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Biology and Biochemistry

D-Index
51
Citations
12741
World Ranking
16997
National Ranking
7007

Overview

Andreas T Matouschek is affiliated with The University of Texas at Austin in the United States. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology with significant contributions also in Medicine.

Their work focuses on several subfields, including Molecular Biology, Oncology, Cell Biology, Epidemiology, and Infectious Diseases. They have addressed a range of topics, notably Ubiquitin and proteasome pathways, Glycosylation and Glycoproteins Research, Endoplasmic Reticulum Stress and Disease, Peptidase Inhibition and Analysis, Autophagy in Disease and Therapy, DNA Repair Mechanisms, and Genomics and Chromatin Dynamics.

Matouschek's recent publications include:

  • The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates, 2020, Nature Communications
  • Mechanisms of substrate recognition by the 26S proteasome, 2020, Current Opinion in Structural Biology
  • A masked initiation region in retinoblastoma protein regulates its proteasomal degradation, 2020, Nature Communications
  • SARS-CoV-2 viral load is associated with risk of transmission to household and community contacts, 2022, BMC Infectious Diseases
  • Poly(ADP-ribose) binding and macroH2A mediate recruitment and functions of KDM5A at DNA lesions, 2021, The Journal of Cell Biology

Frequent coauthors in Matouschek's publications include:

  • Amit Kumar Singh Gautam (7 collaborations)
  • Caroline Davis (5 collaborations)
  • David E. Clemmer (5 collaborations)
  • Adam Anthony (4 collaborations)
  • Martin F. Jarrold (4 collaborations)

Some of the main publication venues for Matouschek's research are:

  • Nature Communications
  • The Journal of Cell Biology
  • Analytical Chemistry
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Journal of Proteome Research

Best Publications

  • The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding

    Alan R. Fersht;Andreas T Matouschek;Luis Serrano

  • Mapping the transition state and pathway of protein folding by protein engineering

    Andreas T Matouschek;James T. Kellis;Luis Serrano;Alan R. Fersht

  • Transient folding intermediates characterized by protein engineering

    Andreas T Matouschek;James T. Kellis;Luis Serrano;Mark Bycroft

  • Aggregated and monomeric α-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function

    Heather Snyder;Kwame Mensah;Catherine Theisler;Jack M. Lee

  • An unstructured initiation site is required for efficient proteasome-mediated degradation.

    Sumit Prakash;Lin Tian;Kevin S. Ratliff;Rebecca E. Lehotzky

  • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.

    Luis Serrano;James T. Kellis;Pauline Cann;Andreas Matouschek

  • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal

    Cheolju Lee;Michael P Schwartz;Sumit Prakash;Masahiro Iwakura

  • Inefficient degradation of truncated polyglutamine proteins by the proteasome.

    Carina I Holmberg;Kristine E Staniszewski;Kwame N Mensah;Andreas Matouschek

  • Targeting proteins for degradation

    Andreas Matouschek

  • The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.

    Luis Serrano;Andreas T Matouschek;Alan R. Fersht

  • Regulated protein turnover: snapshots of the proteasome in action.

    Sucharita Bhattacharyya;Houqing Yu;Carsten Mim;Andreas T Matouschek

  • Detection and characterization of a folding intermediate in barnase by NMR

    Mark Bycroft;Andreas T Matouschek;James T. Kellis;Luis Serrano

  • The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.

    Andreas Matouschek;Luis Serrano;Alan R. Fersht

  • Cyclophilin catalyzes protein folding in yeast mitochondria.

    Andreas T Matouschek;Sabine Rospert;Karl Schmid;Benjamin S. Glick;Benjamin S. Glick

  • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.

    Andreas Matouschek;Alan R. Fersht

  • Protein unfolding by mitochondria. The Hsp70 import motor.

    Andreas T Matouschek;Nikolaus Pfanner;Wolfgang Voos

  • The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.

    Luis Serrano;Andreas T Matouschek;Alan R. Fersht

  • Intrinsically disordered segments affect protein half-life in the cell and during evolution

    Robin van der Lee;Robin van der Lee;Benjamin Lang;Kai Kruse;Jörg Gsponer

  • Protein unfolding — an important process in vivo?

    Andreas T Matouschek

  • Lack of a Robust Unfoldase Activity Confers a Unique Level of Substrate Specificity to the Universal AAA Protease FtsH.

    Christophe Herman;Sumit Prakash;Chi Zen Lu;Andreas Matouschek

Frequent Co-Authors

Luis Serrano
Luis Serrano Centre for Genomic Regulation
Alan R. Fersht
Alan R. Fersht University of Cambridge
Benjamin S. Glick
Benjamin S. Glick University of Chicago
Gottfried Schatz
Gottfried Schatz University of Basel
Benjamin Wolozin
Benjamin Wolozin Boston University
Sabine Rospert
Sabine Rospert University of Freiburg
Vladimir N. Uversky
Vladimir N. Uversky University of South Florida
Monika Fuxreiter
Monika Fuxreiter University of Padua
M. Madan Babu
M. Madan Babu St. Jude Children's Research Hospital
Carlos Bustamante
Carlos Bustamante Stanford University

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