Marlene Belfort

ORCID: 0000-0002-1592-5618
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About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • Bacteriophages and microbial interactions
  • RNA modifications and cancer
  • Bacterial Genetics and Biotechnology
  • RNA Research and Splicing
  • CRISPR and Genetic Engineering
  • Advanced biosensing and bioanalysis techniques
  • Biochemical and Molecular Research
  • Enzyme Structure and Function
  • Genomics and Phylogenetic Studies
  • Monoclonal and Polyclonal Antibodies Research
  • DNA and Nucleic Acid Chemistry
  • RNA Interference and Gene Delivery
  • Chromosomal and Genetic Variations
  • Escherichia coli research studies
  • Viral Infections and Immunology Research
  • Glycosylation and Glycoproteins Research
  • Protein Structure and Dynamics
  • Cancer Research and Treatments
  • RNA regulation and disease
  • Microbial Community Ecology and Physiology
  • Fungal Infections and Studies
  • DNA Repair Mechanisms
  • Viral Infectious Diseases and Gene Expression in Insects
  • Tuberculosis Research and Epidemiology

University at Albany, State University of New York
2015-2024

Texas Children's Hospital
2023

Albany State University
1989-2019

John Wiley & Sons (United States)
2019

Hudson Institute
2019

New York State Department of Health
2004-2018

Wadsworth Center
2005-2018

Institute of Biological, Environmental and Rural Sciences
2016

Children's Hospital of Philadelphia
2014

Rensselaer Polytechnic Institute
1997-2013

Journal Article Protein splicing elements: inteins and exteins — a definition of terms recommended nomenclature Get access Francine B. Perler, Perler * *To whom correspondence should be addressed Search for other works by this author on: Oxford Academic PubMed Google Scholar Elaine O. Davis, Davis 1National Institute Medical ResearchMill Hill, London, UK Gary E. Dean, Dean 2University Cincinnati College MedicineCincinnati, OH 45267-0524 Frederick S. Gimble, Gimble 3Institute Biosciences...

10.1093/nar/22.7.1125 article EN Nucleic Acids Research 1994-01-01

Journal Article Structural conventions for group I introns Get access John M. Burke, Burke * To whom correspondence and reprint requests should be addressed Search other works by this author on: Oxford Academic PubMed Google Scholar Mariene Belfort, Belfort 1Wadsworth Center Laboratories Research, New York State Department of HealthAlbany, NY 12201 Thomas R. Cech, Cech 2Department Chemistry Biochemistry, University ColoradoBoulder, CO 80309, USA Wayne Davies, Davies 3Allelix, Inc.6850...

10.1093/nar/15.18.7217 article EN Nucleic Acids Research 1987-01-01

DsrA is an 87-nt untranslated RNA that regulates both the global transcriptional silencer and nucleoid protein H-NS stationary phase stress response sigma factor RpoS (σ s ). We demonstrate acts via specific RNA:RNA base pairing interactions at hns locus to antagonize translation. also give evidence supports a role for rpoS enhance Negative regulation of by achieved interaction blocking translation RNA. In contrast, results suggest positive occurs formation structure activates cis -acting...

10.1073/pnas.95.21.12456 article EN Proceedings of the National Academy of Sciences 1998-10-13

The Lactococcus lactis group II intron Ll.ltrB is similar to mobile yeast mtDNA introns, which encode reverse transcriptase, RNA maturase, and DNA endonuclease activities for site-specific insertion. Here, we show that the Lactococcal can be expressed spliced efficiently in Escherichia coli. intron-encoded protein LtrA has transcriptase maturase activities, with latter activity shown both vivo vitro, a first any protein. As of associated RNP particles containing excised RNA. Also, cleaves...

10.1101/gad.11.21.2910 article EN Genes & Development 1997-11-01

The continuous sequence of 2.3 kilobases in a 3-kilobase DNA fragment encoding the structural gene for coliphage T4 thymidylate synthase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45) was determined by using M13 dideoxy chain-termination method. From coding information within this and that provided analysis selected CNBr peptides from protein product, primary structure determined. most significant finding these studies is presence 1017-base-pair interruption...

10.1073/pnas.81.10.3049 article EN Proceedings of the National Academy of Sciences 1984-05-01

DsrA is an 87-nucleotide regulatory RNA of Escherichia coli that acts in trans by RNA–RNA interactions with two different mRNAs, hns and rpo S. has opposite effects on these transcriptional regulators. H-NS levels decrease, whereas RpoS (σ s ) increase. Here we show enhances mRNA turnover yet stabilizes S mRNA, either directly or via translation. Computational footprinting approaches led to a refined structure for DsrA, model which interacts the start stop codon regions form coaxial stack....

10.1073/pnas.170281497 article EN Proceedings of the National Academy of Sciences 2000-08-22

To address the effect of host proteins on self-splicing properties group I introns bacteriophage T4, we have purified an activity from Escherichia coli extracts that facilitates both trans- and cis-splicing T4 in vitro. The is attributable to a number proteins, several which are ribosomal proteins. Although these variable abilities stimulate splicing, protein S12 most effective. mitigates negative effects splicing large internal open reading frames (ORFs) common introns. In contrast shown...

10.1101/gad.8.13.1575 article EN Genes & Development 1994-07-01

Group II intron homing occurs primarily by a mechanism in which the RNA reverse splices into DNA target site and is then transcribed intron-encoded protein. The recognized an RNP complex containing protein excised RNA. Here, we analyzed target-site requirements for Lactococcus lactis Ll.LtrB group vitro vivo. Our results suggest model similar to yeast mtDNA introns, first recognizes small number of nucleotide residues double-stranded causes unwinding, enabling base-pair with splicing....

10.1101/gad.14.5.559 article EN Genes & Development 2000-03-01

Inteins are protein-splicing elements, most of which contain conserved sequence blocks that define a family homing endonucleases. Like group I introns encode such endonucleases, inteins mobile genetic elements. Recent crystallography and computer modeling studies suggest consist two structural domains correspond to the endonuclease To determine whether bipartite structure is mirrored by functional independence domain, entire component was deleted from Mycobacterium tuberculosis recA intein....

10.1073/pnas.94.21.11466 article EN Proceedings of the National Academy of Sciences 1997-10-14
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