Andreas Matouschek
American biologist
Andreas Matouschek's AcademicInfluence.com Rankings

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Biology
Andreas Matouschek's Degrees
- PhD Biology Stanford University
- Masters Biology Stanford University
- Bachelors Biology Stanford University
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Why Is Andreas Matouschek Influential?
(Suggest an Edit or Addition)According to Wikipedia, Andreas Matouschek is a biochemist at The University of Texas at Austin, where he is a professor in the College of Natural Sciences. His graduate work with Alan Fersht resulted in the seminal application of phi-value analysis to the study of barnase, a bacterial RNAse used in many protein folding studies. Development of phi value analysis in combination with extensive protein engineering enabled an understanding of the kinetic intermediates during protein folding of barnase. In subsequent postdoctoral work at the University of Basel, he studied how mitochondria refold proteins after importing them. In 1996, he moved to Northwestern University. In 2012, he moved to The University of Texas at Austin.
Andreas Matouschek's Published Works
Published Works
- The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. (1992) (850)
- Mapping the transition state and pathway of protein folding by protein engineering (1989) (652)
- An unstructured initiation site is required for efficient proteasome-mediated degradation (2004) (432)
- Aggregated and Monomeric α-Synuclein Bind to the S6′ Proteasomal Protein and Inhibit Proteasomal Function* (2003) (428)
- Transient folding intermediates characterized by protein engineering (1990) (408)
- ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. (2001) (400)
- The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. (1992) (358)
- Inefficient degradation of truncated polyglutamine proteins by the proteasome (2004) (287)
- Regulated protein turnover: snapshots of the proteasome in action (2014) (242)
- The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. (1992) (230)
- Targeting proteins for degradation. (2009) (226)
- Detection and characterization of a folding intermediate in barnase by NMR (1990) (201)
- The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. (1992) (199)
- Cyclophilin catalyzes protein folding in yeast mitochondria. (1995) (187)
- Intrinsically Disordered Segments Affect Protein Half-Life in the Cell and during Evolution (2014) (185)
- Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. (2003) (173)
- Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. (1993) (165)
- Protein unfolding--an important process in vivo? (2003) (157)
- Defining the geometry of the two-component proteasome degron (2011) (154)
- Active unfolding of precursor proteins during mitochondrial protein import (1997) (143)
- Protein unfolding by mitochondria (2000) (140)
- Protein unfolding by the mitochondrial membrane potential (2002) (136)
- Protein unfolding in the cell. (2004) (135)
- Substrate selection by the proteasome during degradation of protein complexes (2008) (126)
- The dimensions of the protein import channels in the outer and inner mitochondrial membranes. (1999) (120)
- A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB (2005) (120)
- Mitochondria unfold precursor proteins by unraveling them from their N-termini (1999) (118)
- Movement of the position of the transition state in protein folding. (1995) (117)
- Controlling a single protein in a nanopore through electrostatic traps. (2008) (112)
- Paradigms of protein degradation by the proteasome. (2014) (106)
- Disordered Proteinaceous Machines (2014) (103)
- Sequence composition of disordered regions fine-tunes protein half-life (2015) (103)
- The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models. (1992) (95)
- Rad23 escapes degradation because it lacks a proteasome initiation region (2011) (93)
- The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies. (1992) (92)
- Hsp60‐independent protein folding in the matrix of yeast mitochondria. (1996) (92)
- Effect of protein structure on mitochondrial import (2005) (91)
- Recognition of Client Proteins by the Proteasome. (2017) (85)
- Protein engineering in analysis of protein folding pathways and stability. (1991) (78)
- ATP-dependent Proteases Differ Substantially in Their Ability to Unfold Globular Proteins* (2009) (75)
- Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. (1994) (72)
- Concurrent Translocation of Multiple Polypeptide Chains through the Proteasomal Degradation Channel* (2002) (72)
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates (2020) (71)
- Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome* (2016) (53)
- β-Synuclein Reduces Proteasomal Inhibition by α-Synuclein but Not γ-Synuclein* (2005) (53)
- Sequence- and species-dependence of proteasomal processivity. (2012) (52)
- The Structure of Precursor Proteins during Import into Mitochondria* (1999) (49)
- Ubiquitin‐like domains can target to the proteasome but proteolysis requires a disordered region (2016) (47)
- The force exerted by the membrane potential during protein import into the mitochondrial matrix. (2004) (46)
- Protein targeting to ATP-dependent proteases. (2008) (44)
- The Hsp70 import motor (2000) (39)
- A Three-part Signal Governs Differential Processing of Gli1 and Gli3 Proteins by the Proteasome* (2011) (38)
- Top-Down 193-nm Ultraviolet Photodissociation Mass Spectrometry for Simultaneous Determination of Polyubiquitin Chain Length and Topology (2015) (36)
- To degrade or release: ubiquitin-chain remodeling. (2007) (35)
- Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. (2011) (34)
- A Rapid and Versatile Method for Generating Proteins with Defined Ubiquitin Chains. (2016) (33)
- Finding a protein's Achilles heel (2003) (30)
- Barreling through the outer membrane (2001) (28)
- beta-Synuclein reduces proteasomal inhibition by alpha-synuclein but not gamma-synuclein. (2005) (27)
- Pathway of protein folding. (1992) (25)
- An Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome Adaptors (2016) (24)
- Mechanisms of substrate recognition by the 26S proteasome. (2020) (23)
- An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates. (2016) (22)
- Substrate selection by the proteasome through initiation regions (2019) (20)
- Pathway and stability of protein folding. (1991) (19)
- Effect of the protein import machinery at the mitochondrial surface on precursor stability. (2000) (19)
- A masked initiation region in retinoblastoma protein regulates its proteasomal degradation (2020) (17)
- Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation Regions. (2015) (13)
- Where to start and when to stop (2006) (12)
- Mouse Mammary Tumor Virus Signal Peptide Uses a Novel p97-Dependent and Derlin-Independent Retrotranslocation Mechanism To Escape Proteasomal Degradation (2017) (11)
- Poly(ADP-ribose) binding and macroH2A mediate recruitment and functions of KDM5A at DNA lesions (2021) (11)
- SARS-CoV-2 viral load is associated with risk of transmission to household and community contacts (2022) (10)
- An Ancient Portal to Proteolysis (2012) (9)
- Import and folding of proteins by mitochondria. (1995) (8)
- Physical-organic molecular biology: pathway and stability of protein folding (1991) (7)
- How to pick a protein and pull at it (2008) (7)
- Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force (2019) (7)
- Folding pathway enigma (1990) (6)
- Ramping up degradation for proliferation (2016) (5)
- Scalable In Vitro Proteasome Activity Assay. (2018) (5)
- Erratum: Targeting proteins for degradation (2009) (4)
- Recognizing misfolded proteins in the endoplasmic reticulum (2000) (4)
- Poly(ADP-ribose)-binding and macroH2A mediate recruitment and functions of KDM5A at DNA lesions (2020) (4)
- Making it easier to regulate protein stability. (2010) (3)
- Pup grows up: in vitro characterization of the degradation of pupylated proteins (2010) (3)
- A nuclear magnetic resonance study of alamethicin-, δ-haemolysin-, and melittin-induced sodium leakage from large unilamellar vesicles (1988) (3)
- Chance, Destiny, and the Inner Workings of ClpXP (2014) (2)
- Use of Multiple Ion Fragmentation Methods to Identify Protein Cross-Links and Facilitate Comparison of Data Interpretation Algorithms. (2020) (2)
- Design principles that protect the proteasome from self‐destruction (2020) (2)
- Decoding without the cipher (2019) (1)
- 1P041 SELECTING PROTEINS FOR DEGRADATION: THE INITIATION STEP(Proteins-functions, methodology, and protein enigineering,Oral Presentations) (2007) (0)
- How ClpX unfolds GFP in stages by pulling. (2011) (0)
- Simple sequence domain of Ci regulates proteolytic processing (2006) (0)
- A Rapid and Versatile Method to Generate Proteins with Defined Ubiquitin Chains (2016) (0)
- The Thesis Committee for Antony Martin Harvey Certifies that this is the approved version of the following thesis: Evaluation of MRN Complex and ATM Protein-Protein Interactions using Cleavable DSSO Crosslinking and Mass Spectrometry APPROVED BY SUPERVISING COMMITTEE: (2017) (0)
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates (2020) (0)
- Decision letter: Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate (2019) (0)
- ATP-dependent proteases: The cell’s degradation machines (2011) (0)
- Decision letter: Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding (2020) (0)
- 2TA1-03 Optimal spacing between ubiquitin modification and unstructured initiation site for efficient proteasome-mediated degradation(The 47th Annual Meeting of the Biophysical Society of Japan) (2009) (0)
- A masked initiation region in retinoblastoma protein regulates its proteasomal degradation (2020) (0)
- Correction to Disordered Proteinaceous Machines (2015) (0)
- Erratum: Where to start and when to stop (2006) (0)
- 1P034 1YA0915 Defining the geometry of the two-component proteasome degron(Protein:Structure & Function,Early Research in Biophysics Award Candidate Presentations,Early Research in Biophysics Award,The 48th Annual Meeting of the Biophysical Society of Japan) (2010) (0)
- The Thesis Committee for Antony Martin Harvey Certifies that this is the approved version of the following thesis: Evaluation of MRN Complex and ATM Protein-Protein Interactions using Cleavable DSSO Crosslinking and Mass Spectrometry APPROVED BY SUPERVISING COMMITTEE: (2017) (0)
- Proteasome targeting by ubiquitin-like domains (2016) (0)
- Table of Contents (1996) (0)
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