Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.

Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D

Nucleic acids research, 2024

doi:10.1093/nar/gkae1107.

The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation.

Lomoschitz A, Meyer J, Guitart T, Krepl M, Lapouge K, Hayn C, Schweimer K, Simon B, Šponer J, Gebauer F, Hennig J

Biophysical chemistry, 2024

doi:10.1016/j.bpc.2024.107346.

The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity.

Álvarez L, Haubrich K, Iselin L, Gillioz L, Ruscica V, Lapouge K, Augsten S, Huppertz I, Choudhury NR, Simon B, Masiewicz P, Lethier M, Cusack S, Rittinger K, Gabel F, Leitner A, Michlewski G, Hentze MW, Allain FHT, Castello A, Hennig J

Nature communications, 2024

doi:10.1038/s41467-024-52918-x.

Exploring the expanding universe of host-virus interactions mediated by viral RNA.

Castello A, Álvarez L, Kamel W, Iselin L, Hennig J

Molecular cell, 2024

doi:10.1016/j.molcel.2024.08.027.

Response to Forker et al.

Griffith-Jones S, Álvarez L, Mukhopadhyay U, Gharbi S, Rettel M, Adams M, Hennig J, Bhogaraju S

The EMBO journal, 2024

doi:10.1038/s44318-024-00141-1.

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase.

Bohl V, Hollmann NM, Melzer T, Katikaridis P, Meins L, Simon B, Flemming D, Sinning I, Hennig J, Mogk A

eLife, 2024

doi:10.7554/eLife.92746.

Structural basis for RAD18 regulation by MAGEA4 and its implications for RING ubiquitin ligase binding by MAGE family proteins.

Griffith-Jones S, Álvarez L, Mukhopadhyay U, Gharbi S, Rettel M, Adams M, Hennig J, Bhogaraju S

The EMBO journal, 2024

doi:10.1038/s44318-024-00058-9.

Tropomyosin 1-I/C coordinates kinesin-1 and dynein motors during oskar mRNA transport.

Heber S, McClintock MA, Simon B, Mehtab E, Lapouge K, Hennig J, Bullock SL, Ephrussi A

Nature structural & molecular biology, 2024

doi:10.1038/s41594-024-01212-x.

Regulation and mechanisms of action of RNA helicases.

Lang N, Jagtap PKA, Hennig J

RNA biology, 2024

doi:10.1080/15476286.2024.2415801.

Structural basis of RNA-induced autoregulation of the DExH-type RNA helicase maleless.

Jagtap PKA, Müller M, Kiss AE, Thomae AW, Lapouge K, Beck M, Becker PB, Hennig J

Molecular cell, 2023

doi:10.1016/j.molcel.2023.10.026.

Structural basis of aggregate binding by the AAA+ disaggregase ClpG.

Katikaridis P, Simon B, Jenne T, Moon S, Lee C, Hennig J, Mogk A

The Journal of biological chemistry, 2023

doi:10.1016/j.jbc.2023.105336.

Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.

Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J

Nucleic acids research, 2023

doi:10.1093/nar/gkac1277.

A KLK6 activity-based probe reveals a role for KLK6 activity in pancreatic cancer cell invasion.

Zhang L, Lovell S, De Vita E, Jagtap PKA, Lucy D, Goya Grocin A, Kjær S, Borg A, Hennig J, Miller AK, Tate EW

Journal of the American Chemical Society, 2022

doi:10.1021/jacs.2c07378.

Structure and dynamics of the von Willebrand Factor C6 domain.

Chen PC, Kutzki F, Mojzisch A, Simon B, Xu ER, Aponte-Santamaría C, Horny K, Jeffries C, Schneppenheim R, Wilmanns M, Brehm MA, Gräter F, Hennig J

Journal of structural biology, 2022

doi:10.1016/j.jsb.2022.107923.

Correction: scalable synthesis and structural characterization of reversible KLK6 inhibitors.

Baumann A, Isak D, Lohbeck J, Jagtap PKA, Janosch H, Miller AK

RSC Advances, 2022

doi:10.1039/D2RA90102A.

Scalable synthesis and structural characterization of reversible KLK6 inhibitors.

Baumann A, Isak D, Lohbeck J, Jagtap PKA, Janosch H, Miller AK

RSC Advances, 2022

doi:10.1039/d2ra04670a.

Riboregulation of Enolase 1 activity controls glycolysis and embryonic stem cell differentiation.

Huppertz I, Perez-Perri JI, Mantas P, Sekaran T, Schwarzl T, Russo F, Ferring-Appel D, Koskova Z, Dimitrova-Paternoga L, Kafkia E, Hennig J, Neveu PA, Patil K, Hentze MW

Molecular cell, 2022

doi:10.1016/j.molcel.2022.05.019.

Vault RNA1-1 riboregulates the autophagic function of p62 by binding to K7/R21 that are critical for p62 oligomerisation.

Büscher M, Horos R, Huppertz I, Haubrich K, Dobrev N, Baudin F, Hennig J, Hentze MW

RNA (New York, N.Y.), 2022

doi:10.1261/rna.079129.122.

Bioaccumulation of therapeutic drugs by human gut bacteria.

Klünemann M, Andrejev S, Blasche S, Mateus A, Phapale P, Devendran S, Vappiani J, Simon B, Scott TA, Kafkia E, Konstantinidis D, Zirngibl K, Mastrorilli E, Banzhaf M, Mackmull MT, Hövelmann F, Nesme L, Brochado AR, Maier L, Bock T, Periwal V, Kumar M, Kim Y, Tramontano M, Schultz C, Beck M, Hennig J, Zimmermann M, Sévin DC, Cabreiro F, Savitski MM, Bork P, Typas A, Patil KR

Nature, 2021

doi:10.1038/s41586-021-03891-8.

Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans.

Perez-Borrajero C, Podvalnaya N, Holleis K, Lichtenberger R, Karaulanov E, Simon B, Basquin J, Hennig J, Ketting RF, Falk S

Genes & development, 2021

doi:10.1101/gad.348648.121.

Validation and classification of RNA binding proteins identified by mRNA interactome capture.

Vaishali, Dimitrova-Paternoga L, Haubrich K, Sun M, Ephrussi A, Hennig J

RNA , 2021

doi:10.1261/rna.078700.121.

Structure and dynamics of the quaternary hunchback mRNA translation repression complex.

Macošek J, Simon B, Linse JB, Jagtap PKA, Winter SL, Foot J, Lapouge K, Perez K, Rettel M, Ivanović MT, Masiewicz P, Murciano B, Savitski MM, Loedige I, Hub JS, Gabel F, Hennig J

Nucleic acids research, 2021

doi:10.1093/nar/gkab635.

Molecular basis of mRNA transport by a kinesin-1-atypical tropomyosin complex.

Dimitrova-Paternoga L, Jagtap PKA, Cyrklaff A, Vaishali, Lapouge K, Sehr P, Perez K, Heber S, Löw C, Hennig J, Ephrussi A

Genes & development, 2021

doi:10.1101/gad.348443.121.

Divergent evolution toward sex chromosome-specific gene regulation in Drosophila.

Villa R, Jagtap PKA, Thomae AW, Campos Sparr A, Forné I, Hennig J, Straub T, Becker PB

Genes & development, 2021

doi:10.1101/gad.348411.121.

Mechanism of riboregulation of p62 proteinoligomerisation by vault RNA1-1 inselective autophagy.

Büscher M, Horos R, Haubrich K, Dobrev N, Baudin F, Hennig J, Hentze MW

2021

doi:10.1101/2021.04.12.439413.

Gain-of-function variant p.Pro2555Arg of von Willebrand factor increases aggregate size through altering stem dynamics.

Huck V, Chen PC, Xu ER, Tischer A, Klemm U, Aponte-Santamaría C, Mess C, Obser T, Kutzki F, König G, Denis C, Gräter F, Wilmanns M, Auton M, Schneider SW, Schneppenheim R, Hennig J, Brehm MA

Thrombosis and haemostasis, 2020

doi:10.1055/a-1344-4405.

Author Correction: molecular dissection of amyloid disaggregation by human HSP70.

Wentink AS, Nillegoda NB, Feufel J, Ubartaitė G, Schneider CP, De Los Rios P, Hennig J, Barducci A, Bukau B

Nature, 2020

doi:10.1038/s41586-020-03090-x.

Molecular dissection of amyloid disaggregation by human HSP70.

Wentink AS, Nillegoda NB, Feufel J, Ubartaitė G, Schneider CP, De Los Rios P, Hennig J, Barducci A, Bukau B

Nature, 2020

doi:10.1038/s41586-020-2904-6.

Transcriptional regulation of the N ε -fructoselysine metabolism in Escherichia coli by global and substrate-specific cues.

von Armansperg BG, Koller F, Gericke N, Hellwig M, Jagtap PKA, Heermann R, Hennig J, Henle T, Lassak J

Molecular microbiology, 2020

doi:10.1111/mmi.14608.

Pseudo-RNA-binding domains mediate RNA structure specificity in Upstream of N-Ras.

Hollmann NM, Jagtap PKA, Masiewicz P, Guitart T, Simon B, Provaznik J, Stein F, Haberkant P, Sweetapple LJ, Villacorta L, Moojiman D, Benes V, Savitski MM, Gebauer F, Hennig J

2020

doi:10.1016/j.celrep.2020.107930.

Structure-based screening of binding affinities via small-angle X-ray scattering.

Chen PC, Masiewicz P, Perez K, Hennig J

2020

doi:10.1107/S2052252520004169.

Macrocyclic peptides uncover a novel binding mode for reversible inhibitors of LSD1.

Yang J, Talibov VO, Peintner S, Rhee C, Poongavanam V, Geitmann M, Sebastiano MR, Simon B, Hennig J, Dobritzsch D, Danielson UH, Kihlberg J

ACS omega, 2020

doi:10.1021/acsomega.9b03493.

Mechanistic insights into transcription factor cooperativity and its impact on protein-phenotype interactions.

Ibarra IL, Hollmann NM, Klaus B, Augsten S, Velten B, Hennig J, Zaugg JB

Nature communications, 2020

doi:10.1038/s41467-019-13888-7.

Integrative structural biology of protein-RNA complexes.

Dimitrova-Paternoga L, Jagtap PKA, Chen PC, Hennig J

Structure (London, England : 1993), 2019

doi:10.1016/j.str.2019.11.017.

Highlight: young research groups in Germany - continued.

Hennig J, Feige MJ

Biological chemistry, 2019

doi:10.1515/hsz-2019-0361.

Combined small-angle X-ray and neutron scattering restraints in molecular dynamics simulations.

Chen PC, Shevchuk R, Strnad FM, Lorenz C, Karge L, Gilles R, Stadler AM, Hennig J, Hub JS

Journal of chemical theory and computation, 2019

doi:10.1021/acs.jctc.9b00292.

Structural basis of an asymmetric condensin ATPase cycle.

Hassler M, Shaltiel IA, Kschonsak M, Simon B, Merkel F, Thärichen L, Bailey HJ, Macošek J, Bravo S, Metz J, Hennig J, Haering CH

Molecular cell, 2019

doi:10.1016/j.molcel.2019.03.037.

Switching the post-translational modification of translation elongation factor EF-P.

Volkwein W, Krafczyk R, Jagtap PKA, Parr M, Mankina E, Macosek J, Guo Z, Fürst M, Pfab M, Frishman D, Hennig J, Jung K, Lassak J

2019

doi:10.3389/fmicb.2019.01148.

Emerging RNA-binding roles in the TRIM family of ubiquitin ligases.

Williams FP, Haubrich K, Perez-Borrajero C, Hennig J

Biological chemistry, 2019

doi:10.1515/hsz-2019-0158.

Highlight: young research groups in Germany.

GBM Young Investigators, Hennig J, Feige MJ

Biological chemistry, 2019

doi:10.1515/hsz-2019-0246.

Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.

Pravin Kumar Ankush Jagtap, Marisa Müller, Pawel Masiewicz, Sören von Bülow, Nele Merret Hollmann, Po-Chia Chen, Bernd Simon, Andreas W Thomae, Peter B Becker, Janosch Hennig

2019

doi:10.1093/nar/gkz125.

Structure and dynamics of the platelet integrin-binding C4 domain of von Willebrand factor.

Xu ER, von Bülow S, Chen PC, Lenting PJ, Kolšek K, Aponte-Santamaría C, Simon B, Foot J, Obser T, Schneppenheim R, Gräter F, Denis CV, Wilmanns M, Hennig J

Blood, 2018

doi:10.1182/blood-2018-04-843615.

The role of small-angle scattering in structure-based screening applications.

Chen PC, Hennig J

Biophysical reviews, 2018

doi:10.1007/s12551-018-0464-x.

Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition.

Koliopoulos MG, Lethier M, van der Veen AG, Haubrich K, Hennig J, Kowalinski E, Stevens RV, Martin SR, Reis E Sousa C, Cusack S, Rittinger K

Nature communications, 2018

doi:10.1038/s41467-018-04214-8.

A general small-angle X-ray scattering-based screening protocol validated for protein-RNA interactions.

Chen PC, Masiewicz P, Rybin V, Svergun D, Hennig J

ACS combinatorial science, 2018

doi:10.1021/acscombsci.8b00007.

Ab Initio prediction of NMR spin relaxation parameters from molecular dynamics simulations.

Chen PC, Hologne M, Walker O, Hennig J

Journal of chemical theory and computation, 2018

doi:10.1021/acs.jctc.7b00750.

Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P.

Krafczyk R, Macošek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Röder A, Jung K, Hennig J, Lassak J

mBio, 2017

doi:10.1128/mBio.01412-17.

Segmental, domain-selective perdeuteration and small-angle neutron scattering for structural analysis of multi-domain proteins.

Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M

Angewandte Chemie (International ed. in English), 2017

doi:10.1002/anie.201702904.

Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody.

Li X, Krafczyk R, Macošek J, Li Y-L, Zou Y, Simon B, Pan X, Wu Q-Y, Yan F, Li S, Hennig J, Jung K, Lassak J, Hu H-G

Chemical science, 2016

doi:10.1039/c6sc02889f.

Improved accuracy from joint X-ray and NMR refinement of a protein-RNA complex structure.

Carlon A, Ravera E, Hennig J, Parigi G, Sattler M, Luchinat C

Journal of the American Chemical Society, 2016

doi:10.1021/jacs.5b11598.

Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.

Horn A, Hennig J, Ahmed YL, Stier G, Wild K, Sattler M, Sinning I

Nature communications, 2015

doi:10.1038/ncomms9875.

The crystal structure of the NHL domain in complex with RNA reveals the molecular basis of Drosophila brain-tumor-mediated gene regulation.

Loedige I, Jakob L, Treiber T, Ray D, Stotz M, Treiber N, Hennig J, Cook KB, Morris Q, Hughes TR, Engelmann JC, Krahn MP, Meister G

Cell reports, 2015

doi:10.1016/j.celrep.2015.09.068.

Efficient segmental isotope labeling of multi-domain proteins using Sortase A.

Freiburger L, Sonntag M, Hennig J, Li J, Zou P, Sattler M

Journal of biomolecular NMR, 2015

doi:10.1007/s10858-015-9981-0.

Deciphering the protein-RNA recognition code: Combining large-scale quantitative methods with structural biology.

Hennig J, Sattler M

BioEssays : news and reviews in molecular, cellular and developmental biology, 2015

doi:10.1002/bies.201500033.

Structural analysis of protein-RNA complexes in solution using NMR paramagnetic relaxation enhancements.

Hennig J, Warner LR, Simon B, Geerlof A, Mackereth CD, Sattler M

Methods in enzymology, 2015

doi:10.1016/bs.mie.2015.02.006.

The EBNA-2 N-terminal transactivation domain folds into a dimeric structure required for target gene activation.

Friberg A, Thumann S, Hennig J, Zou P, Nössner E, Ling PD, Sattler M, Kempkes B

PLoS pathogens, 2015

doi:10.1371/journal.ppat.1004910.

Local destabilization of the metal-binding region in human copper-zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS.

Hennig J, Andrésen C, Museth AK, Lundström P, Tibell LA, Jonsson BH

Biochemistry, 2015

doi:10.1021/bi500606j.

Structural basis for the assembly of the Sxl-Unr translation regulatory complex.

Hennig J, Militti C, Popowicz GM, Wang I, Sonntag M, Geerlof A, Gabel F, Gebauer F, Sattler M

Nature, 2014

doi:10.1038/nature13693.

The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.

Feige MJ, Gräwert MA, Marcinowski M, Hennig J, Behnke J, Ausländer D, Herold EM, Peschek J, Castro CD, Flajnik M, Hendershot LM, Sattler M, Groll M, Buchner J

Proceedings of the National Academy of Sciences of the United States of America, 2014

doi:10.1073/pnas.1321502111.

The dynamic duo: combining NMR and small angle scattering in structural biology.

Hennig J, Sattler M

Protein science : a publication of the Protein Society, 2014

doi:10.1002/pro.2467.

Breaking the protein-RNA recognition code.

Hennig J, Gebauer F, Sattler M

Cell cycle (Georgetown, Tex.), 2014

doi:10.4161/15384101.2014.986625.

Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1.

Wang I, Hennig J, Jagtap PK, Sonntag M, Valcárcel J, Sattler M

Nucleic acids research, 2014

doi:10.1093/nar/gku193.

The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation.

Loedige I, Stotz M, Qamar S, Kramer K, Hennig J, Schubert T, Löffler P, Längst G, Merkl R, Urlaub H, Meister G

Genes & development, 2014

doi:10.1101/gad.236513.113.

Structural features of Argonaute-GW182 protein interactions.

Pfaff J, Hennig J, Herzog F, Aebersold R, Sattler M, Niessing D, Meister G

Proceedings of the National Academy of Sciences of the United States of America, 2013

doi:10.1073/pnas.1308510110.

Protein conformational exchange measured by 1H R1ρ relaxation dispersion of methyl groups.

Weininger U, Blissing AT, Hennig J, Ahlner A, Liu Z, Vogel HJ, Akke M, Lundström P

Journal of biomolecular NMR, 2013

doi:10.1007/s10858-013-9764-4.

Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex.

Hennig J, Wang I, Sonntag M, Gabel F, Sattler M

Journal of biomolecular NMR, 2013

doi:10.1007/s10858-013-9719-9.

Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: a biophysical characterization of TPMT*2 and TPMT*5.

Wennerstrand P, Dametto P, Hennig J, Klingstedt T, Skoglund K, Appell ML, Mårtensson LG

Biochemistry, 2012

doi:10.1021/bi300377d.

MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry.

Hennig J, de Vries SJ, Hennig KD, Randles L, Walters KJ, Sunnerhagen M, Bonvin AM

BMC structural biology, 2012

doi:10.1186/1472-6807-12-29.

Anti-Ro52 autoantibodies from patients with Sjogren's syndrome inhibit the Ro52 E3 ligase activity by blocking the E3/E2 interface.

Espinosa A, Hennig J, Ambrosi A, Anandapadmanaban M, Abelius MS, Sheng Y, Nyberg F, Arrowsmith CH, Sunnerhagen M, Wahren-Herlenius M

The Journal of biological chemistry, 2011

doi:10.1074/jbc.m111.241786.

MTMDAT: Automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins.

Hennig J, Hennig KD, Sunnerhagen M

Bioinformatics (Oxford, England), 2008

doi:10.1093/bioinformatics/btn116.

The fellowship of the RING: the RING-B-box linker region interacts with the RING in TRIM21/Ro52, contains a native autoantigenic epitope in Sjogren syndrome, and is an integral and conserved region in TRIM proteins.

Hennig J, Bresell A, Sandberg M, Hennig KD, Wahren-Herlenius M, Persson B, Sunnerhagen M

Journal of molecular biology, 2008

doi:10.1016/j.jmb.2008.01.005.

Structural, functional and immunologic characterization of folded subdomains in the Ro52 protein targeted in Sjogren's syndrome.

Ottosson L, Hennig J, Espinosa A, Brauner S, Wahren-Herlenius M, Sunnerhagen M

Molecular immunology, 2006

doi:10.1016/j.molimm.2005.04.013.

Structural organization and Zn2+-dependent subdomain interactions involving autoantigenic epitopes in the Ring-B-box-coiled-coil (RBCC) region of Ro52.

Hennig J, Ottosson L, Andrésen C, Horvath L, Kuchroo VK, Broo K, Wahren-Herlenius M, Sunnerhagen M

The Journal of biological chemistry, 2005

doi:10.1074/jbc.m503066200.

Structurally derived mutations define congenital heart block-related epitopes within the 200-239 amino acid stretch of the Ro52 protein.

Ottosson L, Salomonsson S, Hennig J, Sonesson SE, Dörner T, Raats J, Kuchroo VK, Sunnerhagen M, Wahren-Herlenius M

Scandinavian journal of immunology, 2005

doi:10.1111/j.0300-9475.2005.01542.x.