Structural and kinetic insights into tRNA promoter engagement by yeast general transcription factor TFIIIC.

Seifert-Dávila W, Chaban A, Baudin F, Girbig M, Hauptmann L, Hoffmann T, Duss O, Eustermann S, Müller CW

Nucleic acids research, 2025

doi:10.1093/nar/gkae1174.

Structural insights into distinct mechanisms of RNA polymerase II and III recruitment to snRNA promoters.

Shah SZ, Perry TN, Graziadei A, Cecatiello V, Kaliyappan T, Misiaszek AD, Müller CW, Ramsay EP, Vannini A

Nature communications, 2025

doi:10.1038/s41467-024-55553-8.

Structural insight into the DNMT1 reaction cycle by cryo-electron microscopy.

De I, Weidenhausen J, Concha N, Müller CW

PloS one, 2024

doi:10.1371/journal.pone.0307850.

Novel pathogenic variants in POLR3K cause POLR3‐related leukodystrophy.

Perrier S, Macintosh J, Misiaszek AD, Lambert G, Guerrero K, Tran LT, Müller CW, Pastinen T, Maegawa GHB, Thiffault I, Bernard G, Oetting W

Human mutation, 2024

doi:10.1155/2024/8807171.

EasyGrid: a versatile platform for automated cryo-EM sample preparation and quality control.

Gemin O, Armijo V, Hons M, Bissardon C, Linares R, Bowler MW, Wolff G, Kovalev K, Babenko A, Salo VT, Schneider S, Rossi C, Lecomte L, Deckers T, Lauzier K, Janocha R, Felisaz F, Sinoir J, Galej W, Mahamid J, Müller CW, Eustermann S, Mattei S, Cipriani F, Papp G

bioRxiv, 2024

doi:10.1101/2024.01.18.576170.

Genetically encoded multimeric tags for subcellular protein localization in cryo-EM.

Fung HKH, Hayashi Y, Salo VT, Babenko A, Zagoriy I, Brunner A, Ellenberg J, Müller CW, Cuylen-Haering S, Mahamid J

Nature methods, 2023

doi:10.1038/s41592-023-02053-0.

Hypomyelination, hypodontia and craniofacial abnormalities in a Polr3b mouse model of leukodystrophy.

Michell-Robinson MA, Watt KEN, Grouza V, Macintosh J, Pinard M, Tuznik M, Chen X, Darbelli L, Wu CL, Perrier S, Chitsaz D, Uccelli NA, Liu H, Cox TC, Müller CW, Kennedy TE, Coulombe B, Rudko DA, Trainor PA, Bernard G

Brain : a journal of neurology, 2023

doi:10.1093/brain/awad249.

Structural insights into human TFIIIC promoter recognition.

Seifert-Davila W, Girbig M, Hauptmann L, Hoffmann T, Eustermann S, Müller CW

Science advances, 2023

doi:10.1126/sciadv.adh2019.

The mission to ensure continued funding for excellent basic research.

Lamond AI, Dikic I, Nussenzweig A, Müller CW, Thornton JM, Yaffe MB

EMBO reports, 2023

doi:10.15252/embr.202357498.

Molecular mechanisms of stress-induced reactivation in mumps virus condensates.

Zhang X, Sridharan S, Zagoriy I, Eugster Oegema C, Ching C, Pflaesterer T, Fung HKH, Becher I, Poser I, Müller CW, Hyman AA, Savitski MM, Mahamid J

Cell, 2023

doi:10.1016/j.cell.2023.03.015.

Genetically encoded multimeric tags for intracellular protein localisation in cryo-EM.

Fung KHH, Hayashi Y, Salo TV, Babenko A, Zagoriy I, Brunner A, Ellenberg J, Müller CW, Cuylen-Haering S, Mahamid J

bioRxiv, 2022

doi:10.1101/2022.12.10.519870.

Architecture of the yeast Pol III pre-termination complex and pausing mechanism on poly(dT) termination signals.

Girbig M, Xie J, Grötsch H, Libri D, Porrua O, Müller CW

Cell reports, 2022

doi:10.1016/j.celrep.2022.111316.

An integrated model for termination of RNA polymerase III transcription.

Xie J, Aiello U, Clement Y, Haidara N, Girbig M, Schmitzova J, Pena V, Müller CW, Libri D, Porrua O

Science advances, 2022

doi:10.1126/sciadv.abm9875.

Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.

Girbig M, Misiaszek AD, Müller CW

Nature reviews. Molecular cell biology, 2022

doi:10.1038/s41580-022-00476-9.

Mechanism of RNA polymerase I selection by transcription factor UAF.

Baudin F, Murciano B, Fung HKH, Fromm SA, Mattei S, Mahamid J, Müller CW

Science advances, 2022

doi:10.1126/sciadv.abn5725.

Cryo-EM structures of human RNA polymerase I.

Misiaszek AD, Girbig M, Grötsch H, Baudin F, Murciano B, Lafita A, Müller CW

Nature structural & molecular biology, 2022

doi:10.1038/s41594-021-00693-4.

A modular platform for automated cryo-FIB workflows.

Klumpe S, Fung HKH, Goetz SK, Zagoriy I, Hampoelz B, Zhang X, Erdmann PS, Baumbach J, Müller CW, Beck M, Plitzko JM, Mahamid J

eLife, 2021

doi:10.7554/eLife.70506.

Structural basis of DNA methylation-dependent site selectivity of the Epstein-Barr virus lytic switch protein ZEBRA/Zta/BZLF1.

Bernaudat F, Gustems M, Günther J, Oliva MF, Buschle A, Göbel C, Pagniez P, Lupo J, Signor L, Müller CW, Morand P, Sattler M, Hammerschmidt W, Petosa C

Nucleic acids research, 2021

doi:10.1093/nar/gkab1183.

Cryo-EM structures of human RNA polymerase III in its unbound and transcribing states.

Girbig M, Misiaszek AD, Vorländer MK, Lafita A, Grötsch H, Baudin F, Bateman A, Müller CW

Nature structural & molecular biology, 2021

doi:10.1038/s41594-020-00555-5.

Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.

Vorländer MK, Jungblut A, Karius K, Baudin F, Grötsch H, Kosinski J, Müller CW

Nature communications, 2020

doi:10.1038/s41467-020-18707-y.

In-cell architecture of the nuclear pore and snapshots of its turnover.

Allegretti M, Zimmerli CE, Rantos V, Wilfling F, Ronchi P, Fung HKH, Lee CW, Hagen W, Turoňová B, Karius K, Börmel M, Zhang X, Müller CW, Schwab Y, Mahamid J, Pfander B, Kosinski J, Beck M

Nature, 2020

doi:10.1038/s41586-020-2670-5.

Structural basis for RNA polymerase III transcription repression by Maf1.

Vorländer MK, Baudin F, Moir RD, Wetzel R, Hagen WJH, Willis IM, Müller CW

Nature structural & molecular biology, 2020

doi:10.1038/s41594-020-0383-y.

Molecular insight into RNA polymerase I promoter recognition and promoter melting.

Sadian Y, Baudin F, Tafur L, Murciano B, Wetzel R, Weis F, Müller CW

Nature communications, 2019

doi:10.1038/s41467-019-13510-w.

Molecular basis of tRNA recognition by the Elongator complex.

Dauden MI, Jaciuk M, Weis F, Lin TY, Kleindienst C, Abbassi NEH, Khatter H, Krutyhołowa R, Breunig KD, Kosinski J, Müller CW, Glatt S

Science advances, 2019

doi:10.1126/sciadv.aaw2326.

Unleashing the power of ASH1L methyltransferase.

De I, Müller CW

Structure (London, England : 1993), 2019

doi:10.1016/j.str.2019.04.012.

The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2.

Tafur L, Sadian Y, Hanske J, Wetzel R, Weis F, Müller CW

eLife, 2019

doi:10.7554/eLife.43204.

Structural basis for the activation of the deubiquitinase Calypso by the Polycomb protein ASX.

De I, Chittock EC, Grötsch H, Miller TCR, McCarthy AA, Müller CW

Structure (London, England : 1993), 2018

doi:10.1016/j.str.2018.11.013.

The signalling conformation of the insulin receptor ectodomain.

Weis F, Menting JG, Margetts MB, Chan SJ, Xu Y, Tennagels N, Wohlfart P, Langer T, Müller CW, Dreyer MK, Lawrence MC

Nature communications, 2018

doi:10.1038/s41467-018-06826-6.

The cryo-EM resolution revolution and transcription complexes.

Hanske J, Sadian Y, Müller CW

Current opinion in structural biology, 2018

doi:10.1016/j.sbi.2018.07.002.

Pervasive protein thermal stability variation during the cell cycle.

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

Cell, 2018

doi:10.1016/j.cell.2018.03.053.

Structural asymmetry in the eukaryotic Elongator complex.

Dauden MI, Jaciuk M, Müller CW, Glatt S

FEBS letters, 2018

doi:10.1002/1873-3468.12865.

Molecular mechanism of promoter opening by RNA polymerase III.

Vorländer MK, Khatter H, Wetzel R, Hagen WJH, Müller CW

Nature, 2018

doi:10.1038/nature25440.

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

Cusack S, Müller CW

Current opinion in structural biology, 2017

doi:10.1016/j.sbi.2017.11.004.

RNA polymerase I and III: similar yet unique.

Khatter H, Vorländer MK, Müller CW

Current opinion in structural biology, 2017

doi:10.1016/j.sbi.2017.05.008.

Structural insights into transcription initiation by yeast RNA polymerase I.

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

The EMBO journal, 2017

doi:10.15252/embj.201796958.

A synthetic biology approach to probing nucleosome symmetry.

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

eLife, 2017

doi:10.7554/eLife.28836.

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

Patel J, Lama L, Hoffmann NA, Cobo J, Müller CW, Ryan K

Gene, 2017

doi:10.1016/j.gene.2016.09.001.

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

Jeske M, Müller CW, Ephrussi A

Genes & development, 2017

doi:10.1101/gad.297051.117.

Molecular architecture of polycomb repressive complexes.

Chittock EC, Latwiel S, Miller TC, Müller CW

Biochemical Society transactions, 2017

doi:10.1042/bst20160173.

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

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

NATURE COMMUNICATIONS, 2016

doi:10.1038/ncomms13855.

Molecular Structures of Transcribing RNA Polymerase I

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

2016

doi:10.1016/j.molcel.2016.11.013.

Architecture of the yeast Elongator complex

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

doi:10.15252/embr.201643353.

Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.

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

Nature structural & molecular biology, 2016

doi:10.1038/nsmb.3265.

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

Hoffmann NA, Sadian Y, Tafur L, Kosinski J, Müller CW

Transcription, 2016

doi:10.1080/21541264.2016.1203628.

Transcribing RNA polymerase III observed by electron cryo-microscopy.

Hoffmann NA, Jakobi AJ, Vorländer MK, Sachse C, Müller CW

The FEBS journal, 2016

doi:10.1111/febs.13732.

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

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

Nature methods, 2016

doi:10.1038/nmeth.3838.

Complex Interdependence Regulates Heterotypic Transcription Factor Distribution and Coordinates Cardiogenesis.

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

Cell, 2016

doi:10.1016/j.cell.2016.01.004.

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

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

PloS one, 2016

doi:10.1371/journal.pone.0146457.

Molecular structures of unbound and transcribing RNA polymerase III.

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

Nature, 2015

doi:10.1038/nature16143.

The crystal structure of the Drosophila germline inducer oskar identifies two domains with distinct Vasa helicase- and RNA-binding activities.

Jeske M, Bordi M, Glatt S, Müller S, Rybin V, Müller CW, Ephrussi A

Cell Reports, 2015

doi:10.1016/j.celrep.2015.06.055.

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

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

Nature communications, 2015

doi:10.1038/ncomms8387.

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

Kosinski J, von Appen A, Ori A, Karius K, Müller CW, Beck M

Journal of structural biology, 2015

doi:10.1016/j.jsb.2015.01.014.

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

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

Structure (London, England : 1993), 2015

doi:10.1016/j.str.2014.11.008.

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

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

Nucleic acids research, 2014

doi:10.1093/nar/gku1147.

Structural biology: Enzyme-chromatin complex visualized.

Müller J, Müller CW

Nature, 2014

doi:10.1038/514572a.

Solving the RNA polymerase I structural puzzle.

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

Acta crystallographica. Section D, Biological crystallography, 2014

doi:10.1107/s1399004714015788.

Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Kalb R, Latwiel S, Baymaz HI, Jansen PW, Müller CW, Vermeulen M, Müller J

Nature structural & molecular biology, 2014

doi:10.1038/nsmb.2833.

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

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

Genes & development, 2013

doi:10.1101/gad.226621.113.

Crystal structure of the 14-subunit RNA polymerase I

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

Nature, 2013

doi:10.1038/nature12636.

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

Taylor NM, Baudin F, von Scheven G, Müller CW

Nucleic acids research, 2013

doi:10.1093/nar/gkt664.

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

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

Structure (London, England : 1993), 2013

doi:10.1016/j.str.2013.06.003.

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

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

The Journal of biological chemistry, 2013

doi:10.1074/jbc.m112.427856.

Structural insights into Elongator function

Glatt S, Müller CW

Current opinion in structural biology, 2013

doi:10.1016/j.sbi.2013.02.009.

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

Baudin F, Müller CW

Methods in molecular biology (Clifton, N.J.), 2013

doi:10.1007/978-1-62703-242-1_21.

The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase

Glatt S, Létoquart J, Faux C, Taylor NM, Séraphin B, Müller CW

Nature structural & molecular biology, 2012

doi:10.1038/nsmb.2234.

Elongator: transcriptional or translational regulator?

Glatt S, Séraphin B, Müller CW

Transcription, 2012

doi:10.4161/trns.21525.

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

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

The Journal of biological chemistry, 2011

doi:10.1074/jbc.m110.207407.

Recognizing and remodeling the nucleosome

Glatt S, Alfieri C, Müller CW

Current opinion in structural biology, 2011

doi:10.1016/j.sbi.2011.02.003.

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

Boulo S, Akarsu H, Lotteau V, Müller CW, Ruigrok RW, Baudin F

Virology, 2011

doi:10.1016/j.virol.2010.10.001.

Analyzing RNA polymerase III by electron cryomicroscopy

Fernández-Tornero C, Böttcher B, Rashid UJ, Müller CW

RNA biology, 2011

doi:10.4161/rna.8.5.16021.

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

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

Structure (London, England : 1993), 2011

doi:10.1016/j.str.2010.11.009.

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

Langer K, Dian C, Rybin V, Müller CW, Petosa C

PloS one, 2011

doi:10.1371/journal.pone.0017011.

Conformational flexibility of RNA polymerase III during transcriptional elongation

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

The EMBO journal, 2010

doi:10.1038/emboj.2010.266.

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

Gajda A, Towpik J, Steuerwald U, Müller CW, Lefebvre O, Boguta M

The Journal of biological chemistry, 2010

doi:10.1074/jbc.m110.125286.

A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae.

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

Molecular systems biology, 2010

doi:10.1038/msb.2010.87.

Solving the NES problem

Mattaj IW, Müller CW

Nature structural & molecular biology, 2010

doi:10.1038/nsmb1110-1288.

WD40 proteins propel cellular networks

Stirnimann CU, Petsalaki E, Russell RB, Müller CW

Trends in biochemical sciences, 2010

doi:10.1016/j.tibs.2010.04.003.

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

Stirnimann CU, Ptchelkine D, Grimm C, Müller CW

Journal of molecular biology, 2010

doi:10.1016/j.jmb.2010.04.052.

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

Rousseaux S, Petosa C, Müller CW, Khochbin S

Medecine sciences : M/S, 2010

doi:10.1051/medsci/2010262130.

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

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

Nature, 2009

doi:10.1038/nature08397.

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

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

The EMBO journal, 2009

doi:10.1038/emboj.2009.147.

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

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

The EMBO journal, 2008

doi:10.1038/emboj.2008.184.

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

Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW

Proteins, 2008

doi:10.1002/prot.21720.

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

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

EMBO reports, 2007

doi:10.1038/sj.embor.7401085.

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

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

Molecular cell, 2007

doi:10.1016/j.molcel.2007.02.016.

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

Berger JM, Muller CW

CURRENT OPINION IN STRUCTURAL BIOLOGY, 2007

doi:10.1016/j.sbi.2007.01.010.

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

Mylona A, Fernández-Tornero C, Legrand P, Haupt M, Sentenac A, Acker J, Müller CW

Molecular cell, 2006

doi:10.1016/j.molcel.2006.08.013.

HDAC6-p97/VCP controlled polyubiquitin chain turnover

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

The EMBO journal, 2006

doi:10.1038/sj.emboj.7601210.

Karyopherin flexibility in nucleocytoplasmic transport

Conti E, Müller CW, Stewart M

Current opinion in structural biology, 2006

doi:10.1016/j.sbi.2006.03.010.

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

Morand P, Budayova-Spano M, Perrissin M, Müller CW, Petosa C

Acta crystallographica. Section F, Structural biology and crystallization communications, 2006

doi:10.1107/s1744309106002971.

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

Mylona A, Acker J, Fernández-Tornero C, Sentenac A, Müller CW

Protein expression and purification, 2006

doi:10.1016/j.pep.2005.06.013.

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

Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Müller CW

Molecular cell, 2006

doi:10.1016/j.molcel.2006.01.006.

Protein/DNA Interaction

Morand, P & Müller, C.W

2006

doi:.

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

Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB

Molecular and cellular biology, 2005

doi:10.1128/mcb.25.22.9886-9896.2005.

Interaction of influenza virus proteins with nucleosomes

Garcia-Robles I, Akarsu H, Müller CW, Ruigrok RW, Baudin F

Virology, 2005

doi:10.1016/j.virol.2004.09.036.

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

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

Molecular cell, 2004

doi:10.1016/j.molcel.2004.11.018.

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

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

The Journal of biological chemistry, 2004

doi:10.1074/jbc.m407235200.

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

Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Müller CW

Molecular cell, 2004

doi:10.1016/s1097-2765(04)00130-3.

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

Akarsu H, Burmeister WP, Petosa C, Petit I, Müller CW, Ruigrok RW, Baudin F

The EMBO journal, 2003

doi:10.1093/emboj/cdg449.

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

Grüne T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Müller CW

Molecular cell, 2003

doi:10.1016/s1097-2765(03)00273-9.

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

Angelov D, Charra M, Müller CW, Cadet J, Dimitrov S

Photochemistry and photobiology, 2003

doi:10.1562/0031-8655(2003)077<0592:ssotnp>2.0.co;2.

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

Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Müller CW

The EMBO journal, 2003

doi:10.1093/emboj/cdg182.

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

Müller CW, Soler-Lopez M, Gewinner C, Groner B

2003

doi:10.1007/978-94-017-3000-6_21.

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

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

FEBS letters, 2002

doi:10.1016/s0014-5793(02)03257-x.

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

Coll M, Seidman JG, Müller CW

Structure (London, England : 1993), 2002

doi:10.1016/s0969-2126(02)00722-0.

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

Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Müller CW

The EMBO journal, 2001

doi:10.1093/emboj/20.22.6180.

Comparison of ARM and HEAT protein repeats

Andrade MA, Petosa C, O'Donoghue SI, Müller CW, Bork P

Journal of molecular biology, 2001

doi:10.1006/jmbi.2001.4624.

Transcription factors: global and detailed views

Müller CW

Current opinion in structural biology, 2001

doi:10.1016/s0959-440x(00)00163-9.

DNA recognition by NF kappa B and STAT transcription factors

Müller CW

Ernst Schering Research Foundation workshop, 2001

doi:.

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

Cingolani G, Lashuel HA, Gerace L, Müller CW

FEBS letters, 2000

doi:10.1016/s0014-5793(00)02154-2.

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

Cramer P, Varrot A, Barillas-Mury C, Kafatos FC, Müller CW

Structure (London, England : 1993), 1999

doi:10.1016/s0969-2126(99)80107-5.

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

Cingolani G, Petosa C, Weis K, Müller CW

Nature, 1999

doi:10.1038/20367.

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

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

Proceedings of the National Academy of Sciences of the United States of America, 1999

doi:10.1073/pnas.96.6.2919.

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

Cramer P, Müller CW

Structure (London, England : 1993), 1999

doi:10.1016/s0969-2126(99)80002-1.

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

Becker S, Corthals GL, Aebersold R, Groner B, Müller CW

FEBS letters, 1998

doi:10.1016/s0014-5793(98)01543-9.

Three-dimensional structure of the Stat3beta homodimer bound to DNA

Becker S, Groner B, Müller CW

Nature, 1998

doi:10.1038/28101.

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

Cramer P, Larson CJ, Verdine GL, Müller CW

The EMBO journal, 1997

doi:10.1093/emboj/16.23.7078.

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

Müller CW, Herrmann BG

Nature, 1997

doi:10.1038/39929.

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

Cramer P, Müller CW

FEBS letters, 1997

doi:10.1016/s0014-5793(97)00217-2.

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

Ferrer E, Wiersma M, Kazimierczak B, Müller CW, Eritja R

Bioconjugate chemistry, 1997

doi:10.1021/bc970042l.

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

Müller CW, Rey FA, Harrison SC

Nature structural biology, 1996

doi:10.1038/nsb0396-224.

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

Müller CW, Schlauderer GJ, Reinstein J, Schulz GE

Structure (London, England : 1993), 1996

doi:10.1016/s0969-2126(96)00018-4.

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

Müller CW, Harrison SC

FEBS letters, 1995

doi:10.1016/0014-5793(95)00541-g.

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

Müller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC

Nature, 1995

doi:10.1038/373311a0.

Delineation of two functional regions of transcription factor TFIIB.

Barberis A, Müller CW, Harrison SC, Ptashne M

Proceedings of the National Academy of Sciences of the United States of America, 1993

doi:10.1073/pnas.90.12.5628.

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

Müller CW, Schulz GE

Proteins, 1993

doi:10.1002/prot.340150106.

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

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

JOURNAL OF CRYSTAL GROWTH, 1992

doi:10.1016/0022-0248(92)90273-L.

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.

Müller CW, Schulz GE

Journal of molecular biology, 1992

doi:10.1016/0022-2836(92)90582-5.

Induced-fit movements in adenylate kinases.

Schulz GE, Müller CW, Diederichs K

Journal of molecular biology, 1990

doi:10.1016/s0022-2836(05)80250-5.

Crystallization of proteins under microgravity

Erdmann, V.A., Lippman, C., Betzel, C., Dauter, Z., Wilson, K., Hilgenfeld, R., Hoven, J., Liesum, A., Saenger W, Müller-Fahrnow A, Hinrichs W, Duevel M,Schulz GE, Müller CW, Wittmann HG, Yonath A, Weber G, Stegen K, Plaas-Link A

FEBS LETTERS, 1989

doi:10.1016/0014-5793(89)81526-1.

Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate.

Müller CW, Schulz GE

Journal of molecular biology, 1988

doi:10.1016/0022-2836(88)90567-0.