Michael R. Lieber

ORCID: 0000-0003-3700-6345
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About
Contact & Profiles
Research Areas
  • DNA Repair Mechanisms
  • T-cell and B-cell Immunology
  • DNA and Nucleic Acid Chemistry
  • CRISPR and Genetic Engineering
  • Immune Cell Function and Interaction
  • Acute Lymphoblastic Leukemia research
  • Cytomegalovirus and herpesvirus research
  • Genomics and Chromatin Dynamics
  • RNA and protein synthesis mechanisms
  • Cancer therapeutics and mechanisms
  • PARP inhibition in cancer therapy
  • Monoclonal and Polyclonal Antibodies Research
  • Immunodeficiency and Autoimmune Disorders
  • Carcinogens and Genotoxicity Assessment
  • Genetics and Neurodevelopmental Disorders
  • Fungal and yeast genetics research
  • Chronic Lymphocytic Leukemia Research
  • Genomic variations and chromosomal abnormalities
  • Bacterial Genetics and Biotechnology
  • Cancer Genomics and Diagnostics
  • Epigenetics and DNA Methylation
  • Lymphoma Diagnosis and Treatment
  • Toxin Mechanisms and Immunotoxins
  • RNA Interference and Gene Delivery
  • Microtubule and mitosis dynamics

University of Southern California
2015-2024

University of California, San Francisco
2024

University of California, Berkeley
2024

National Cancer Centre Singapore
2024

University of California System
2024

Southern California University for Professional Studies
2003-2024

USC Norris Comprehensive Cancer Center
2007-2019

Washington University in St. Louis
1984-2018

Yokohama City University
2018

Keck Hospital of USC
2009-2018

Patients with human severe combined immunodeficiency (SCID) can be divided into those B lymphocytes (B + SCID) and without − SCID). Although several genetic causes are known for SCID, the etiology of SCID has not been defined. Six 14 patients tested were found to carry a mutation recombinase activating gene 1 ( RAG-1 ), RAG-2 , or both. This resulted in functional inability form antigen receptors through recombination links defect one site-specific systems disease.

10.1126/science.274.5284.97 article EN Science 1996-10-04

Dnmt3L is required for the establishment of maternal methylation imprints at imprinting centers (ICs). Dnmt3L, however, lacks conserved catalytic domain common to DNA methyltransferases. In an attempt define its function, we coexpressed DNMT3L with each two known de novo methyltransferases, Dnmt3a and DNMT3B, in human cells monitored by using replicating minichromosomes carrying various ICs as targets. Coexpression DNMT3B led little or no change target methylation. However, coexpression...

10.1073/pnas.262443999 article EN Proceedings of the National Academy of Sciences 2002-12-12

Two conserved DNA sequences serve as joining signals in the assembly of immunoglobulins and T-cell receptors from V-, (D)-, J-coding segments during lymphoid differentiation. We have examined V(D)J recombination a function signal sequence. Plasmid substrates with mutations one or both heptamer-spacer-nonamer were tested for pre-B-cell line active recombination. No variant recombines more efficiently than consensus forms signals. find heptamer sequence to be most important; specifically,...

10.1101/gad.3.7.1053 article EN Genes & Development 1989-07-01

Three genetic complementation groups of rodent cells are defective for both repair x-ray-induced double-strand breaks and V(D)J recombination. Cells from one group lack a DNA end-binding activity that is biochemically antigenically similar to the Ku autoantigen. Transfection complementary (cDNA) encoded 86-kilodalton subunit rescued these mutant activity, x-ray resistance, recombination activity. These results establish role in Furthermore, as component DNA-dependent protein kinase, may...

10.1126/science.7939667 article EN Science 1994-10-14

The 5'-->3'-exonuclease domain of Escherichia coli DNA polymerase I is required for the completion lagging strand synthesis, and yet this not present in any eukaryotic polymerases. Recently, gene encoding functional evolutionary equivalent has been identified. It called FEN-1 mouse human cells RTH1 Saccharomyces cerevisiae. This 42-kDa enzyme Okazaki fragment processing. Here we report that physically interacts with proliferating cell nuclear antigen (PCNA), processivity factor polymerases...

10.1074/jbc.270.38.22109 article EN cc-by Journal of Biological Chemistry 1995-09-01

Structure-specific nucleases catalyze critical reactions in DNA replication, recombination, and repair. Recently, a structure-specific endonuclease, FEN-1, has been purified shown to cleave flap structures. Here, we describe the cloning of murine FEN-1 gene. The nucleotide sequence is highly homologous Saccharomyces cerevisiae genes YKL510 RAD2. We show that truncated RAD2 protein are also endonucleases. substrate specificity implicates branched structures as important intermediates excision...

10.1101/gad.8.11.1344 article EN Genes & Development 1994-06-01
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