|
●
|
Delley CL, Striebel F, Heydenreich FM, Özcelik D, Weber-Ban E. (2011) Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation. J Biol Chem. Dec 30; [Epub ahead of print] Pubmed
|
|
●
|
Ranjan N, Damberger FF, Sutter M, Allain FH, Weber-Ban E* (2010) Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins. J Mol Biol, Jan 28;405(4):1040-55. Pubmed
|
|
●
|
Guth E, Thommen M, Weber-Ban E* (2010) Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. J. Biol. Chem., Feb 11;286(6):4412-9 Pubmed
|
|
●
|
Imkamp F, Striebel F, Sutter M, Ozcelik D, Zimmermann N, Sander P, Weber-Ban E* (2010) Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway. EMBO Rep., 11(10): 791-7. Pubmed Comment
|
|
●
|
Sutter M, Damberger F, Imkamp F, Allain FHT* and Weber-Ban E* (2010) Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the sidechain of its C-terminal glutamate. JACS, 132(16): 5610-2. Pubmed
|
|
●
|
Striebel F, Hunkeler M, Summer H and Weber-Ban E* (2010) The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup’s N-terminus. EMBO Journal, 29(7), 1262–1271. Pubmed Comment
|
|
●
|
Imkamp F, Rosenberger T, Striebel F, Keller PM, Amstutz B, Sander P and Weber-Ban E* (2009) Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. Molecular Microbiology 75(3), 744-754. Pubmed
|
|
●
|
Sutter M, Striebel F, Damberger F, Allain FH*, Weber-Ban E* (2009) A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa. FEBS Letters, 583(19):3151-7. Pubmed
|
|
●
|
Kress W and Weber-Ban E* (2009) The Alternating Power Stroke of a 6-Cylinder AAA Protease Chaperone Engine. Mol Cell 35, 545-547. Pubmed
|
|
●
|
Kress W, Maglica Z and Weber-Ban E* (2009) Clp chaperone-proteases: structure and function. Res Microbiol, 160: 618-628. Pubmed
|
|
●
|
Kress W, Mutschler H and Weber-Ban E* (2009) Both ATPase domains of ClpA are critical for processing of stable protein structures. J Biol Chem, 284(45): 31441-52. Pubmed
|
|
●
|
Kolygo K, Ranjan N, Kress W, Striebel F, Hollenstein K, Neelsen K, Steiner M, Summer H and Weber-Ban E* (2009) Studying Chaperone-Proteases using a Real-Time Approach based on FRET. J Struct Biol 168(2):267-77. Pubmed
|
|
●
|
Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A and Weber-Ban E* (2009) Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 16, 647-651. Pubmed
|
|
●
|
Striebel F, Kress W, and Weber-Ban E* (2009) Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes. Curr Opin Struct Biol 19, 209-17. Pubmed
|
|
●
|
Maglica Z, Kolygo K, and Weber-Ban E* (2009) Optimal Efficiency of ClpAP and ClpXP Chaperone-Proteases Is Achieved by Architectural Symmetry. Structure 17, 508-16. Pubmed Comment
|
|
●
|
Raschle T, Speziga D, Kress W, Moccand C, Gehrig P, Amrhein N, Weber-Ban E and Fitzpatrick TB* (2008) Intersubunit Crosstalk in Pyridoxal 5’-Phosphate Synthase, Coordinated by the C-terminus of the Synthase Subunit. J Biol Chem 284, 7706-18. Pubmed
|
|
●
|
Maglica Z, Striebel F and Weber-Ban E* (2008) An Intrinsic Degradation Tag on the ClpA C-terminus Regulates the Balance of ClpAP Complexes with Different Substrate Specificity. J Mol Biol 384, 503-11. Pubmed
|
|
●
|
Sutter M, Boehringer D, Gutmann S, Günther S, Prangishvili D, Loessner M, Stetter K, Weber-Ban E* and Ban N* (2008) Structural basis of enzyme encapsulation into a bacterial nanocompartment. Nat Struct Mol Biol 15, 939-947. Pubmed Comment
|
|
●
|
Cranz-Mileva S, Imkamp F, Kolygo K, Maglica Z, Kress W and Weber-Ban E* (2008) The Flexible Attachment of the N-Domains to the ClpA Ring Body allows their Use On Demand. J Mol Biol 378, 412-424. Pubmed
|
|
●
|
Kress W, Mutschler H and Weber-Ban E* (2007) Assembly Pathway of an AAA+ Protein: Tracking ClpA and ClpAP Complex Formation in Real Time. Biochemistry 46, 6183-93. Pubmed
|
|
●
|
Summer H, Bruderer R, Weber-Ban EU* (2005) Characterization of a new AAA+ protein from archaea. J Struct Biol 156, 120-129. Pubmed
|
|
●
|
Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A and Bukau B* (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119 (5): 653-65. Pubmed
|
|
●
|
Vetsch M, Puorger C, Spirig T, Grauschopf U, Weber-Ban EU and Glockshuber R* (2004) Pilus chaperones represent a new type of protein-folding catalyst. Nature 431 (7006): 329-33. Pubmed
|
|
●
|
Dougan DA, Weber-Ban EU and Bukau B* (2003) Targeted Delivery of an ssrA-tagged Substrate by the Adapter Protein SspB to its Cognate AAA+ Protein ClpX. Molecular Cell 12 (2), 373-380. Pubmed
|
|
●
|
Reid B , Fenton W, Horwich A L and Weber-Ban EU* (2001) ClpA Mediates Directional Translocation of Substrate Proteins into the ClpP Protease. PNAS 98 (7): 3768-3772. Pubmed
|
|
●
|
Weber-Ban EU, Hur O, Bagwell C, Banik U, Yang LH, Miles EW and Dunn MF* (2001) Investigation of Allosteric Linkages in the Regulation of Tryptophan Synthase: The Roles of Salt Bridges and Monovalent Cations Probed by Site-Directed Mutation, Optical Spectroscopy and Kinetics. Biochemistry 40, 3497-3511. Pubmed
|
|
●
|
Weber-Ban EU, Reid BG, Miranker AD and Horwich AL* (1999) Global Unfolding of a Substrate Protein by the Hsp100 Chaperone ClpA. Nature 401, 90-93. Pubmed Comment
|
|
●
|
Horwich AL, Weber-Ban EU and Finley D* (1999) Chaperone Rings in Protein Folding and Degradation. PNAS 96 (29):11033-40. Pubmed
|
|
●
|
Woehl EU and Dunn MF* (1999) Mechanisms of Monovalent Cation Action in Enzyme Catalysis: The Tryptophan Synthase a-, b- and ab-Reactions. Biochemistry 38, 7131-7141. Pubmed
|
|
●
|
Woehl EU and Dunn MF* (1999) Mechanisms of Monovalent Cation Action in Enzyme Catalysis: The First Stage of the Tryptophan Synthase b-Reaction. Biochemistry 38, 7118-7130. Pubmed
|
|
●
|
Pan P, Woehl EU & Dunn MF* (1997) Protein Architecture, Dynamics, and Allostery in Tryptophan Synthase Channeling. TIBS 22, 22-27. Pubmed
|
|
●
|
Cook PF, Tai CH, Hwang CC, Woehl EU, Dunn MF and Schnackerz KD* (1996) Substitution of Pyridoxal 5'-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides an Effective Test of Mechanism of a-Aminoacrylate Formation. J Biol Chem 271(42), 25842-25849. Pubmed
|
|
●
|
Hwang CC, Woehl EU, Minter DE, Dunn MF and Cook PF* (1996) Kinetic Isotope Effects as a Probe of the b-Elimination Reaction Catalyzed by O-Acetyl Serine Sulfhydrylase. Biochemistry 35, 6358-6365. Pubmed
|
|
●
|
Woehl EU, Tai CH, Dunn MF and Cook PF* (1996) Formation of the a-Aminoacrylate Intermediate Limits the Overall Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Biochemistry 35, 4776-4783. Pubmed
|
|
●
|
Leja CA, Woehl EU and Dunn MF* (1995) Allosteric Linkages between b-Site Covalent transformations and a-Site Activation and Deactivation in the Tryptophan Synthase Bienzyme Complex. Biochemistry 34, 6552-6561. Pubmed
|
|
●
|
Woehl EU and Dunn MF* (1995) Monovalent Metal Ions Play an Essential Role in Catalysis and Intersubunit Communication in the Tryptophan Synthase Bienzyme Complex. Biochemistry 34, 9466-9476. Pubmed
|
|
●
|
Dunn MF*, Brzovic PS, Leja CA, Pan P and Woehl EU (1994) The Roles of Chemical Transformation, Loop Closure, Tunnel Function and Metal Ion Activation in the Tryptophan Synthase Bienzyme Complex. Biochemistry of Vitamin B6 and PQQ (Marino, G., Sannia, G. & Bossa, F., Eds.) pp. 119-224, Birkhäuser Verlag, Basel.
|
|
●
|
Woehl EU and Dunn MF* (1995) The Roles of Na+ and K+ in Pyridoxal Phosphate Enzyme Catalysis. Coordination Chemistry Reviews 144, 147-197.
|
|
●
|
Choudhury K, Sundaramoorthy M, Hickman A, Yonetani T, Woehl EU, Dunn MF and Poulos TL* (1994) Role of the Proximal Ligand in Peroxidase Catalysis. J Biol Chem 32, 20239-20249. Pubmed
|
