Becher I, Andrés-Pons A, Romanov N, Stein F, Schramm M, Baudin F, Helm D, Kurzawa N, Mateus A, Mackmull MT, Typas A, Müller CW, Bork P, Beck M, Savitski MM. (2018)

Pervasive Protein Thermal Stability Variation during the Cell Cycle.

Cell doi: 10.1016/j.cell.2018.03.053
Europe PMC | doi

Dauden MI, Jaciuk M, Müller CW, Glatt S. (2018)

Structural asymmetry in the eukaryotic Elongator complex.

FEBS Lett doi: 10.1002/1873-3468.12865
Europe PMC | doi

Vorländer MK, Khatter H, Wetzel R, Hagen WJH, Müller CW. (2018)

Molecular mechanism of promoter opening by RNA polymerase III.

Nature 553(7688):295-300. doi: 10.1038/nature25440
Europe PMC | doi

Cusack S, Müller CW. (2017)

Editorial overview: Protein-nucleic acid interactions: An expanding universe.

Curr. Opin. Struct. Biol. 47 doi: 10.1016/j.sbi.2017.11.004
Europe PMC | doi

Khatter H, Vorländer MK, Müller CW. (2017)

RNA polymerase I and III: similar yet unique.

Curr Opin Struct Biol 47:88-94. doi: 10.1016/j.sbi.2017.05.008
Europe PMC | doi

Sadian Y, Tafur L, Kosinski J, Jakobi AJ, Wetzel R, Buczak K, Hagen WJ, Beck M, Sachse C, Müller CW. (2017)

Structural insights into transcription initiation by yeast RNA polymerase I.

EMBO J doi: 10.15252/embj.201796958
Europe PMC | doi

Ichikawa Y, Connelly CF, Appleboim A, Miller TC, Jacobi H, Abshiru NA, Chou HJ, Chen Y, Sharma U, Zheng Y, Thomas PM, Chen HV, Bajaj V, Müller CW, Kelleher NL, Friedman N, Bolon DN, Rando OJ, Kaufman PD. (2017)

A synthetic biology approach to probing nucleosome symmetry.

Elife 6 doi: 10.7554/eLife.28836
Europe PMC | doi

Patel J, Lama L, Hoffmann NA, Cobo J, Müller CW, Ryan K. (2017)

RNA polymerase III initiation on coligo DNA templates containing loops of variable sequence, size and nucleotide chemistry.

Gene 612:49-54. doi: 10.1016/j.gene.2016.09.001
Europe PMC | doi

Jeske M, Müller CW, Ephrussi A. (2017)

The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage.

Genes Dev doi: 10.1101/gad.297051.117
Europe PMC | doi

Chittock EC, Latwiel S, Miller TC, Müller CW. (2017)

Molecular architecture of polycomb repressive complexes.

Biochem. Soc. Trans. 45(1):193-205. doi: 10.1042/bst20160173
Europe PMC | doi

Miller TC, Simon B, Rybin V, Grötsch H, Curtet S, Khochbin S, Carlomagno T, Müller CW. (2016)

A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT

Nat Commun 7:13855. doi: 10.1038/ncomms13855
Europe PMC | doi

Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJ, Sachse C, Müller CW. (2016)

Molecular Structures of Transcribing RNA Polymerase I

Mol Cell. 64(6):1135-1143. doi: 10.1016/j.molcel.2016.11.013
Europe PMC | doi

Dauden MI, Kosinski J, Kolaj-Robin O, Desfosses A, Ori A, Faux C, Hoffmann NA, Onuma OF, Breunig KD, Beck M, Sachse C, Séraphin B, Glatt S, Müller CW. (2016)

Architecture of the yeast Elongator complex

EMBO Rep. e201643353. doi: 10.15252/embr.201643353
Europe PMC | doi

Glatt S, Zabel R, Kolaj-Robin O, Onuma OF, Baudin F, Graziadei A, Taverniti V, Lin TY, Baymann F, Séraphin B, Breunig KD, Müller CW. (2016)

Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.

Nat. Struct. Mol. Biol. 23(9):794-802. doi: 10.1038/nsmb.3265
Europe PMC | doi

Hoffmann NA, Sadian Y, Tafur L, Kosinski J, Müller CW. (2016)

Specialization versus Conservation: How Pol I and Pol III use the conserved architecture of the pre-initiation complex for specialized transcription.

Transcription 7(4):127-132. doi: 10.1080/21541264.2016.1203628
Europe PMC | doi

Hoffmann NA, Jakobi AJ, Vorländer MK, Sachse C, Müller CW. (2016)

Transcribing RNA polymerase III observed by electron cryo-microscopy.

FEBS J. 283(15):2811-2819. doi: 10.1111/febs.13732
Europe PMC | doi

Ferber M, Kosinski J, Ori A, Rashid UJ, Moreno-Morcillo M, Simon B, Bouvier G, Batista PR, Müller CW, Beck M, Nilges M. (2016)

Automated structure modeling of large protein assemblies using crosslinks as distance restraints.

Nat. Methods doi: 10.1038/nmeth.3838
Europe PMC | doi

Luna-Zurita L, Stirnimann CU, Glatt S, Kaynak BL, Thomas S, Baudin F, Samee MA, He D, Small EM, Mileikovsky M, Nagy A, Holloway AK, Pollard KS, Müller CW, Bruneau BG. (2016)

Complex Interdependence Regulates Heterotypic Transcription Factor Distribution and Coordinates Cardiogenesis.

Cell doi: 10.1016/j.cell.2016.01.004
Europe PMC | doi

Silva-Martin N, Daudén MI, Glatt S, Hoffmann NA, Kastritis P, Bork P, Beck M, Müller CW. (2016)

The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.

PLoS ONE 11(1) doi: 10.1371/journal.pone.0146457
Europe PMC | doi

Hoffmann NA, Jakobi AJ, Moreno-Morcillo M, Glatt S, Kosinski J, Hagen WJ, Sachse C, Müller CW. (2015)

Molecular structures of unbound and transcribing RNA polymerase III.

Nature 528(7581):231-236. doi: 10.1038/nature16143
Europe PMC | doi

Jeske M, Bordi M, Glatt S, Müller S, Rybin V, Müller CW, Ephrussi A. (2015)

The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities.

Cell Rep 12(4):1-12. doi: 10.1016/j.celrep.2015.06.055
Europe PMC | doi

Male G, von Appen A, Glatt S, Taylor NM, Cristovao M, Groetsch H, Beck M, Müller CW. (2015)

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.

Nat Commun 6 doi: 10.1038/ncomms8387
Europe PMC | doi

Kosinski J, von Appen A, Ori A, Karius K, Müller CW, Beck M. (2015)

Xlink Analyzer: Software for analysis and visualization of cross-linking data in the context of three-dimensional structures.

J. Struct. Biol. 189(3):177-183. doi: 10.1016/j.jsb.2015.01.014
Europe PMC | doi

Glatt S, Zabel R, Vonkova I, Kumar A, Netz DJ, Pierik AJ, Rybin V, Lill R, Gavin A, Balbach J, Breunig KD, Müller CW. (2015)

Structure of the Kti11/Kti13 Heterodimer and Its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2.

Structure 23(1):149-160. doi: 10.1016/j.str.2014.11.008
Europe PMC | doi

Bock T, Chen WH, Ori A, Malik N, Silva-Martin N, Huerta-Cepas J, Powell ST, Kastritis PL, Smyshlyaev G, Vonkova I, Kirkpatrick J, Doerks T, Nesme L, Baßler J, Kos M, Hurt E, Carlomagno T, Gavin AC, Barabas O, Müller CW, van Noort V, Beck M, Bork P. (2014)

An integrated approach for genome annotation of the eukaryotic thermophile Chaetomium thermophilum.

Nucleic Acids Res. 42(22):13525-13533. doi: 10.1093/nar/gku1147
Europe PMC | doi

Müller J, Müller CW. (2014)

Structural biology: Enzyme-chromatin complex visualized.

Nature 514(7524):572-573. doi: 10.1038/514572a
Europe PMC | doi

Moreno-Morcillo M, Taylor NM, Gruene T, Legrand P, Rashid UJ, Ruiz FM, Steuerwald U, Müller CW, Fernández-Tornero C. (2014)

Solving the RNA polymerase I structural puzzle.

Acta Crystallogr. D Biol. Crystallogr. 70(Pt 10):2570-2582. doi: 10.1107/s1399004714015788
Europe PMC | doi

Kalb R, Latwiel S, Baymaz HI, Jansen PW, Müller CW, Vermeulen M, Müller J. (2014)

Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Nat. Struct. Mol. Biol. 21:569-571. doi: 10.1038/nsmb.2833
Europe PMC | doi

Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Müller J, Müller CW. (2013)

Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements.

Genes Dev. 27(21):2367-2379. doi: 10.1101/gad.226621.113
Europe PMC | doi

Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW. (2013)

Crystal structure of the 14-subunit RNA polymerase I

Nature 502(7473):644-649. doi: 10.1038/nature12636
Europe PMC | doi

Taylor NM, Baudin F, von Scheven G, Müller CW. (2013)

RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74

Nucleic Acids Res. 41(19):9183-9196. doi: 10.1093/nar/gkt664
Europe PMC | doi

Dian C, Bernaudat F, Langer K, Oliva MF, Fornerod M, Schoehn G, Müller CW, Petosa C. (2013)

Structure of a truncation mutant of the nuclear export factor CRM1 provides insights into the auto-inhibitory role of its C-terminal helix

Structure 21(8):1338-1349. doi: 10.1016/j.str.2013.06.003
Europe PMC | doi

Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW. (2013)

Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC

J. Biol. Chem. 288(21):15110-15120. doi: 10.1074/jbc.m112.427856
Europe PMC | doi

Glatt S, Müller CW. (2013)

Structural insights into Elongator function

Curr. Opin. Struct. Biol. 23(2):235-242. doi: 10.1016/j.sbi.2013.02.009
Europe PMC | doi

Baudin F, Müller CW. (2013)

Bacterial expression, purification, and crystallization of tyrosine phosphorylated STAT proteins

Methods Mol. Biol. 967:301-317. doi: 10.1007/978-1-62703-242-1_21
Europe PMC | doi

Glatt S, Létoquart J, Faux C, Taylor NM, Séraphin B, Müller CW. (2012)

The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase

Nat. Struct. Mol. Biol. 19(3):314-320. doi: 10.1038/nsmb.2234
Europe PMC | doi

Glatt S, Séraphin B, Müller CW. (2012)

Elongator: transcriptional or translational regulator?

Transcription 3(6):273-276. doi: 10.4161/trns.21525
Europe PMC | doi

Nowak AJ, Alfieri C, Stirnimann CU, Rybin V, Baudin F, Ly-Hartig N, Lindner D, Müller CW. (2011)

Chromatin-modifying complex component Nurf55/p55 associates with histones H3 and H4 and polycomb repressive complex 2 subunit Su(z)12 through partially overlapping binding sites

J. Biol. Chem. 286(26):23388-23396. doi: 10.1074/jbc.m110.207407
Europe PMC | doi

Glatt S, Alfieri C, Müller CW. (2011)

Recognizing and remodeling the nucleosome

Curr. Opin. Struct. Biol. 21(3):335-341. doi: 10.1016/j.sbi.2011.02.003
Europe PMC | doi

Boulo S, Akarsu H, Lotteau V, Müller CW, Ruigrok RW, Baudin F. (2011)

Human importin alpha and RNA do not compete for binding to influenza A virus nucleoprotein

Virology 409(1):84-90. doi: 10.1016/j.virol.2010.10.001
Europe PMC | doi

Fernández-Tornero C, Böttcher B, Rashid UJ, Müller CW. (2011)

Analyzing RNA polymerase III by electron cryomicroscopy

RNA Biol 8(5):760-765. doi: 10.4161/rna.8.5.16021
Europe PMC | doi

Lane LA, Fernández-Tornero C, Zhou M, Morgner N, Ptchelkine D, Steuerwald U, Politis A, Lindner D, Gvozdenovic J, Gavin AC, Müller CW, Robinson CV. (2011)

Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III

Structure 19(1):90-100. doi: 10.1016/j.str.2010.11.009
Europe PMC | doi

Langer K, Dian C, Rybin V, Müller CW, Petosa C. (2011)

Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain

PLoS ONE 6(2):e17011. doi: 10.1371/journal.pone.0017011
Europe PMC | doi

Fernández-Tornero C, Böttcher B, Rashid UJ, Steuerwald U, Flörchinger B, Devos DP, Lindner D, Müller CW. (2010)

Conformational flexibility of RNA polymerase III during transcriptional elongation

EMBO J. 29(22):3762-3772. doi: 10.1038/emboj.2010.266
Europe PMC | doi

Gajda A, Towpik J, Steuerwald U, Müller CW, Lefebvre O, Boguta M. (2010)

Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1

J. Biol. Chem. 285(46):35719-35727. doi: 10.1074/jbc.m110.125286
Europe PMC | doi

Gallego O, Betts MJ, Gvozdenovic-Jeremic J, Maeda K, Matetzki C, Aguilar-Gurrieri C, Beltran-Alvarez P, Bonn S, Fernández-Tornero C, Jensen LJ, Kuhn M, Trott J, Rybin V, Müller CW, Bork P, Kaksonen M, Russell RB, Gavin AC. (2010)

A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Mol. Syst. Biol. 6:430. doi: 10.1038/msb.2010.87
Europe PMC | doi

Mattaj IW, Müller CW. (2010)

Solving the NES problem

Nat. Struct. Mol. Biol. 17(11):1288-1289. doi: 10.1038/nsmb1110-1288
Europe PMC | doi

Stirnimann CU, Petsalaki E, Russell RB, Müller CW. (2010)

WD40 proteins propel cellular networks

Trends Biochem. Sci. 35(10):565-574. doi: 10.1016/j.tibs.2010.04.003
Europe PMC | doi

Stirnimann CU, Ptchelkine D, Grimm C, Müller CW. (2010)

Structural basis of TBX5-DNA recognition: the T-box domain in its DNA-bound and -unbound form

J. Mol. Biol. 400(1):71-81. doi: 10.1016/j.jmb.2010.04.052
Europe PMC | doi

Rousseaux S, Petosa C, Müller CW, Khochbin S. (2010)

[A novel key element in post-meiotic male genome reprogramming]

Med Sci (Paris) 26(2):130-132. doi: 10.1051/medsci/2010262130
Europe PMC | doi

Morinière J, Rousseaux S, Steuerwald U, Soler-López M, Curtet S, Vitte AL, Govin J, Gaucher J, Sadoul K, Hart DJ, Krijgsveld J, Khochbin S, Müller CW, Petosa C. (2009)

Cooperative binding of two acetylation marks on a histone tail by a single bromodomain

Nature 461(7264):664-668. doi: 10.1038/nature08397
Europe PMC | doi

Grimm C, Matos R, Ly-Hartig N, Steuerwald U, Lindner D, Rybin V, Müller J, Müller CW. (2009)

Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt

EMBO J. 28(13):1965-1977. doi: 10.1038/emboj.2009.147
Europe PMC | doi

Hamès C, Ptchelkine D, Grimm C, Thevenon E, Moyroud E, Gérard F, Martiel JL, Benlloch R, Parcy F, Müller CW. (2008)

Structural basis for LEAFY floral switch function and similarity with helix-turn-helix proteins

EMBO J. 27(19):2628-2637. doi: 10.1038/emboj.2008.184
Europe PMC | doi

Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. (2008)

Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer

Proteins 71(1):1-7. doi: 10.1002/prot.21720
Europe PMC | doi

Grimm C, de Ayala Alonso AG, Rybin V, Steuerwald U, Ly-Hartig N, Fischle W, Müller J, Müller CW. (2007)

Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg

EMBO Rep. 8(11):1031-1037. doi: 10.1038/sj.embor.7401085
Europe PMC | doi

Fernández-Tornero C, Böttcher B, Riva M, Carles C, Steuerwald U, Ruigrok RW, Sentenac A, Müller CW, Schoehn G. (2007)

Insights into transcription initiation and termination from the electron microscopy structure of yeast RNA polymerase III

Mol. Cell 25(6):813-823. doi: 10.1016/j.molcel.2007.02.016
Europe PMC | doi

Berger JM, Muller CW. (2007)

Protein-nucleic acid interactions: some assembly required - Editorial overview

CURR OPIN STRUC BIOL 17(1):77-79. doi: 10.1016/j.sbi.2007.01.010
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Mylona A, Fernández-Tornero C, Legrand P, Haupt M, Sentenac A, Acker J, Müller CW. (2006)

Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly

Mol. Cell 24(2):221-232. doi: 10.1016/j.molcel.2006.08.013
Europe PMC | doi

Boyault C, Gilquin B, Zhang Y, Rybin V, Garman E, Meyer-Klaucke W, Matthias P, Müller CW, Khochbin S. (2006)

HDAC6-p97/VCP controlled polyubiquitin chain turnover

EMBO J. 25(14):3357-3366. doi: 10.1038/sj.emboj.7601210
Europe PMC | doi

Conti E, Müller CW, Stewart M. (2006)

Karyopherin flexibility in nucleocytoplasmic transport

Curr. Opin. Struct. Biol. 16(2):237-244. doi: 10.1016/j.sbi.2006.03.010
Europe PMC | doi

Morand P, Budayova-Spano M, Perrissin M, Müller CW, Petosa C. (2006)

Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein-Barr virus ZEBRA protein

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 3):210-214. doi: 10.1107/s1744309106002971
Europe PMC | doi

Mylona A, Acker J, Fernández-Tornero C, Sentenac A, Müller CW. (2006)

Expression, proteolytic analysis, reconstitution, and crystallization of the tau60/tau91 subcomplex of yeast TFIIIC

Protein Expr. Purif. 45(2):255-261. doi: 10.1016/j.pep.2005.06.013
Europe PMC | doi

Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Müller CW. (2006)

Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein

Mol. Cell 21(4):565-572. doi: 10.1016/j.molcel.2006.01.006
Europe PMC | doi

Morand, P & Müller, C.W. (2006)

Protein/DNA Interaction

In: Ganten, D. & Ruckpaul, K.(Eds.), Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine. Springer. pp 1538-1542.

Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. (2005)

The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions

Mol. Cell. Biol. 25(22):9886-9896. doi: 10.1128/mcb.25.22.9886-9896.2005
Europe PMC | doi

Garcia-Robles I, Akarsu H, Müller CW, Ruigrok RW, Baudin F. (2005)

Interaction of influenza virus proteins with nucleosomes

Virology 332(1):329-336. doi: 10.1016/j.virol.2004.09.036
Europe PMC | doi

Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-López M, Baudin F, Mattaj IW, Müller CW. (2004)

Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex

Mol. Cell 16(5):761-775. doi: 10.1016/j.molcel.2004.11.018
Europe PMC | doi

Angelov D, Lenouvel F, Hans F, Müller CW, Bouvet P, Bednar J, Moudrianakis EN, Cadet J, Dimitrov S. (2004)

The histone octamer is invisible when NF-kappaB binds to the nucleosome

J. Biol. Chem. 279(41):42374-42382. doi: 10.1074/jbc.m407235200
Europe PMC | doi

Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Müller CW. (2004)

Structure of an activated Dictyostelium STAT in its DNA-unbound form

Mol. Cell 13(6):791-804. doi: 10.1016/s1097-2765(04)00130-3
Europe PMC | doi

Akarsu H, Burmeister WP, Petosa C, Petit I, Müller CW, Ruigrok RW, Baudin F. (2003)

Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

EMBO J. 22(18):4646-4655. doi: 10.1093/emboj/cdg449
Europe PMC | doi

Grüne T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Müller CW. (2003)

Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI

Mol. Cell 12(2):449-460. doi: 10.1016/s1097-2765(03)00273-9
Europe PMC | doi

Angelov D, Charra M, Müller CW, Cadet J, Dimitrov S. (2003)

Solution study of the NF-kappaB p50-DNA complex by UV laser protein-DNA cross-linking

Photochem. Photobiol. 77(6):592-596. doi: 10.1562/0031-8655(2003)077<0592:ssotnp>2.0.co;2
Europe PMC | doi

Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Müller CW. (2003)

Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition

EMBO J. 22(8):1835-1845. doi: 10.1093/emboj/cdg182
Europe PMC | doi

Müller CW, Soler-Lopez M, Gewinner C, Groner B. (2003)

X-ray crystal structure of STAT proteins and structure-activity relationships

Springer Netherlands.doi: 10.1007/978-94-017-3000-6_21
Europe PMC | doi

Cohen SX, Moulin M, Schilling O, Meyer-Klaucke W, Schreiber J, Wegner M, Müller CW. (2002)

The GCM domain is a Zn-coordinating DNA-binding domain

FEBS Lett. 528(1-3):95-100. doi: 10.1016/s0014-5793(02)03257-x
Europe PMC | doi

Coll M, Seidman JG, Müller CW. (2002)

Structure of the DNA-bound T-box domain of human TBX3, a transcription factor responsible for ulnar-mammary syndrome

Structure 10(3):343-356. doi: 10.1016/s0969-2126(02)00722-0
Europe PMC | doi

Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Müller CW. (2001)

Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family

EMBO J. 20(22):6180-6190. doi: 10.1093/emboj/20.22.6180
Europe PMC | doi

Andrade MA, Petosa C, O'Donoghue SI, Müller CW, Bork P. (2001)

Comparison of ARM and HEAT protein repeats

J. Mol. Biol. 309(1):1-18. doi: 10.1006/jmbi.2001.4624
Europe PMC | doi

Müller CW. (2001)

Transcription factors: global and detailed views

Curr. Opin. Struct. Biol. 11(1):26-32. doi: 10.1016/s0959-440x(00)00163-9
Europe PMC | doi

Müller CW. (2001)

DNA recognition by NF kappa B and STAT transcription factors

Ernst Schering Res. Found. Workshop (34):143-166.
Europe PMC

Cingolani G, Lashuel HA, Gerace L, Müller CW. (2000)

Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association

FEBS Lett. 484(3):291-298. doi: 10.1016/s0014-5793(00)02154-2
Europe PMC | doi

Cramer P, Varrot A, Barillas-Mury C, Kafatos FC, Müller CW. (1999)

Structure of the specificity domain of the Dorsal homologue Gambif1 bound to DNA

Structure 7(7):841-852. doi: 10.1016/s0969-2126(99)80107-5
Europe PMC | doi

Cingolani G, Petosa C, Weis K, Müller CW. (1999)

Structure of importin-beta bound to the IBB domain of importin-alpha

Nature 399(6733):221-229. doi: 10.1038/20367
Europe PMC | doi

Basson CT, Huang T, Lin RC, Bachinsky DR, Weremowicz S, Vaglio A, Bruzzone R, Quadrelli R, Lerone M, Romeo G, Silengo M, Pereira A, Krieger J, Mesquita SF, Kamisago M, Morton CC, Pierpont ME, Müller CW, Seidman JG, Seidman CE. (1999)

Different TBX5 interactions in heart and limb defined by Holt-Oram syndrome mutations

Proc. Natl. Acad. Sci. U.S.A. 96(6):2919-2924. doi: 10.1073/pnas.96.6.2919
Europe PMC | doi

Cramer P, Müller CW. (1999)

A firm hand on NFkappaB: structures of the IkappaBalpha-NFkappaB complex

Structure 7(1):R1-6. doi: 10.1016/s0969-2126(99)80002-1
Europe PMC | doi

Becker S, Corthals GL, Aebersold R, Groner B, Müller CW. (1998)

Expression of a tyrosine phosphorylated, DNA binding Stat3beta dimer in bacteria

FEBS Lett. 441(1):141-147. doi: 10.1016/s0014-5793(98)01543-9
Europe PMC | doi

Becker S, Groner B, Müller CW. (1998)

Three-dimensional structure of the Stat3beta homodimer bound to DNA

Nature 394(6689):145-151. doi: 10.1038/28101
Europe PMC | doi

Cramer P, Larson CJ, Verdine GL, Müller CW. (1997)

Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1 A resolution

EMBO J. 16(23):7078-7090. doi: 10.1093/emboj/16.23.7078
Europe PMC | doi

Müller CW, Herrmann BG. (1997)

Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor

Nature 389(6653):884-888. doi: 10.1038/39929
Europe PMC | doi

Cramer P, Müller CW. (1997)

Engineering of diffraction-quality crystals of the NF-kappaB P52 homodimer:DNA complex.

FEBS Lett. 405(3):373-377. doi: 10.1016/s0014-5793(97)00217-2
Europe PMC | doi

Ferrer E, Wiersma M, Kazimierczak B, Müller CW, Eritja R. (1997)

Preparation and properties of oligodeoxynucleotides containing 5-iodouracil and 5-bromo- and 5-iodocytosine

Bioconjug. Chem. 8(5):757-761. doi: 10.1021/bc970042l
Europe PMC | doi

Müller CW, Rey FA, Harrison SC. (1996)

Comparison of two different DNA-binding modes of the NF-kappa B p50 homodimer.

Nat. Struct. Biol. 3(3):224-227. doi: 10.1038/nsb0396-224
Europe PMC | doi

Müller CW, Schlauderer GJ, Reinstein J, Schulz GE. (1996)

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding.

Structure 4(2):147-156. doi: 10.1016/s0969-2126(96)00018-4
Europe PMC | doi

Müller CW, Harrison SC. (1995)

The structure of the NF-kappa B p50:DNA-complex: a starting point for analyzing the Rel family.

FEBS Lett. 369(1):113-117. doi: 10.1016/0014-5793(95)00541-g
Europe PMC | doi

Müller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC. (1995)

Structure of the NF-kappa B p50 homodimer bound to DNA

Nature 373(6512):311-317. doi: 10.1038/373311a0
Europe PMC | doi

Barberis A, Müller CW, Harrison SC, Ptashne M. (1993)

Delineation of two functional regions of transcription factor TFIIB.

Proc. Natl. Acad. Sci. U.S.A. 90(12):5628-5632. doi: 10.1073/pnas.90.12.5628
Europe PMC | doi

Müller CW, Schulz GE. (1993)

Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.

Proteins 15(1):42-49. doi: 10.1002/prot.340150106
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Schulz GE, Dreyer M, Klein C, Kreusch A, Mittl P, Müller CW, Müller-Dieckmann J, Müller YA, Proba K, Schlauderer G, Spürgin P, Sthele T, Weisss MS. (1992)

Highly ordered crystals of channel-forming membrane proteins, of nucleoside-monophosphate kinases, of FAD-containing oxidoreductases and of sugar-processing enzymes and their mutants

J CRYST GROWTH 122(1-4):385-392. doi: 10.1016/0022-0248(92)90273-L
doi

Müller CW, Schulz GE. (1992)

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state.

J. Mol. Biol. 224(1):159-177. doi: 10.1016/0022-2836(92)90582-5
Europe PMC | doi

Schulz GE, Müller CW, Diederichs K. (1990)

Induced-fit movements in adenylate kinases.

J. Mol. Biol. 213(4):627-630. doi: 10.1016/s0022-2836(05)80250-5
Europe PMC | doi