| Year |
Citation |
Score |
| 2023 |
Davis C, Spaller BL, Choi E, Kurrasch J, Chong H, Elsasser S, Finley D, Matouschek A. A strict requirement in proteasome substrates for spacing between ubiquitin tag and degradation initiation elements. Biorxiv : the Preprint Server For Biology. PMID 37609285 DOI: 10.1101/2023.08.08.552540 |
0.388 |
|
| 2020 |
Davis C, Spaller BL, Matouschek A. Mechanisms of substrate recognition by the 26S proteasome. Current Opinion in Structural Biology. 67: 161-169. PMID 33296738 DOI: 10.1016/j.sbi.2020.10.010 |
0.494 |
|
| 2020 |
Tomita T, Huibregtse JM, Matouschek A. A masked initiation region in retinoblastoma protein regulates its proteasomal degradation. Nature Communications. 11: 2019. PMID 32332747 DOI: 10.1038/S41467-020-16003-3 |
0.442 |
|
| 2020 |
Martinez-Fonts K, Davis C, Tomita T, Elsasser S, Nager AR, Shi Y, Finley D, Matouschek A. The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates. Nature Communications. 11: 477. PMID 31980598 DOI: 10.1038/S41467-019-13906-8 |
0.394 |
|
| 2019 |
Tomita T, Matouschek AT. Substrate selection by the proteasome through initiation regions Protein Science. 28: 1222-1232. PMID 31074920 DOI: 10.1002/Pro.3642 |
0.529 |
|
| 2019 |
Gautam AKS, Matouschek AT. Decoding without the cipher Nature Chemical Biology. 15: 210-212. PMID 30770910 DOI: 10.1038/S41589-019-0230-9 |
0.483 |
|
| 2019 |
Matouschek A, Hill CP. Decision letter: Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate Elife. DOI: 10.7554/Elife.52774.Sa1 |
0.37 |
|
| 2018 |
Gautam AKS, Martinez-Fonts K, Matouschek AT. Scalable In Vitro Proteasome Activity Assay. Methods of Molecular Biology. 1844: 321-341. PMID 30242719 DOI: 10.1007/978-1-4939-8706-1_21 |
0.414 |
|
| 2017 |
Byun H, Das P, Yu H, Aleman A, Lozano MM, Matouschek A, Dudley JP. Mouse Mammary Tumor Virus Signal Peptide Uses a Novel p97-Dependent and Derlin-Independent Retrotranslocation Mechanism To Escape Proteasomal Degradation. Mbio. 8. PMID 28351922 DOI: 10.1128/Mbio.00328-17 |
0.456 |
|
| 2017 |
Yu H, Matouschek A. Recognition of Client Proteins by the Proteasome. Annual Review of Biophysics. PMID 28301771 DOI: 10.1146/Annurev-Biophys-070816-033719 |
0.569 |
|
| 2016 |
Bhattacharyya S, Renn JP, Yu H, Marko JF, Matouschek A. An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates. Analytical Biochemistry. PMID 27296635 DOI: 10.1016/J.Ab.2016.05.026 |
0.487 |
|
| 2016 |
Yu H, Kago G, Yellman CM, Matouschek A. Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region. The Embo Journal. PMID 27234297 DOI: 10.15252/Embj.201593147 |
0.478 |
|
| 2016 |
Yu H, Singh Gautam AK, Wilmington SR, Wylie D, Martinez-Fonts K, Kago G, Warburton M, Chavali S, Inobe T, Finkelstein IJ, Babu MM, Matouschek A. Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome. The Journal of Biological Chemistry. PMID 27226608 DOI: 10.1074/Jbc.M116.727578 |
0.398 |
|
| 2016 |
Wilmington SR, Matouschek AT. An Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome Adaptors. Plos One. 11. PMID 27043013 DOI: 10.1371/Journal.Pone.0152679 |
0.541 |
|
| 2016 |
Martinez-Fonts K, Matouschek AT. A Rapid and Versatile Method for Generating Proteins with Defined Ubiquitin Chains. Biochemistry. 55: 1898-1908. PMID 26943792 DOI: 10.1021/Acs.Biochem.5B01310 |
0.502 |
|
| 2016 |
Huibregtse JM, Matouschek A. Ramping up degradation for proliferation. Nature Cell Biology. 18: 141-2. PMID 26820437 DOI: 10.1038/Ncb3306 |
0.478 |
|
| 2015 |
Takahashi K, Matouschek A, Inobe T. Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation Regions. Acs Chemical Biology. PMID 26278914 DOI: 10.1021/Acschembio.5B00554 |
0.517 |
|
| 2015 |
Fishbain S, Inobe T, Israeli E, Chavali S, Yu H, Kago G, Babu MM, Matouschek AT. Sequence composition of disordered regions fine-tunes protein half-life. Nature Structural & Molecular Biology. 22: 214-221. PMID 25643324 DOI: 10.1038/Nsmb.2958 |
0.42 |
|
| 2015 |
Cannon JR, Martinez-Fonts K, Robotham SA, Matouschek A, Brodbelt JS. Top-down 193-nm ultraviolet photodissociation mass spectrometry for simultaneous determination of polyubiquitin chain length and topology. Analytical Chemistry. 87: 1812-20. PMID 25559986 DOI: 10.1021/Ac5038363 |
0.381 |
|
| 2014 |
van der Lee R, Lang B, Kruse K, Gsponer J, Sánchez de Groot N, Huynen MA, Matouschek A, Fuxreiter M, Babu MM. Intrinsically disordered segments affect protein half-life in the cell and during evolution. Cell Reports. 8: 1832-44. PMID 25220455 DOI: 10.1016/J.Celrep.2014.07.055 |
0.472 |
|
| 2014 |
Russell R, Matouschek A. Chance, destiny, and the inner workings of ClpXP. Cell. 158: 479-80. PMID 25083864 DOI: 10.1016/J.Cell.2014.07.009 |
0.35 |
|
| 2014 |
Inobe T, Matouschek AT. Paradigms of protein degradation by the proteasome. Current Opinion in Structural Biology. 24: 156-164. PMID 24632559 DOI: 10.1016/J.Sbi.2014.02.002 |
0.577 |
|
| 2014 |
Bhattacharyya S, Yu H, Mim C, Matouschek A. Regulated protein turnover: snapshots of the proteasome in action. Nature Reviews. Molecular Cell Biology. 15: 122-33. PMID 24452470 DOI: 10.1038/Nrm3741 |
0.48 |
|
| 2012 |
Matouschek A, Finley D. Cell biology. An ancient portal to proteolysis. Science (New York, N.Y.). 337: 813-4. PMID 22904006 DOI: 10.1126/Science.1227301 |
0.547 |
|
| 2012 |
Kraut DA, Israeli E, Schrader EK, Patil A, Nakai K, Nanavati D, Inobe T, Matouschek A. Sequence- and species-dependence of proteasomal processivity. Acs Chemical Biology. 7: 1444-53. PMID 22716912 DOI: 10.1021/Cb3001155 |
0.796 |
|
| 2011 |
Schrader EK, Harstad KG, Holmgren RA, Matouschek A. A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome. The Journal of Biological Chemistry. 286: 39051-8. PMID 21921029 DOI: 10.1074/Jbc.M111.274993 |
0.773 |
|
| 2011 |
Kraut DA, Matouschek A. Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. Acs Chemical Biology. 6: 1087-95. PMID 21815694 DOI: 10.1021/Cb2002285 |
0.506 |
|
| 2011 |
Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. Rad23 escapes degradation because it lacks a proteasome initiation region. Nature Communications. 2: 192. PMID 21304521 DOI: 10.1038/Ncomms1194 |
0.713 |
|
| 2011 |
Inobe T, Fishbain S, Prakash S, Matouschek A. Defining the geometry of the two-component proteasome degron. Nature Chemical Biology. 7: 161-7. PMID 21278740 DOI: 10.1038/Nchembio.521 |
0.723 |
|
| 2010 |
Schrader EK, Wilmington SR, Matouschek A. Making it easier to regulate protein stability. Chemistry & Biology. 17: 917-8. PMID 20851337 DOI: 10.1016/J.Chembiol.2010.09.004 |
0.8 |
|
| 2010 |
Kraut DA, Matouschek A. Pup grows up: in vitro characterization of the degradation of pupylated proteins. The Embo Journal. 29: 1163-4. PMID 20372178 DOI: 10.1038/Emboj.2010.40 |
0.479 |
|
| 2010 |
Inobe T, Prakash S, Fishbain S, Matouschek A. 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) Seibutsu Butsuri. 50: S24-S25. DOI: 10.2142/Biophys.50.S24_5 |
0.599 |
|
| 2009 |
Schrader EK, Harstad KG, Matouschek A. Targeting proteins for degradation. Nature Chemical Biology. 5: 815-22. PMID 19841631 DOI: 10.1038/nchembio.250 |
0.818 |
|
| 2009 |
Koodathingal P, Jaffe NE, Kraut DA, Prakash S, Fishbain S, Herman C, Matouschek A. ATP-dependent proteases differ substantially in their ability to unfold globular proteins. The Journal of Biological Chemistry. 284: 18674-84. PMID 19383601 DOI: 10.1074/Jbc.M900783200 |
0.798 |
|
| 2009 |
Prakash S, Inobe T, Hatch AJ, Matouschek A. Substrate selection by the proteasome during degradation of protein complexes. Nature Chemical Biology. 5: 29-36. PMID 19029916 DOI: 10.1038/Nchembio.130 |
0.746 |
|
| 2009 |
Inobe T, Fishbain S, Prakash S, Matouschek A. 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) Seibutsu Butsuri. 49: S39. DOI: 10.2142/Biophys.49.S39_2 |
0.572 |
|
| 2009 |
Schrader EK, Harstad KG, Matouschek AT. Erratum: Targeting proteins for degradation Nature Chemical Biology. 5: 954-954. DOI: 10.1038/Nchembio1209-954C |
0.755 |
|
| 2008 |
Inobe T, Kraut DA, Matouschek A. How to pick a protein and pull at it. Nature Structural & Molecular Biology. 15: 1135-6. PMID 18985068 DOI: 10.1038/Nsmb1108-1135 |
0.393 |
|
| 2008 |
Mohammad MM, Prakash S, Matouschek A, Movileanu L. Controlling a single protein in a nanopore through electrostatic traps. Journal of the American Chemical Society. 130: 4081-8. PMID 18321107 DOI: 10.1021/Ja710787A |
0.685 |
|
| 2008 |
Inobe T, Matouschek A. Protein targeting to ATP-dependent proteases. Current Opinion in Structural Biology. 18: 43-51. PMID 18276129 DOI: 10.1016/J.Sbi.2007.12.014 |
0.521 |
|
| 2007 |
Kraut DA, Prakash S, Matouschek A. To degrade or release: ubiquitin-chain remodeling. Trends in Cell Biology. 17: 419-21. PMID 17900906 DOI: 10.1016/J.Tcb.2007.06.008 |
0.728 |
|
| 2007 |
Inobe T, Prakash S, Tian L, Matouschek A. 1P041 SELECTING PROTEINS FOR DEGRADATION: THE INITIATION STEP(Proteins-functions, methodology, and protein enigineering,Oral Presentations) Seibutsu Butsuri. 47: S33. DOI: 10.2142/Biophys.47.S33_4 |
0.712 |
|
| 2006 |
Tian L, Matouschek A. Where to start and when to stop Nature Structural and Molecular Biology. 13: 668-670. PMID 16886005 DOI: 10.1038/Nsmb0806-668 |
0.482 |
|
| 2005 |
Tian L, Holmgren RA, Matouschek A. A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB Nature Structural and Molecular Biology. 12: 1045-1053. PMID 16299518 DOI: 10.1038/Nsmb1018 |
0.44 |
|
| 2005 |
Wilcox AJ, Choy J, Bustamante C, Matouschek A. Effect of protein structure on mitochondrial import. Proceedings of the National Academy of Sciences of the United States of America. 102: 15435-40. PMID 16230614 DOI: 10.1073/Pnas.0507324102 |
0.615 |
|
| 2005 |
Snyder H, Mensah K, Hsu C, Hashimoto M, Surgucheva IG, Festoff B, Surguchov A, Masliah E, Matouschek A, Wolozin B. beta-Synuclein reduces proteasomal inhibition by alpha-synuclein but not gamma-synuclein. The Journal of Biological Chemistry. 280: 7562-9. PMID 15591046 DOI: 10.1074/Jbc.M412887200 |
0.729 |
|
| 2004 |
Prakash S, Matouschek A. Protein unfolding in the cell. Trends in Biochemical Sciences. 29: 593-600. PMID 15501678 DOI: 10.1016/J.Tibs.2004.09.011 |
0.752 |
|
| 2004 |
Holmberg CI, Staniszewski KE, Mensah KN, Matouschek A, Morimoto RI. Inefficient degradation of truncated polyglutamine proteins by the proteasome. The Embo Journal. 23: 4307-18. PMID 15470501 DOI: 10.1038/Sj.Emboj.7600426 |
0.788 |
|
| 2004 |
Prakash S, Tian L, Ratliff KS, Lehotzky RE, Matouschek A. An unstructured initiation site is required for efficient proteasome-mediated degradation Nature Structural and Molecular Biology. 11: 830-837. PMID 15311270 DOI: 10.1038/Nsmb814 |
0.734 |
|
| 2003 |
Matouschek A, Bustamante C. Finding a protein's Achilles heel Nature Structural Biology. 10: 674-676. PMID 12942137 DOI: 10.1038/Nsb0903-674 |
0.493 |
|
| 2003 |
Herman C, Prakash S, Lu CZ, Matouschek A, Gross CA. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Molecular Cell. 11: 659-69. PMID 12667449 DOI: 10.1016/S1097-2765(03)00068-6 |
0.694 |
|
| 2003 |
Matouschek AT. Protein unfolding — an important process in vivo? Current Opinion in Structural Biology. 13: 98-109. PMID 12581666 DOI: 10.1016/S0959-440X(03)00010-1 |
0.582 |
|
| 2003 |
Snyder H, Mensah K, Theisler C, Lee J, Matouschek A, Wolozin B. Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function. The Journal of Biological Chemistry. 278: 11753-9. PMID 12551928 DOI: 10.1074/Jbc.M208641200 |
0.74 |
|
| 2002 |
Lee C, Prakash S, Matouschek A. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. The Journal of Biological Chemistry. 277: 34760-5. PMID 12080075 DOI: 10.1074/Jbc.M204750200 |
0.702 |
|
| 2002 |
Huang S, Ratliff KS, Matouschek A. Protein unfolding by the mitochondrial membrane potential. Nature Structural Biology. 9: 301-7. PMID 11887183 DOI: 10.1038/Nsb772 |
0.61 |
|
| 2001 |
Lee C, Schwartz MP, Prakash S, Iwakura M, Matouschek A. ATP-Dependent Proteases Degrade Their Substrates by Processively Unraveling Them from the Degradation Signal Molecular Cell. 7: 627-637. PMID 11463387 DOI: 10.1016/S1097-2765(01)00209-X |
0.737 |
|
| 2001 |
Matouschek A, Glick BS. Barreling through the outer membrane Nature Structural Biology. 8: 284-286. PMID 11276240 DOI: 10.1038/86140 |
0.311 |
|
| 2001 |
Huang S, Murphy S, Matouschek A. Effect of the protein import machinery at the mitochondrial surface on precursor stability. Proceedings of the National Academy of Sciences of the United States of America. 97: 12991-6. PMID 11069283 DOI: 10.1073/Pnas.230243097 |
0.663 |
|
| 2000 |
Matouschek AT, Pfanner N, Voos W. Protein unfolding by mitochondria. The Hsp70 import motor. Embo Reports. 1: 404-410. PMID 11258479 DOI: 10.1093/Embo-Reports/Kvd093 |
0.522 |
|
| 2000 |
Matouschek A. Recognizing misfolded proteins in the endoplasmic reticulum. Nature Structural & Molecular Biology. 7: 265-266. PMID 10742164 DOI: 10.1038/74012 |
0.491 |
|
| 1999 |
Huang S, Ratliff KS, Schwartz MP, Spenner JM, Matouschek A. Mitochondria unfold precursor proteins by unraveling them from their N-termini. Nature Structural Biology. 6: 1132-8. PMID 10581555 DOI: 10.1038/70073 |
0.706 |
|
| 1999 |
Schwartz MP, Matouschek AT. The dimensions of the protein import channels in the outer and inner mitochondrial membranes. Proceedings of the National Academy of Sciences of the United States of America. 96: 13086-13090. PMID 10557277 DOI: 10.1073/Pnas.96.23.13086 |
0.36 |
|
| 1999 |
Schwartz MP, Huang S, Matouschek AT. The Structure of Precursor Proteins during Import into Mitochondria Journal of Biological Chemistry. 274: 12759-12764. PMID 10212260 DOI: 10.1074/Jbc.274.18.12759 |
0.675 |
|
| 1997 |
Matouschek A, Azem A, Ratliff K, Glick BS, Schmid K, Schatz G. Active unfolding of precursor proteins during mitochondrial protein import. The Embo Journal. 16: 6727-36. PMID 9362487 DOI: 10.1093/Emboj/16.22.6727 |
0.466 |
|
| 1996 |
Rospert S, Looser R, Dubaquie Y, Matouschek A, Glick BS, Schatz G. Hsp60-independent protein folding in the matrix of yeast mitochondria. The Embo Journal. 15: 764-74. PMID 8631298 DOI: 10.1002/J.1460-2075.1996.Tb00412.X |
0.5 |
|
| 1995 |
Lithgow T, Horst M, Rospert S, Matouschek A, Haucke V, Schatz G. Import and folding of proteins by mitochondria. Cold Spring Harbor Symposia On Quantitative Biology. 60: 609-17. PMID 8824434 DOI: 10.1101/Sqb.1995.060.01.065 |
0.527 |
|
| 1995 |
Matouschek A, Rospert S, Schmid K, Glick BS, Schatz G. Cyclophilin catalyzes protein folding in yeast mitochondria. Proceedings of the National Academy of Sciences of the United States of America. 92: 6319-23. PMID 7603990 DOI: 10.1073/Pnas.92.14.6319 |
0.506 |
|
| 1995 |
Matouschek A, Otzen DE, Itzhaki LS, Jackson SE, Fersht AR. Movement of the position of the transition state in protein folding Biochemistry. 34: 13656-13662. PMID 7577956 DOI: 10.1021/Bi00041A047 |
0.324 |
|
| 1994 |
Matouschek A, Matthews JM, Johnson CM, Fersht AR. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions Protein Engineering, Design and Selection. 7: 1089-1095. PMID 7831279 DOI: 10.1093/Protein/7.9.1089 |
0.306 |
|
| 1993 |
Matouschek A, Fersht AR. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 90: 7814-7818. PMID 8356089 DOI: 10.1073/Pnas.90.16.7814 |
0.396 |
|
| 1993 |
Fersht AR, Matouschek A, Sancho J, Serrano L, Vuilleumier S. Pathway of protein folding. Faraday Discussions. 183-93. PMID 1290932 DOI: 10.1039/Fd9929300183 |
0.426 |
|
| 1992 |
Serrano L, Matouschek A, Fersht AR. The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models. Journal of Molecular Biology. 224: 847-59. PMID 1569561 DOI: 10.1016/0022-2836(92)90566-3 |
0.384 |
|
| 1992 |
Matouschek A, Serrano L, Meiering EM, Bycroft M, Fersht AR. 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. Journal of Molecular Biology. 224: 837-45. PMID 1569560 DOI: 10.1016/0022-2836(92)90565-2 |
0.452 |
|
| 1992 |
Matouschek A, Serrano L, Fersht AR. The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. Journal of Molecular Biology. 224: 819-35. PMID 1569559 DOI: 10.1016/0022-2836(92)90564-Z |
0.314 |
|
| 1992 |
Serrano L, Matouschek A, Fersht AR. The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. Journal of Molecular Biology. 224: 805-18. PMID 1569558 DOI: 10.1016/0022-2836(92)90563-Y |
0.415 |
|
| 1992 |
Serrano L, Kellis JT, Cann P, Matouschek A, Fersht AR. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. Journal of Molecular Biology. 224: 783-804. PMID 1569557 DOI: 10.1016/0022-2836(92)90562-X |
0.331 |
|
| 1992 |
Fersht AR, Matouschek A, Serrano L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. Journal of Molecular Biology. 224: 771-82. PMID 1569556 DOI: 10.1016/0022-2836(92)90561-W |
0.375 |
|
| 1991 |
Matouschek AT, Fersht AR. Protein engineering in analysis of protein folding pathways and stability Methods in Enzymology. 202: 82-112. PMID 1784198 DOI: 10.1016/0076-6879(91)02008-W |
0.43 |
|
| 1991 |
Fersht AR, Bycroft M, Horovitz A, Kellis JT, Matouschek A, Serrano L. Pathway and stability of protein folding Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 332: 171-176. PMID 1678536 DOI: 10.1098/Rstb.1991.0046 |
0.485 |
|
| 1991 |
Fersht AR, Matouschek AT, Bycroft M, Kellis JT, Serrano L. Physical-Organic Molecular Biology : Pathway And Stability Of Protein Folding Pure and Applied Chemistry. 63: 187-194. DOI: 10.1351/Pac199163020187 |
0.483 |
|
| 1990 |
Bycroft M, Matouschek AT, Kellis JT, Serrano L, Fersht AR. Detection and characterization of a folding intermediate in barnase by NMR Nature. 346: 488-490. PMID 2377210 DOI: 10.1038/346488A0 |
0.412 |
|
| 1990 |
Matouschek AT, Kellis JT, Serrano L, Bycroft M, Fersht AR. Transient folding intermediates characterized by protein engineering Nature. 346: 440-445. PMID 2377205 DOI: 10.1038/346440A0 |
0.362 |
|
| 1989 |
Matouschek AT, Kellis JT, Serrano L, Fersht AR. Mapping the transition state and pathway of protein folding by protein engineering Nature. 340: 122-126. PMID 2739734 DOI: 10.1038/340122A0 |
0.381 |
|
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