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Molecular Biology

D-Index
95
Citations
31455
World Ranking
637
National Ranking
347

Overview

Mark T. Bedford is affiliated with The University of Texas MD Anderson Cancer Center in the United States. Their research primarily spans the field of Biochemistry, Genetics, and Molecular Biology, with a total of 127 publications. Within this main field, they focus extensively on Molecular Biology, Oncology, Infectious Diseases, Plant Science, and Immunology.

The scientist's work addresses a variety of specialized topics including cancer-related gene regulation, epigenetics and DNA methylation, RNA modifications and cancer, genomics and chromatin dynamics, protein degradation and inhibitors, PARP inhibition in cancer therapy, and mosquito-borne diseases and control.

Some of their recent notable papers include:

  • CARM1 regulates replication fork speed and stress response by stimulating PARP1 (2021, Molecular Cell)
  • Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions (2020, Epigenetics & Chromatin)
  • The intrinsic substrate specificity of the human tyrosine kinome (2024, Nature)
  • Discovery of First-in-Class Protein Arginine Methyltransferase 5 (PRMT5) Degraders (2020, Journal of Medicinal Chemistry)
  • SARS-CoV-2 Envelope (E) protein interacts with PDZ-domain-2 of host tight junction protein ZO1 (2021, PLoS ONE)

Mark T. Bedford frequently collaborates with other researchers in the field. Their most frequent co-authors include Lila M. Gierasch, F. Peter Guengerich, Ruma Banerjee, Roger Colbran, and Peter Cresswell.

The scientist's publications appear predominantly in venues such as the Journal of Biological Chemistry with 38 publications, bioRxiv (Cold Spring Harbor Laboratory) with 10 publications, UNC Libraries with 5 publications, Nucleic Acids Research with 4 publications, and Nature Communications with 4 publications.

Best Publications

  • Protein Arginine Methylation in Mammals: Who, What, and Why

    Mark T. Bedford;Steven G. Clarke

  • Arginine methylation an emerging regulator of protein function.

    Mark T. Bedford;Stéphane Richard

  • Protein arginine methyltransferases and cancer.

    Yanzhong Yang;Mark T. Bedford

  • p53 is regulated by the lysine demethylase LSD1

    Jing Huang;Roopsha Sengupta;Alexsandra B. Espejo;Min Gyu Lee

  • Developmental localization of the splicing alternatives of fibroblast growth factor receptor-2 (FGFR2).

    Avi Orr-Urtreger;Mark T. Bedford;Tatjana Burakova;Esther Arman

  • Tudor, MBT and chromo domains gauge the degree of lysine methylation

    Jeesun Kim;Jeremy Daniel;Alexsandra Espejo;Aimee Lake

  • Histone arginine methylation

    Alessandra Di Lorenzo;Mark T. Bedford

  • Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A

    Ying Huang;Jia Fang;Mark T. Bedford;Yi Zhang

  • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.

    Donghang Cheng;Jocelyn Côté;Salam Shaaban;Mark T. Bedford

  • A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse

    Gunnar Schotta;Roopsha Sengupta;Roopsha Sengupta;Stefan Kubicek;Stephen Malin

  • Immunoaffinity Enrichment and Mass Spectrometry Analysis of Protein Methylation

    Ailan Guo;Hongbo Gu;Jing Zhou;Daniel Mulhern

  • Arginine methylation at a glance.

    Mark T. Bedford

  • The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity *

    Adam Frankel;Neelu Yadav;Jaeho Lee;Tina L. Branscombe

  • Small molecule regulators of protein arginine methyltransferases.

    Donghang Cheng;Neelu Yadav;Randall W. King;Maurice S. Swanson

  • Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

    Yanqi Chang;Xing Zhang;John R. Horton;Anup K. Upadhyay

  • Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation

    Scott B Rothbart;Krzysztof Krajewski;Nataliya Nady;Wolfram Tempel

  • Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.

    Xiaobing Shi;Ioulia Kachirskaia;Kay L. Walter;Jen Hao A. Kuo

  • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice.

    Neelu Yadav;Jaeho Lee;Jeesun Kim;Jianjun Shen

  • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

    Mark T. Bedford;Adam Frankel;Michael B. Yaffe;Steven Clarke

  • Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1

    Jocelyn Côté;François Michel Boisvert;Marie Chloé Boulanger;Mark T. Bedford

Frequent Co-Authors

Xiaodong Cheng
Xiaodong Cheng The University of Texas MD Anderson Cancer Center
Steven Clarke
Steven Clarke University of California, Los Angeles
Brian D. Strahl
Brian D. Strahl University of North Carolina at Chapel Hill
Mien Chie Hung
Mien Chie Hung China Medical University
Marius Sudol
Marius Sudol Icahn School of Medicine at Mount Sinai
Stephen V. Frye
Stephen V. Frye University of North Carolina at Chapel Hill
Xiaobing Shi
Xiaobing Shi Van Andel Institute
Sharon Y.R. Dent
Sharon Y.R. Dent The University of Texas MD Anderson Cancer Center
Jianjun Shen
Jianjun Shen The University of Texas MD Anderson Cancer Center
Cheryl H. Arrowsmith
Cheryl H. Arrowsmith Structural Genomics Consortium

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