fidelity M‐DNA polymerases, limited. Here, we use a high‐throughput sequencing assay characterize rate leading showed...

10.1096/fasebj.2020.34.s1.00315 article EN The FASEB Journal 2020-04-01
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