Protein Unfolding in the Cell

Protein Folding in the Cell

Protein Folding in vitro

Book Chapters

Protein Unfolding in the Cell :

Schrader, E.K., Harstad, K.G. & Matouschek, A.
Targeting proteins for degradation.
Nature Chem. Biol. 2009 Nov;5(11):815-22.

Koodathingal, P., Jaffe, N.E., Kraut, D.A., Prakash, S., Fishbain, S., Herman, C. & Matouschek, A.
ATP-dependent proteases differ substantially in their ability to unfold globular proteins.
J. Biol. Chem. 2009 Jul 10;284(28):18674-84.

Prakash, S., Inobe, T., Hatch, A.J. & Matouschek, A.
Substrate selection by the proteasome during degradation of protein complexes.
Nature Chem. Biol. 2009 Jan;5(1):29-36.

Inobe, T., Kraut, D.A. & Matouschek, A.
How to pick a protein and pull at it.
Nature Struct. Molec. Biol. 2008 Nov;15(11):1135-6

Mohammad, M., Prakash, S., Matouschek, A. & Movileanu, L.
Controlling a single protein in a nanopore through electrostatic traps.
J. Amer. Chem. Soc. 2008 Mar 26;130(12):4081-8.

Inobe, T. & Matouschek, A.
Protein targeting to ATP-dependent proteases.
Curr. Opin. Struct. Biol. 2008 Feb;18(1):43-51.

Kraut, D.A., Prakash, S. & Matouschek, A.
To degrade or release: ubiquitin chain remodeling.
Trends Cell Biol. 2007 Sep;17(9):419-21.

Tian L., Matouschek A.
Where to start and when to stop.
Nature Struct. Mol. Biol. 2006 Aug;13(8), 668-70. [PDF]

Tian L, Holmgren RA, Matouschek A.
A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-kappaB.
Nature Struct. Mol. Biol. 2005 Dec;12(12):1045-53.[PDF]

Wilcox AJ, Choy J, Bustamante C, Matouschek A.
Effect of protein structure on mitochondrial import.
Proc. Natl. Acad. Sci. U S A. 2005 Oct 25;102(43):15435-40 [PDF]

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
J. Biol. Chem. 2005 Mar 4;280(9):7562-9 [PDF]

Prakash S., Matouschek A.
Protein unfolding in the cell
Trends Biochem. Sci. 2004 Nov; 29(11), 593-600.[PDF]

Holmberg CI, Staniszewski KE, Mensah KN, Matouschek A, Morimoto RI.
Inefficient degradation of truncated polyglutamine proteins by the proteasome
EMBO J. 2004 Oct 27;23(21):4307-18 [PDF]

Prakash S., Tian L., Ratliff K.S., Lehotzky R. L., Matouschek A.
An unstructured initiation site is required for efficient proteasome-mediated degradation
Nature Struct. Mol. Biol. 2004 Sept; 11(9), 830-837. [PDF]
News and Views by Kenniston JA and Sauer RT in Nature Struct. Mol. Biol. 2004 Sep;11(9):800-2.

Shariff K., Ghosal S., Matouschek A.
The Force Exerted by the Membrane Potential during Protein Import into the Mitochondrial Matrix
Biophys. J. 2004 Jun; 86(6), 3647-3652. [PDF]

Matouschek A. and Bustamante C.
Finding a protein's Achilles heel.
Nature Struct. Biol. 2003 Sep;10(9):674-6 [PDF]

Matouschek A
Protein unfolding - an important process in vivo
Curr. Opin. Struct. Biol. 2003 Feb; 13(1), 98-109. [PDF]

Herman C., Prakash S., Lu C.Z., Matouschek A., Gross C.A.
Lack of a Robust Unfoldase Activity Confers a Unique Level of Substrate Specificity to the Universal AAA Protease FtsH
Mol. Cell 2003 Mar; 11(3), 659-669. [PDF]

Snyder H., Mensah K., Theisler C., Lee J.M., Matouschek A., Wolozin B.
Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function
J. Biol. Chem. 2003 Mar; 278(14), 11753-59. [PDF]

Lee C., Prakash S., Matouschek A.
Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
J. Biol. Chem. 2002 Sept; 277(38), 34760-34765. [PDF]

Huang S., Ratliff K.S., Matouschek A..
Protein unfolding by the mitochondrial membrane potential
Nature Struct. Biol. 2002 Apr; 9(4), 301 - 307. [PDF]
News and Views by Pfanner N and Truscott KN in Nature Struct. Biol. 2002 Apr;9(4):234-6.

Matouschek A., Glick B.S.
Barreling through the outer membrane
Nature Struct. Biol. 2001 Apr;8(4):284-6.

Lee C.*, Schwartz M.P.*, Prakash S., Iwakura M., Matouschek A. ( * :- co-authors )
ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
Mol. Cell. 2001 Mar;7(3):627-37. [PDF]
News and Views by Hochstrasser M and Wang J in Nature Struct. Biol. 2001 Apr;8(4):294-6.

Matouschek A., Pfanner N., Voos W.
Protein unfolding by mitochondria. The Hsp70 import motor
EMBO Rep. 2000 Nov;1(5):404-10. [PDF]

Huang S, Murphy S, Matouschek A.
Effect of the protein import machinery at the mitochondrial surface on precursor stability
Proc. Natl. Acad. Sci. U S A. 2000 Nov 21;97(24):12991-6. [PDF]

Matouschek A.
Recognizing misfolded proteins in the endoplasmic reticulum
Nature Struct. Biol. 2000 Apr;7(4):265-6.

Huang S., Ratliff K.S., Schwartz M.P., Spenner J.M., Matouschek A.
Mitochondria unfold precursor proteins by unraveling them from their N-termini
Nature Struct. Biol. 1999 Dec;6(12):1132-8. [PDF]
News and Views by Hebert DN. in Nature Struct. Biol. 1999 Dec;6(12):1084-5

Schwartz M.P., Matouschek A.
The dimensions of the protein import channels in the outer and inner mitochondrial membranes
Proc. Natl. Acad. Sci. U S A. 1999 Nov 9;96(23):13086-90. [PDF]

Schwartz M.P., Huang S., Matouschek A.
The structure of precursor proteins during import into mitochondria
J. Biol. Chem. 1999 Apr 30;274(18):12759-64. [PDF]

Matouschek A., Azem A., Ratliff K., Glick B.S., Schmid K., Schatz G.
Active unfolding of precursor proteins during mitochondrial protein import
EMBO J. 1997 Nov 17;16(22):6727-36. [PDF]

Book Chapters:

Koodathingal P., Jaffe N.E., Matouschek A.
Protein Unfolding in the Cell
Protein Folding Handbook Part II. 2004;:250-270 WILEY-VCH Verlag GmbH & Co

Matouschek, A. (1997).
Saccharomyces cerevisiae mitochondrial cyclophilin Cpr3/Cyp3.
Guidebook to Molecular chaperones and Protein Folding Catalysts. Gething, M.-J., ed., Oxford University Press.

Matouschek, A., Serrano, L., & Fersht, A.R. (1994).
Analysis of Protein Folding by Protein Engineering.
in "Protein Folding", Frontiers in Molecular Biology Series, IRL Press, Oxford 1994.

Matouschek, A. & Fersht, A.R. (1991).
Use of protein engineering for mapping the transition state and protein folding pathway.
Methods in Enzymology 202, 82-112.

Protein Folding in the Cell :

Rospert S, Looser R, Dubaquie Y, Matouschek A, Glick BS, Schatz G.
Hsp60-independent protein folding in the matrix of yeast mitochondria.
EMBO J. 1996 Feb 15;15(4):764-74.

Matouschek A, Rospert S, Schmid K, Glick BS, Schatz G.
Cyclophilin catalyzes protein folding in yeast mitochondria.
Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6319-23.

Lithgow T, Horst M, Rospert S, Matouschek A, Haucke V, Schatz G
Import and folding of proteins by mitochondria.
Cold Spring Harb Symp Quant Biol. 1995;60:609-17

Protein Folding in vitro :

Matouschek A, Otzen DE, Itzhaki LS, Jackson SE, Fersht AR.
Movement of the position of the transition state in protein folding.
Biochemistry. 1995 Oct 17;34(41):13656-62

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 Eng. 1994 Sep;7(9):1089-95.

Matouschek A, Fersht AR.
Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.
Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7814-8.

Fersht AR, Matouschek A, Serrano L.
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
J Mol Biol. 1992 Apr 5;224(3):771-82.

Serrano L, Kellis JT Jr, Cann P, Matouschek A, Fersht AR.
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.
J Mol Biol. 1992 Apr 5;224(3):783-804.

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.
J Mol Biol. 1992 Apr 5;224(3):805-18.

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.
J Mol Biol. 1992 Apr 5;224(3):819-35.

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.
J Mol Biol. 1992 Apr 5;224(3):837-45.

Serrano L, Matouschek A, Fersht AR.
The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.
J Mol Biol. 1992 Apr 5;224(3):847-59.

Fersht AR, Matouschek A, Sancho J, Serrano L, Vuilleumier S.
Pathway of protein folding.
Faraday Discuss. 1992;(93):183-93.

Fersht AR, Bycroft M, Horovitz A, Kellis JT Jr, Matouschek A, Serrano L.
Pathway and stability of protein folding.
Philos Trans R Soc Lond B Biol Sci. 1991 May 29;332(1263):171-6.

Matouschek A, Fersht AR.
Protein engineering in analysis of protein folding pathways and stability.
Methods Enzymol. 1991;202:82-112.

Bycroft M, Matouschek A, Kellis JT Jr, Serrano L, Fersht AR.
Detection and characterization of a folding intermediate in barnase by NMR.
Nature. 1990 Aug 2;346(6283):488-90.

Matouschek A, Kellis JT Jr, Serrano L, Bycroft M, Fersht AR.
Transient folding intermediates characterized by protein engineering.
Nature. 1990 Aug 2;346(6283):440-5.

Matouschek A, Kellis JT Jr, Serrano L, Fersht AR.
Mapping the transition state and pathway of protein folding by protein engineering.
Nature. 1989 Jul 13;340(6229):122-6.