List of Publications

2012  

[95] Bepperling A., Alte F., Kriehuber T., Braun N., Weinkauf S., Groll M., Haslbeck M. and Buchner J. 
Alternative bacterial two-component small heat shock protein systems 
Proc. Natl. Acad. Sci. USA, 2012, 109 (50), 20407-12

[94] Brouwer A.J., Jonker A., Werkhoven P., Kuo E., Li N., Gallastegui N., Kemmink J., Florea B.I., Groll M., Overkleeft H. and Liskamp R.M. 
Peptido sulfonyl fluorides as new powerful proteasome inhibitors 
J. Med. Chem., 2012, 55 (24), 10995-1003 

[93] Quitterer F., List A., Beck P., Bacher A. and Groll M.
Biosynthesis of the 22nd Genetically Encoded Amino Acid Pyrrolysine: Structure and Reaction Mechanism of PylC at 1.5Å Resolution
J. Mol. Biol., 2012, 424, 270-282

[92] Stein M.L., Beck P., Kaiser M., Dudler R., Becker C.F. and Groll M. 
One-shot NMR analysis of microbial secretions identifies highly potent proteasome inhibitor
Proc. Natl. Acad. Sci. USA, 2012, 109 (45), 18367-71

[91] Huber E.M., Scharf D.H., Hortschansky H.H., Groll M. and Brakhage A.A.
DNA Minor Groove Sensing and Widening by the CCAAT-Binding Complex
Structure, 2012, 20 (10), 1757–68

[90] Beck P., Dubiella C. and Groll M.
Covalent and non-covalent reversible proteasome inhibition 
Biol. Chem. 2012, 393 (10), 1101-20

[89] Archer C.R., Groll M., Stein M.L., Schellenberg B., Clerc J., Kaiser M., Kondratyuk T.P., Pezzuto J.M., Dudler R. and Bachmann A.S. 
Activity Enhancement of Synthetic Syrbactin Proteasome Inhibitor Hybrid and Biological Evaluation in Tumor Cells 
Biochemistry, 2012, 51 (34), 6880-8

[88] Span I., Wang K., Wang W., Zhang Y., Bacher A., Eisenreich W., Li K., Schulz C., Oldfield E. and Groll M. 
Discovery of an Acetylene Hydratase Activity of the Iron-Sulfur Protein IspH
Nature Com., 2012, 3 (1042), 1-8

[87] Huber E.M. and Groll M. 
Inhibitors for the immuno- and constitutive proteasome: current and future trends in drug development 
Angew. Chem. Int. Ed., 2012, 51 (35), 8708–20

[86] Wang W., Wang K., Span I., Jauch J., Bacher A., Groll M. and Oldfield E.
Are Free Radicals Involved in IspH Catalysis? An EPR and Crystallographic Investigation
J. Am. Chem. Soc., 2012, 134, 11225-34

[85] Gersch M., List A., Groll M. and Sieber S.A. 
Insights into the structural network responsible for oligomerization and activity of the bacterial virulence regulator caseinolytic protease P (ClpP)
J. Biol. Chem., 2012, 287, 9484-94

[84] Schmid A.B., Lagleder S., Gräwert M.A., Röhl A., Hagn F., Wandinger S.K., Cox M.B., Demmer O., Richter K., Groll M., Kessler H., Buchner J. 
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop 
EMBO J., 2012, 31, 1506-17 

[83] Huber, E. and Groll, M.
The 19S Cap Puzzle: A New Jigsaw Piece  
Structure, 2012, 20, 387-8

[82] Gallastegui N. and Groll M. 
Analysing properties of proteasome inhibitors using kinetic and x-ray crystallographic studies 
Methods Mol. Biol., 2012, 832, 373-90.

[81] Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C., Groettrup M. and Groll M.
Immuno- and Constitutive Proteasome Crystal Structures Reveal Differences in Substrate and Inhibitor Specificity 
Cell,  2012, 148, 727–38

[80] Span I., Gräwert T., Bacher A., Eisenreich W. and Groll M.
Crystal structures of mutant IspH proteins reveal a rotation of the substrate's hydroxymethyl group during catalysis 
J. Mol. Biol., 2012, 416, 1-9

[79] Gallastegui N., Beck P., Arciniega M., Huber R., Hillebrand S. and Groll M.
Hydroxyureas as noncovalent proteasome inhibitors
Angew. Chem. Int. Ed., 2012, 51, 247-9

[78] Quitterer F, List A, Eisenreich W, Bacher A, Groll M. 
Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis 
Angew. Chem. Int. Ed., 2012, 51, 1339-42

[77] Gräwert, M.A, Groll, M.
Exploiting nature's rich source of proteasome inhibitors as starting points in drug development
Chem. Commun., 2012, 48, 1364-78

2011

[76] Behrendt CT, Kunfermann A, Illarionova V, Matheeussen A, Pein MK, Gräwert T, Kaiser J, Bacher A, Eisenreich W, Illarionov B, Fischer M, Maes L, Groll M, Kurz T.
Reverse fosmidomycin derivatives against the antimalarial drug target IspC (Dxr)
J. Med. Chem., 2011, 54, 6796-802

[75] Groll M, Potts BC.
Proteasome Structure, Function, and Lessons Learned from Beta-Lactone Inhibitors
Curr. Top. Med. Chem., 2011, 11, 2850-78

[74] Gräwert T, Groll M, Rohdich F, Bacher A, Eisenreich W.
Biochemistry of the non-mevalonate isoprenoid pathway
Cell Mol. Life Sci., 2011, 68, 3797-814

[73] Korotkov, V.S. Ludwig, A., Larionov, O., Lygin, A., Groll M., de Meijere, A.
Synthesis and biological activity of optimized belactosin C congeners
Org. Biomol. Chem., 2011, 22, 7791-8

[72] Potts BC, Albitar MX, Anderson KC, Baritaki S, Berkers C, Bonavida B, Chandra J, Chauhan D, Cusack JC Jr, Fenical W, Ghobrial IM, Groll M, Jensen PR, Lam KS, Lloyd GK, McBride W, McConkey DJ, Miller CP, Neuteboom ST, Oki Y, Ovaa H, Pajonk F, Richardson PG, Roccaro AM, Sloss CM, Spear MA, Valashi E, Younes A, Palladino MA.
Marizomib, a Proteasome Inhibitor for All Seasons: Preclinical Profile and a Framework for Clinical Trials
Current Cancer Drug Targets, 2011,11, 254-84

[71] Gräwert M.A., Gallastegui N., Stein M., Schmidt B., Kloetzel PM., Huber R. and Groll M.
Elucidation of α-Keto-Aldehyde Binding Mechanism Reveals a Novel Lead Structure Motif for Proteasome Inhibition
Angew. Chem. Int. Ed., 2011, 50, 542-44

[70] Clerc J., Li N., Krahn D., Groll M., Bachmann A.S., Florea B.I., Overkleeft H.S., Kaiser M. (2011)
The natural product hybrid of Syringolin A and Glidobactin A synergizes proteasome inhibition potency with subsite selectivity
Chem. Commun., 2011, 47, 385-7

2010

[69] Lee M., Gräwert T., Quitterer F., Rohdich F., Eppinger J., Eisenreich W., Bacher A., Groll M. 
Biosynthesis of isoprenoids: crystal structure of the [4Fe-4S] cluster protein IspG
J. Mol. Biol., 2010, 404, 600-10

[68] Alte F., Stengel A., Philipp Benz J.P., Petersen E., Soll J., Groll M., Bölter B.
Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner
Proc. Natl. Acad. Sci. USA, 2010, 107, 19260-5

[67] Gräwert T., Span I., Bacher A., Groll M.
Reductive dehydroxylation of allyl alcohols by IspH protein
Angew. Chem. Int. Ed. Engl., 2010, 49, 8802-9.

[66] Clerc J., Schellenberg B., Groll M., Bachmann A.S., Huber R., Dudler R., Kaiser M.
Convergent Synthesis and Biological Evaluation of Syringolin A and Derivatives as Eukaryotic 20S Proteasome Inhibitors
Eur. J. Org. Chem., 2010, 21, 3991-4003

[65] Behrendt C.T., Kunfermann A., Illarionova V., Matheeussen A., Gräwert T., Groll M., Rohdich F., Bacher A., Eisenreich W., Fischer M., Maes L., Kurz T. 
Synthesis and antiplasmodial activity of highly active reverse analogues of the antimalarial drug candidate fosmidomycin
Chem. Med. Chem., 2010, 5, 1673-6.

[64] Groll M., Gallastegui N., Maréchal X., Le Ravalec V., Basse N., Richy N., Genin E., Huber R., Moroder L., Vidal J., Reboud-Ravaux M.
20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A
Chem. Med. Chem., 2010, 5,1701-5.

[63] Gallastegui N., Groll M.
The 26S proteasome: assembly and function of a destructive machine
Trends Biochem. Sci., 2010, 35, 634-42

[62] Geist J.G., Lauw S., Illarionova V., Illarionov B., Fischer M., Gräwert T., Rohdich F., Eisenreich W., Kaiser J., Groll M., Scheurer C., Wittlin S., Alonso-Gómez J.L., Schweizer W.B., Bacher A., Diederich F.
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium tuberculosis and Plasmodium falciparum
Chem. Med. Chem., 2010, 5, 1092-101.

[61] Gräwert T., Span I., Eisenreich W., Rohdich F., Eppinger J., Bacher A., Groll M.
Probing the reaction mechanism of IspH protein by x-ray structure analysis
Proc. Natl. Acad. Sci. U S A., 2010, 107, 1077-81

2009

[60] Gallastegui N. and Groll M.
How ATPases unravel a mystery
Structure, 2009, 17, 1279-81

[59] Clerc J., Florea B.I., Kraus M., Groll M., Huber R., Bachmann A.S., Dudler R., Driessen,C., Overkleeft H.S., and Kaiser M.
Syringolin A selectively labels the 20S proteasome in murine EL4 and wildtype and bortezomib adapted leukemic cells lines
Chembiochem., 2009, 10, 2638-43

[58] Groll M., McArthur K.A., Macherla V.R., Manam R.R., and Potts B.C. 
Snapshots of the Fluorosalinosporamide/20S Complex Offer Mechanistic Insights for Fine Tuning Proteasome Inhibition
J. Med. Chem., 2009, 10;52, 5420-8

[57] Gräwert T., Rohdich F., Span I., Bacher A., Eisenreich W., Eppinger J. and Groll M
Structure of active IspH enzyme provides mechanistic insights into substrate reduction
Angew. Chem. Int. Ed., 2009, 48, 5756-59

[56] Clerc J., Groll M., Illich D.J., Bachmann A.S., Huber R., Schellenberg B., Dudler R., Kaiser M.
Synthetic and structural studies on the syrbactin natural products reveal critical determinants of their selectivity and potency of proteasome inhibition
Proc. Natl. Acad. Sci. USA, 2009, 106, 6507-12

[55] Groll M., Huber R. and Moroder L.
The persisting challenge of selective and specific proteasome inhibition
J. Pept.Sci., 2009, 15 , 58-66

[54] Sollner S., Schober M., Wagner A., Prem A., Lorkova L., Palfey B.A., Groll M. and Macheroux P.
Quinone reductase acts as a redox switch of the 20S yeast proteasome
EMBO Rep., 2009, 10, 65-70

2008

[53] Manam RR, McArthur KA, Chao TH, Weiss J, Ali JA, Palombella VJ, Groll M, Lloyd GK, Palladino MA, Neuteboom ST, Macherla VR, Potts BC.
Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides
J. Med. Chem., 2008, 51, 6711-24

[52] Groll M, Balskus EP, Jacobsen EN 
Structural analysis of spiro beta-lactone proteasome inhibitors
J. Am. Chem. Soc., 2008, 130, 14981-3

[51] Schreiner P., Chen X., Husnjak K., Randles L., Zhang N., Elsasser S., Finley D., Dikic I., Walters K. and Groll M.
Ubiquitin docking at the proteasome via a novel PH domain interaction
Nature, 2008, 453 (7194), 548-52

[50] Hines J., Groll M., Fahnestock M. and Crews CM. 
Proteasome Inhibition by Fellutamide B Induces Nerve Growth Factor Synthesis
Chem. & Biol., 2008, 15, 501-12

[49] Groll M., Schellenberg B., Bachmann AS., Archer CR., Huber R., Powell TK., Lindow S., Kaiser M. and Dudler R. 
A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism
Nature, 2008, 452, 755-8

2007

[48] Borissenko L. and Groll M. 
Diversity of proteasomal missions: fine tuning of the immune response
Biol. Chem., 2007, 388 (9), 947-55

[47] Horwitz A., Navon A., Groll M., Smith DM., Reis C. and Goldberg AL.
ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in archaea
J. Biol. Chem., 2007, 282, 22921-9

[46] Borissenko L. and Groll M.
20S proteasome and its inhibitors: crystallographic knowledge for drug development
Chemical Reviews, 2007, 107, 687-717

[45] Bredemeier R., Schlegel T., Ertel F., Vojta A., Borissenko L., Bohnsack M.T., Groll M., von Haeseler A. and Schleiff E.
Functional and phylogenetic properties of the pore forming beta-barrel transporters of the Omp85 family
J. Biol. Chem., 2007, 282, 1882-90

2006

[44] Mokranjac D., Bourenkov G., Hell K., Neupert W. and Groll M.
Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor
EMBO J, 2006, 25, 4675-85

[43] Groll M., Larionov OV., Huber R. and deMeijere A.
Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation
Proc. Natl. Acad. Sci. USA, 2006, 103, 4576-79

[42] Groll M., Berkers CR., Ploegh HL. and Ovaa H.
Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
Structure, 2006, 14, 451-6

[41] Groll M., Huber R. and Potts B. 
Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding
J. Am. Chem. Soc., 2006, 128, 5136-41

[40] Groll M., Götz M., Kaiser M., Weyher E. and Luis Moroder 
TMC-95 based inhibitor design provides evidence for the catalytic versatility of the proteasome
Chem. & Biol., 2006, 13, 607-14

2005

[39] Groll M. and Huber R.
Purification, crystallization and X-ray analysis of the yeast 20S proteasomes
Methods Enzymol., 2005, 398, 329-36

[38] Goettig P., Brandstetter H., Groll M., Göhring W., Konarev P., Svergun DI., Huber R. and Kim J.
X-ray snapshots of peptide processing in mutants of tricorn interacting factor F1 from T. acidophilum
J. Biol. Chem., 2005, 280, 33387-96

[37] Locher M., Lehnert B., Krauss K., Heesemann J., Groll M. and Wilharm G. 
Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT
J. Biol. Chem., 2005, 280, 31149-55

[36] Braun H., Umbreen S., Groll M., Kuckelkorn U., Wiegand E., Drung I., Kloetzel P., Schmidt B. 
Tripeptide mimetics inhibit the 20S proteasome by covalent bonding to the active threonines
J. Biol. Chem., 2005, 280, 28394-401

[35] Groll M., Bochtler M., Brandstetter H., Clausen T. and Huber R.
Molecular machines for protein degradation
Chembiochem., 2005, 6, 222-256

[34] Borissenko L. and Groll M.
Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes
J. Mol. Biol., 2005, 346, 1207-19

2004

[33] Groll M. and Huber R. 
Inhibitors of the eukaryotic 20S proteasome core particle
Biochim Biophys Acta, 2004, 1695, 33-44

[32] Ye1 J., Osborne A., Groll M. and Rapoport T.
RecA-like Motor ATPases - lessons from structures
Biochim Biophys Acta, 2004, 1659, 1-18

[31] Kaiser M.; Groll M., Siciliano C., Assfalg-Machleidt I., Weyher E., Kohno J., Milbradt A., Renner C., Huber R. and Moroder L. 
Inhibition of eukaryotic 20S proteasome by TMC-95A analogues: factorising structural determinants
Chembiochem., 2004, 5, 1256-66

[30] Neumayer W., Groll M., Lehmann V., Antoneka U., Kahler S., Heesemann J. and Wilharm G. 
Yersinia enterocolitica type III secretion chaperone SycH. Recombinant expression, purification, characterisation, and crystallisation
Protein Expr Purif., 2004, 35, 237-47

[29] Kaiser M., Milbradt AG., Siciliano C., Machleidt I., Machleidt W., Groll M., Renner C. and Moroder L.
TMC-95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors
Chemistry & Biodiversity, 2004, 1, 161-73

2003

[28] Groll M. and Clausen T. 
Molecular shredders: How proteasomes fulfill their job
Curr. Opin. Struc Biol., 2003, 13, 665-73

[27] Kaiser M., Siciliano C., Assfalg-Machleidt I., Groll M., Milbradt AG. and Moroder L.
Synthesis of a TMC-95A Ketomethylene Analogue by Cyclization via Intramolecular Suzuki Coupling
Org Lett., 2003, 18;5, 3435-7

[26] Groll M. and Huber R.
Substrate access and processing by the 20S proteasome core particle
Internat. J. Biochem. & Cell Biol., 2003, 5, 606-16

[25] Groll M., Brandstetter H., Bartunik HD., Bourenkow G. and Huber R.
Investigations on the maturation and regulation of archaebacterial proteasomes
J. Mol. Biol., 2003, 327, 75-83

2002

[24] Kim JS., Groll M., Musiol H.J., Behrendt R., Kaiser M., Moroder L., Huber R., and Brandstetter H. 
Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum
J. Mol. Biol., 2002, 324, 1041-50

[23] Brandstetter H., Kim JS., Groll M., Göttig P. and Huber R. 
Structural basis for the processive protein degradation by tricorn protease
Biol. Chem., 2002, 383, 1157-65

[22] Göttig P., Groll M., Kim JS. and Brandstetter H. 
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its mechanism
EMBO J., 2002, 21, 5343-51

[21] Groll M., Nazif T., Huber R. and Bogyo M. 
Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome
Chem. & Biol., 2002, 9, 655-62

[20] Kaiser M., Groll M., Renner C., Huber R. and Moroder L.
The core structure of TMC-95A is a promising lead for reversible proteasome inhibition
Angew. Chem. Int. Ed., 2002, 41/5, 780-3

2001

[19] Brandstetter H., Kim JS., Groll M. and Huber R.
Crystal structure of the tricorn protease reveals a protein disassembly line
Nature, 2001, 414, 466-70

[18] Finley D., Glickman M., Rubin D., Groll M., Schmidt M., Kohler A., Huber R., and Braun B.
The proteasome regulatory particle
YEAST, 2001, 18, S27

[17] Groll M., Koguchi Y., Huber R. and Kohno J.
Crystal structure of the 20S proteasome:TMC-95A complex: A non-covalent proteasome inhibitor
J. Mol. Biol., 2001, 311, 543-8

[16] Kohler A., Bajorek M., Groll M., Moroder L., Rubin DM., Huber R., Glickman M. and Finley D.
The substrate translocation channel of the proteasome
Biochimie., 2001, 83, 325-32

2000

[15] Groll M., Bajorek M., Kohler A., Moroder L., Rubin DM., Huber R., Glickman M. and Finley D.
A gated channel into the proteasome core particle
Nature Struct. Biol., 2000, 7, 1062-7

[14] Loidl G., Musiol HJ., Groll M., Huber R. and Moroder L.
Synthesis of bivalent inhibitors of eucaryotic proteasomes
Journal of Peptide Science., 2000, 6, 36-46

[13] Groll M., Kim KB., Kairies N., Huber R. and Crews CM.
Crystal structure of epoxomicin:20S proteasome reveals molecular basis for selectivity of α'β'-epoxyketone proteasome inhibitors
J. Am. Chem. Soc., 2000, 122, 1237-8

1999

[12] Schmidtke G., Holzhütter H., Bogyo M., Kairies N., Groll M., Emch R. and Groettrup M.
How an inhibitor of the HIV-I protease modulates proteasome activity
J. Biol. Chem., 1999, 274, 35734-40

[11] Bochtler M., Ditzel L., Groll M., Hartmann C. and Huber R.
The proteasome
Annu. Rev. Biophys.& Biomol. Struct., 1999, 28, 295-306

[10] Groll M., Heinemeyer W., Jäger S., Ullrich T, Bochtler M., Wolf Dh. and Huber R.
The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
Proc. Natl. Acad. Sci. USA, 1999, 96, 10976-83

[9] Loidl G., Groll M., Musiol HJ., Ditzel L., Huber R. and Moroder L.
Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes
Chem. & Biol., 1999, 6, 197-204

[8] Jäger S., Groll M., Huber R., Wolf DH. and Heinemeyer W.
Proteasome beta-type subunits: Unequal roles of propeptides in core particle maturation and a hierarchy of active site function
J. Mol. Biol., 1999, 29, 997-1013

[7] Loidl G., Groll M., Musiol HJ., Huber R. and Moroder L.
Bivalency as a principle for proteasome inhibition
Proc. Natl. Acad. Sci. USA, 1999, 96, 5418-22

1998

[6] Nussbaum AK., Dick TP., Keilholz W., Schirle M., Stevanovic S., Dietz K., Heinemeyer W., Groll M., Wolf DH., Huber R., Rammensee HG. and Schild H.
Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase I
Proc. Natl. Acad. Sci. USA, 1998, 95, 12504-9

[5] Dick TP., Nussbaum AK., Deeg M., Heinemeyer W., Groll M., Schirle M., Keilholz W., Stevanovic S., Wolf DH., Huber R., Rammensee HG. and Schild H.
Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants
J. Biol. Chem., 1998, 273, 25637-46

[4] Ditzel L., Huber R., Mann K., Heinemeyer W., Wolf DH. and Groll M.
Conformational constraints for protein self-cleavage in the proteasome
J. Mol. Biol., 1998, 279, 1187-91

1997

[3] Escherich A., Ditzel L., Musiol HJ., Groll M., Huber R. and Moroder L. 
Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasome from Thermoplasma acidophilum and Saccharomyces cerevisiae
Biol. Chem., 1997, 378, 893-8

[2] Bochtler M., Ditzel L., Groll M., Huber R. 
Crystal structure of heat shock locus V (HslV) from Escherichia coli
Proc. Natl. Acad. Sci. USA, 1997, 94, 6070-4

[1] Groll M., Ditzel L., Löwe J., Stock D., Bochtler M., Bartunik HD. and Huber R.
Structure of the 20S proteasome from yeast at 2.4Å resolution
Nature, 1997, 386, 463-71

 

Book chapters 

[10] Gräwert A. M. and Groll M. (2013)
Eukaryotic 20S Proteasome. In Handbook of Proteolytic Enzymes (Rawlings N. D. and Salvesen G. S., Eds), Oxford: Academic Press, 3684–91 

[9] Gräwert A. M. and Groll M. (2013)
PhTET2 Aminopeptidase. In Handbook of Proteolytic Enzymes (Rawlings N. D. and Salvesen G. S., Eds), Oxford: Academic Press, 1645–50 

[8] Huber E., Groll M., (2012)
Kristallstruktur eines molekularen Schredders.
GIT Labor-Fachzeitschrift, WILEY-VCH Verlag GmbH & Co. KGaA, GIT VERLAG, Weinheim, 363-65

[7] Groll M., Bochtler M., Brandstetter H., Clausen T., Huber R. (2005)
Molecular machines for protein degradation In: Functional Nanomaterials (Geckeler K. E. and Rosenberg E., Eds.) American Scientific Publishers, Stevenson Ranch, California, 1-34

[6] Huber R., Bochtler M., Groll M., Brandstetter H. and Clausen T. (2005)
Molecular machines for protein degradation In: Protein Degradation: Ubiquitin and the Chemistry of Life (Mayer J., Ciechanover A. and Rechsteiner M., Eds.) Wiley-VCH, Weinheim, 248-287

[5] Groll M. (2004)
Structural and functional similarities and differences of archaebacterial and eukaryotic 20S proteasomes Habilitationsschrift for receiving the qualification of teaching at the Charité Medical School of the Humboldt-University of Berlin

[4] Groll M. and Huber R. (2004)
Structures of the yeast proteasome core particle in complex with inhibitors In: Proteasome Inhibitors in Cancer Therapy (Adams J., Ed) Humana Press Inc., Totowa, New York, 39-47

[3] Groll M. and Coux O. (2002)
Proteasomes In: Proteinase and Peptidase Inhibition: Recent potential targets for drug development (Smith, H. J. and Simons, C., Eds.) Taylor & Francis, London, New York, 62-83

[2] Bochtler M., Ditzel L., Stock D., Löwe J., Hartmann C., Dorowski A., Huber R. and Groll M. (2001)
Proteasome crystal structures In: Proteasomes: The world of regulatory proteolysis (Hilt W. and Wolf D. H., Eds.) RG Landes Bioscience, Georgetown, Texas, Chapter 3

[1] Groll M. (1998)
Crystallographic and Biochemical Characterisation of the 20S Proteasome from S. cerevisiae Ph.D. thesis, Faculty of Chemistry, Biology and Earth Science of the Technical University of Munich Prof. Dr. M. Groll