{"id":28,"date":"2024-07-11T16:16:06","date_gmt":"2024-07-11T14:16:06","guid":{"rendered":"https:\/\/blogs.urz.uni-halle.de\/halomem\/?page_id=28"},"modified":"2024-07-11T16:16:07","modified_gmt":"2024-07-11T14:16:07","slug":"publications","status":"publish","type":"page","link":"https:\/\/blogs.urz.uni-halle.de\/halomem\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<figure class=\"wp-block-image size-large is-resized\"><img loading=\"lazy\" src=\"https:\/\/blogs.urz.uni-halle.de\/halomem\/files\/2024\/07\/Startbild_Kristall2-1-1024x345.jpg\" alt=\"\" class=\"wp-image-29\" width=\"512\" height=\"173\" srcset=\"https:\/\/blogs.urz.uni-halle.de\/halomem\/files\/2024\/07\/Startbild_Kristall2-1-1024x345.jpg 1024w, https:\/\/blogs.urz.uni-halle.de\/halomem\/files\/2024\/07\/Startbild_Kristall2-1-300x101.jpg 300w, https:\/\/blogs.urz.uni-halle.de\/halomem\/files\/2024\/07\/Startbild_Kristall2-1-768x259.jpg 768w, https:\/\/blogs.urz.uni-halle.de\/halomem\/files\/2024\/07\/Startbild_Kristall2-1.jpg 1434w\" sizes=\"(max-width: 512px) 100vw, 512px\" \/><\/figure>\n\n\n\n<p><strong><u>Publications 2021<\/u><\/strong><\/p>\n\n\n\n<p>*co-first author *co-corresponding author<\/p>\n\n\n\n<p>Barth M, <strong>Schmidt C<\/strong> (2021) Quantitative Cross-Linking of Proteins and Protein Complexes. Methods Mol Biol. 2228:385-400, doi: 10.1007\/978-1-0716-1024-4_26<\/p>\n\n\n\n<p>Rozanova S, Barkovits K, Nikolov M, <strong>Schmidt C<\/strong>, Urlaub H, Marcus K (2021) Quantitative Mass Spectrometry-Based Proteomics: An Overview. Methods Mol Biol. 2228:85-116, doi: 10.1007\/978-1-0716-1024-4_8<\/p>\n\n\n\n<p>Bender J, <strong>Schmidt C<\/strong> (2021) Exploring Phosphoinositide Binding Using Native Mass Spectrometry. Methods Mol Biol. 2251:157-175, doi: 10.1007\/978-1-0716-1142-5_11<\/p>\n\n\n\n<p>S\u00e4nger L, Bender J, Rostowski K, Golbik R, Lilie H, <strong>Schmidt C<\/strong>, Behrens SE, Friedrich S (2021) Alternatively spliced isoforms of AUF1 regulate a miRNA-mRNA interaction differentially through their YGG motif. RNA Biol. 18(6):843-853, doi: 10.1080\/15476286.2020.1822637<\/p>\n\n\n\n<p>Frick M, Schwieger C, <strong>Schmidt C<\/strong> (2021) Liposomes as Carriers of Membrane-Associated Proteins and Peptides for Mass Spectrometric Analysis. Angew Chem Int Ed Engl. 60(20):11523-11530, doi: 10.1002\/anie.202101242<\/p>\n\n\n\n<p>Rehkamp A, T\u00e4nzler D, T\u00fcting C, <strong>Kastritis PL<\/strong>, Iacobucci C, Ihling CH, Kipping M, Koch KW, Sinz A (2021) First 3D-Structural Data of Full-Length Guanylyl Cyclase 1 in Rod-Outer-Segment Preparations of Bovine Retina by Cross-Linking\/Mass Spectrometry. J Mol Biol. 433(10):166947, doi: 10.1016\/j.jmb.2021.166947<\/p>\n\n\n\n<p>Auerswald J, Ebenhan J, Schwieger C, Scrima A, Meister A,<strong> Bacia K<\/strong> (2021) Measuring protein insertion areas in lipid monolayers by fluorescence correlation spectroscopy. Biophys J. 120(8):1333-1342, doi: 10.1016\/j.bpj.2021.02.011<\/p>\n\n\n\n<p>Sorzano COS, Semchonok D, Lin SC, Lo YC, Vilas JL, Jim\u00e9nez-Moreno A, Gragera M, Vacca S, Maluenda D, Mart\u00ednez M, Ram\u00edrez-Aportela E, Melero R, Cuervo A, Conesa JJ, Conesa P, Losana P, Ca\u00f1o LD, de la Morena JJ, Fonseca YC, S\u00e1nchez-Garc\u00eda R, Strelak D, Fern\u00e1ndez-Gim\u00e9nez E, de Isidro F, Herreros D, <strong>Kastritis PL<\/strong>, Marabini R, Bruce BD, Carazo JM (2021) Algorithmic robustness to preferred orientations in single particle analysis by CryoEM. J Struct Biol. 213(1):107695, doi: 10.1016\/j.jsb.2020.107695<\/p>\n\n\n\n<p>Niemeyer M, Castillo EM, Ihling CH, Iacobucci C, Wilde V, Hellmuth A, Hoehenwarter W, Samodelov SL, Zurbriggen MD, <strong>Kastritis PL<\/strong>, Sinz A, Villalobos LIAC (2021) Author correction: Flexibility of intrinsically disordered degrons in AUX\/IAA proteins reinforces auxin co-receptor assemblies. Nat Commun. 12(1):1768, doi: 10.1038\/s41467-021-22151-x<\/p>\n\n\n\n<p>Hoffmann M, Drescher S, Schwieger C, <strong>Hinderberger D<\/strong> (2021) Influence of a single ether bond on assembly, orientation, and miscibility of phosphocholine lipids at the air-water interface. Phys Chem Chem Phys. 23(9):5325-5339, doi: 10.1039\/d0cp06520j<\/p>\n\n\n\n<p>Kyrilis FL, Belapure J, <strong>Kastritis PL<\/strong> (2021) Detecting Protein Communities in Native Cell Extracts by Machine Learning: A Structural Biologist\u2019s Perspective. Front Mol Biosci. 8:660542, doi: 10.3389\/fmolb.2021.660542<\/p>\n\n\n\n<p>Klein ME, Rieckmann M, Sedding D, Hause G, Meister A, M\u00e4der K, Lucas H (2021) Towards the Development of Long Circulating Phosphatidylserine (PS)- and Phosphatidylglycerol (PG)-Enriched Anti-Inflammatory Liposomes: Is PEGylation Effective? Pharmaceutics 13(2):282, doi: 10.3390\/pharmaceutics13020282<\/p>\n\n\n\n<p>Kyrilis FL, Semchonok DA, Skalidis I, T\u00fcting C, Hamdi F, O\u2019Reilly FJ, Rappsilber J, <strong>Kastritis PL<\/strong> (2021) Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts. Cell Rep. 34(6):108727, doi: 10.1016\/j.celrep.2021.108727<\/p>\n\n\n\n<p>Taudte N, Linnert M, Rahfeld JU, Piechotta A, Ramsbeck D, Buchholz M, Kolenko P, Parthier C, Houston JA, Veillard F, Eick S, Potempa J, Schilling S, Demuth HU, <strong>Stubbs MT<\/strong> (2021) Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis. J Biol Chem. 296:100263, doi: 10.1016\/j.jbc.2021.100263<\/p>\n\n\n\n<p><strong><u>Publications 2020<\/u><\/strong><\/p>\n\n\n\n<p>*co-first author *co-corresponding author<\/p>\n\n\n\n<p>Rodrigues JPGLM, Barrera-Vilarmau S, M C Teixeira J, Sorokina M, Seckel E, <strong>Kastritis PL,<\/strong> Levitt M (2020) Insights on cross-species transmission of SARS-CoV-2 from structural modeling. PLoS Comput Biol. 16(12):e1008449, doi: 10.1371\/journal.pcbi.1008449<\/p>\n\n\n\n<p>Leitner A, Bonvin AMJJ, Borchers CH, Chalkley RJ, Chamot-Rooke J, Combe CW, Cox J, Dong MQ, Fischer L, G\u00f6tze M, Gozzo FC, Heck AJR, Hoopmann MR, Huang L, Ishihama Y, Jones AR, Kalisman N, Kohlbacher O, Mechtler K, Moritz RL, Netz E, Novak P, Petrotchenko E, Sali A, Scheltema RA, <strong>Schmidt C<\/strong>, Schriemer D, Sinz A, Sobott F, Stengel F, Thalassinos K, Urlaub H, Viner R, Vizca\u00edno JA, Wilkins MR, Rappsilber J (2020) Toward Increased Reliability, Transparency, and Accessibility in Cross-linking Mass Spectrometry. Structure 28(11):1259-1268, doi: 10.1016\/j.str.2020.09.011<\/p>\n\n\n\n<p>Hoffmann M, Drescher S, Ihling C, <strong>Hinderberger D<\/strong>, Schwieger C (2020) An Azidolipid Monolayer \u2013 Transitions, Miscibility, and UV Reactivity Studied by Infrared Reflection Absorption Spectroscopy. Langmuir. 36(43):12804-12815, doi: 10.1021\/acs.langmuir.0c01726<\/p>\n\n\n\n<p>Barth M, <strong>Schmidt C<\/strong> (2020) Native mass spectrometry-A valuable tool in structural biology. J Mass Spectrom 55(10):e4578, doi: 10.1002\/jms.4578<\/p>\n\n\n\n<p>Skalidis I, T\u00fcting C, <strong>Kastritis PL <\/strong>(2020) Unstructured regions of large enzymatic complexes control the availability of metabolites with signaling functions. Cell Commun Signal 18(1):136, doi: 10.1186\/s12964-020-00631-9<\/p>\n\n\n\n<p>Zhou Y, <strong>Kastritis PL<\/strong>, Dougherty SE, Bouvette J, Hsu AL, Burbaum L, Mosalaganti S, Pfeffer S, Hagen WJH, F\u00f6rster F, Borgnia MJ, Vogel C, Beck M, Bartesaghi A, Silva GM (2020) Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress. Proc Natl Acad Sci U S A. 117(36): 22157-22166, doi:10.1073\/pnas.2005301117<\/p>\n\n\n\n<p>Tr\u00e4ger J, Widder K, Kerth A, Harauz G, <strong>Hinderberger D <\/strong>(2020) Effect of Cholesterol and Myelin Basic Protein (MBP) Content on Lipid Monolayers Mimicking the Cytoplasmic Membrane of Myelin. Cells 9(3): 529. doi:10.3390\/cells9030529<\/p>\n\n\n\n<p>Sorokina M, M C Teixeira J, Barrera-Vilarmau S, Paschke R, Papasotiriou I, Rodrigues JPGLM, <strong>Kastritis PL<\/strong> (2020) Structural models of human ACE2 variants with SARS-CoV-2 Spike protein for structure-based drug design. Sci Data. 7(1): 309, doi:10.1038\/s41597-020-00652-6<\/p>\n\n\n\n<p>Modicano P, Neumann PR, Sch\u00fcller M, Holthof J, Kyrilis FL, Hamdi F, <strong>Kastritis PL<\/strong>, M\u00e4der K, Ann Dailey L (2020) Enhanced optical imaging properties of lipid nanocapsules as vehicles for fluorescent conjugated polymers. Eur J Pharm Biopharm. 154: 297-308, doi:10.1016\/j.ejpb.2020.07.017<\/p>\n\n\n\n<p>Klein ME, Rieckmann M, Lucas H, Meister A, Loppnow H, M\u00e4der K (2020) Phosphatidylserine (PS) and phosphatidylglycerol (PG) enriched mixed micelles (MM): A new nano-drug delivery system with anti-inflammatory potential? Eur J Pharm Sci. 152: 105451, doi:10.1016\/j.ejps.2020.105451<\/p>\n\n\n\n<p>Shah SWH, Schwieger C, Kressler J, Blume A (2020) Monolayer behavior of pure F-DPPC and mixed films with DPPC studied by epifluorescence microscopy and infrared reflection absorption spectroscopy. Chem Phys Lipids. 230: 104918, doi:10.1016\/j.chemphyslip.2020.104918<\/p>\n\n\n\n<p>Auerswald A, Gruber T,<strong> Balbach J<\/strong>, Meister A (2020) Lipid-Dependent Interaction of Human N-BAR Domain Proteins with Sarcolemma Mono- and Bilayers. Langmuir 36(30):8695-8704, doi: 10.1021\/acs.langmuir.0c00649<\/p>\n\n\n\n<p>T\u00fcting C, Iacobucci C, Ihling CH, <strong>Kastritis PL<\/strong>, Sinz A (2020) Structural analysis of 70S ribosomes by cross-linking\/mass spectrometry reveals conformational plasticity. Sci Rep. 10(1):12618, doi: 10.1038\/s41598-020-69313-3<\/p>\n\n\n\n<p>Drescher S, Meister A, Hause G, Neuhaus F, Balog S, Brezesinski G, Zumbuehl A (2020) Tuning the Thickness of a Biomembrane by Stapling Diamidophospholipids with Bolalipids. Langmuir 36(29):8610-8616, doi: 10.1021\/acs.langmuir.0c01522<\/p>\n\n\n\n<p>Maru\u0161i\u010d N, Otrin L, Zhao Z, Lira RB, Kyrilis FL, Hamdi F, <strong>Kastritis PL<\/strong>, Vidakovi\u0107-Koch T, Ivanov I, Sundmacher K, Dimova R (2020) Constructing artificial respiratory chain in polymer compartments: Insights into the interplay between bo3 oxidase and the membrane. Proc Natl Acad Sci U S A. 117(26):15006-15017, doi: 10.1073\/pnas.1919306117<\/p>\n\n\n\n<p>Barth M, Bender J, Kundlacz T, <strong>Schmidt C<\/strong> (2020) Evaluation of NHS-Acetate and DEPC labelling for determination of solvent accessible amino acid residues in protein complexes. J Proteomics 222:103793, doi: 10.1016\/j.jprot.2020.103793<\/p>\n\n\n\n<p>Niemeyer M, Moreno Castillo E, Ihling CH, Iacobucci C, Wilde V, Hellmuth A, Hoehenwarter W, Samodelov SL, Zurbriggen MD, <strong>Kastritis PL<\/strong>, Sinz A, Calder\u00f3n Villalobos LIA (2020) Flexibility of intrinsically disordered degrons in AUX\/IAA proteins reinforces auxin co-receptor assemblies. Nat Commun. 11(1):2277, doi: 10.1038\/s41467-020-16147-2<\/p>\n\n\n\n<p>Hamdi F, T\u00fcting C, Semchonok DA, Visscher KM, Kyrilis FL, Meister A, Skalidis I, Schmidt L, Parthier C, <strong>Stubbs MT<\/strong>,<strong> Kastritis PL<\/strong> (2020) 2.7 \u00c5 cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope. PLoS One. 15(5):e0232540, doi: 10.1371\/journal.pone.0232540<\/p>\n\n\n\n<p>Wittig S, Songailiene I, <strong>Schmidt C<\/strong> (2020) Formation and Stoichiometry of CRISPR-Cascade Complexes with Varying Spacer Lengths Revealed by Native Mass Spectrometry. J Am Soc Mass Spectrom. 31(3):538-546, doi: 10.1021\/jasms.9b00011<\/p>\n\n\n\n<p>Langeveld SAG, Schwieger C, Beekers I, Blaffert J, van Rooij T, Blume A, Kooiman K (2020) Ligand Distribution and Lipid Phase Behavior in Phospholipid-Coated Microbubbles and Monolayers. Langmuir. 36(12):3221-3233, doi: 10.1021\/acs.langmuir.9b03912<\/p>\n\n\n\n<p>Wittig S, Ganzella M, Barth M, Kostmann S, Riedel D, P\u00e9rez-Lara \u00c1, Jahn R, <strong>Schmidt C<\/strong> (2020) Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes. Nat Commun. 12(1):858, doi: 10.1038\/s41467-021-21102-w<\/p>\n\n\n\n<p>Bender J, <strong>Schmidt C<\/strong> (2020) The CroCo cross-link converter: a user-centred tool to convert results from cross-linking mass spectrometry experiments. Bioinformatics 36(4):1296-129, doi: 10.1093\/bioinformatics\/btz732<\/p>\n\n\n\n<p>Klein ME, Mauch S, Rieckmann M, Mart\u00ednez DG, Hause G, Noutsias M, Hofmann U, Lucas H, Meister A, Ramos G, Loppnow H, M\u00e4der K (2020) Phosphatidylserine (PS) and phosphatidylglycerol (PG) nanodispersions as potential anti-inflammatory therapeutics: Comparison of in vitro activity and impact of pegylation. Nanomedicine 102096, doi: 10.1016\/j.nano.2019.102096<\/p>\n\n\n\n<p><strong><u>Publications 2019<\/u><\/strong><\/p>\n\n\n\n<p>*co-first author *co-corresponding author<\/p>\n\n\n\n<p>Volland C, Schott P, Didi\u00e9 M, M\u00e4nner J, Uns\u00f6ld B, Toischer K, <strong>Schmidt C<\/strong>, Urlaub H, Nickels K, Kn\u00f6ll R, Schmidt A, Guan K, Hasenfu\u00df G, Seidler T. (2019) Control of p21Cip by BRAP is Critical for Cardiomyocyte Cell Cycle Progression and Survival. Cardiovasc Res. 116(3):592-604. doi: 10.1093\/cvr\/cvz177.<\/p>\n\n\n\n<p>Pyle E, Guo C, Hofmann T, <strong>Schmidt C<\/strong>, Ribeiro O, Politis A, Byrne B. (2019) Protein-lipid interactions stabilise the oligomeric state of Bor1p from Saccharomyces cerevisiae. Anal Chem. 91(20):13071-13079. doi: 10.1021\/acs.analchem.9b03271.<\/p>\n\n\n\n<p>Faull SV, Lau AMC, Martens C, Ahdash Z, Hansen K, Yebenes H, <strong>Schmidt C<\/strong>, Beuron F, Cronin NB, Morris EP, Politis A. (2019) Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome. Nat Commun. 10(1):3814. doi: 10.1038\/s41467-019-11772-y.<\/p>\n\n\n\n<p>Inga Songailiene, Marius Rutkauskas, Tomas Sinkunas, Elena Manakova, Sabine Wittig, <strong>Carla Schmidt<\/strong>, Virginijus Siksnys*and Ralf Seidel*&nbsp;(2019) Decision-Making in Cascade Complexes Harboring crRNAs of Altered Length Cell Rep 28(12), 3157-3166<\/p>\n\n\n\n<p>Bender J,&nbsp;<strong>Schmidt C<\/strong>. (2019) The CroCo cross-link converter: a user-centred tool to convert results from crosslinking mass spectrometry experiments. Bioinformatics. 36(4):1296-1297. doi: 10.1093\/bioinformatics\/btz732.<\/p>\n\n\n\n<p>Iacobucci C, Piotrowski C, Aebersold R, Amaral BC, Andrews P, Bernfur K, Borchers C, Brodie NI, Bruce JE, Cao Y, Chaignepain S, Chavez JD, Claverol S, Cox J, Davis T, Degliesposti G, Dong MQ, Edinger N, Emanuelsson C, Gay M, G\u00f6tze M, Gomes-Neto F, Gozzo FC, Gutierrez C, Haupt C, Heck AJR, Herzog F, Huang L, Hoopmann MR, Kalisman N, Klykov O, Kuka\u010dka Z, Liu F, MacCoss MJ, Mechtler K, Mesika R, Moritz RL, Nagaraj N, Nesati V, Neves-Ferreira AGC, Ninnis R, Nov\u00e1k P, O\u2019Reilly FJ, Pelzing M, Petrotchenko E, Piersimoni L, Plasencia M, Pukala T, Rand KD, Rappsilber J, Reichmann D, Sailer C, Sarnowski CP, Scheltema RA,&nbsp;<strong>Schmidt C<\/strong>, Schriemer DC, Shi Y, Skehel JM, Slavin M, Sobott F, Solis-Mezarino V, Stephanowitz H, Stengel F, Stieger CE, Trabjerg E, Trnka M, Vilaseca M, Viner R, Xiang Y, Yilmaz S, Zelter A, Ziemianowicz D, Leitner A, Sinz A. (2019) First Community-Wide, Comparative Cross-Linking Mass Spectrometry Study. Anal Chem. 91(11):6953-6961. &nbsp;doi: 10.1021\/acs.analchem.9b00658.<\/p>\n\n\n\n<p>Prajapati S, Haselbach D, Wittig S, Patel MS, Chari A,&nbsp;<strong>Schmidt C<\/strong>, Stark H, Tittmann K (2019) Structural and Functional Analyses of the Human PDH Complex Suggest a \u201cDivision-of-Labor\u201d Mechanism by Local E1 and E3 Clusters. Structure 27(7):1124-1136. doi: 10.1016\/j.str.2019.04.009.<\/p>\n\n\n\n<p>Hofmann T, <strong>Schmidt C<\/strong> (2019) Instrument response of phosphatidylglycerol lipids with varying fatty acyl chain length in nano-ESI shotgun experiments. Chem Phys Lipids. 223:104782. doi: 10.1016\/j.chemphyslip.2019.05.007.<\/p>\n\n\n\n<p>Bender J, <strong>Schmidt C<\/strong>&nbsp;(2019) Mass spectrometry of membrane protein complexes. Biol Chem. 400(7):813-829. doi: 10.1515\/hsz-2018-0443.<\/p>\n\n\n\n<p>Frick M,&nbsp;<strong>Schmidt C&nbsp;<\/strong>(2019) Mass spectrometry \u2013 a Versatile Tool for Characterizing the Lipid Environment of Membrane Protein Assemblies. Chem Phys Lipids. 221:145-157. doi: 10.1016\/j.chemphyslip.2019.04.001<\/p>\n\n\n\n<p>Frick M,&nbsp;<strong>Schmidt C<\/strong> (2019) Massenspektrometrie von Phospholipiden aus Liposomen. Biospektrum 25(2):167-169<\/p>\n\n\n\n<p>Wittig S, Haupt C, Hoffmann W, Kostmann S, Pagel K, <strong>Schmidt C<\/strong> (2019) Oligomerisation of Synaptobrevin-2 Studied by Native Mass Spectrometry and Chemical Cross-Linking. J Am Soc Mass Spectrom. 30(1):149-160. doi: 10.1007\/s13361-018-2000-4<\/p>\n\n\n\n<p><strong><u>Publications 2018<\/u><\/strong><\/p>\n\n\n\n<p>*co-first author *co-corresponding author<\/p>\n\n\n\n<p>Nagarathinam K, Nakada-Nakura Y, Parthier C, Terada T, Juge N, Jaenecke F, Liu K, Hotta Y, Mivaji T, Omote H, Iwata S, Nomura N, <strong>Stubbs MT<\/strong>, Tanabe M (2018) Outward open conformation of a Major Facilitator Superfamily multidrug\/H+ antiporter provides insights into switching mechanism. Nat commun 9(1):4005.<\/p>\n\n\n\n<p>Bonvin AMJJ, Karaca E, <strong>Kastritis PL<\/strong>, Rodrigues JPGLM (2018) Defining distance restraints in HADDOCK. Nat Protoc. 13(7):1503, doi: 10.1038\/s41596-018-0017-6<\/p>\n\n\n\n<p>Frick M, Hofmann T, Haupt C, <strong>Schmidt C<\/strong> (2018) A novel sample preparation strategy for shotgun lipidomics of phospholipids employing multilamellar vesicles. Anal Bioanal Chem. 410(18):4253-4258, doi: 10.1007\/s00216-018-1113-8<\/p>\n\n\n\n<p>Prochaska H, Thieme S, Daum S, Grau J, Schmidtke C, Hallensleben M, John P,<strong> Bacia K<\/strong>, Bonas U (2018) A conserved motif promotes HpaB-regulated export of type III effectors from Xanthomonas. Mol Plant Pathol. doi: 10.1111\/mpp.12725<\/p>\n\n\n\n<p><strong><u>Publications 2017<\/u><\/strong><\/p>\n\n\n\n<p>*involved in equal shares, *co-corresponding author<\/p>\n\n\n\n<p>Nagarathinam K, Jaenecke F, Nakada-Nakura Y, Hotta Y, Liu K, Iwata S,&nbsp;<strong>Stubbs MT<\/strong>, Nomura N, Tanabe M. (2017) The multidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis. Act Crystallogr F Struct Biol Commun 73(Pt 7):423-430.<\/p>\n\n\n\n<p>Blees A, Januliene D, Hofmann T, Koller N,&nbsp;<strong>Schmidt C<\/strong>, Trowitzsch S, Moeller A, Tamp\u00e9 R (2017) Structure of the human MHC-I peptide-loading complex. Nature 551(7681):525-528, doi: 10.1038\/nature24627<\/p>\n\n\n\n<p>Cotrim CA, Weidner A, Strehmel N, Bisol TB, Meyer D, Brandt W, Wessjohann LA, <strong>Stubbs, MT<\/strong> (2017) A Distinct Arimatic Prenyltransferase Associated with the Futalosine Pathway. ChemistrySelect 2:9319-9325, doi: 10.1002\/slct.201702151<\/p>\n\n\n\n<p>Degiacomi M, <strong>Schmidt C<\/strong>, Baldwin AJ, Benesch JLP (2017) Accommodating protein dynamics in the modelling of che-mical cross-links. Structure 25:1751-1757.e5, doi: 10.1016\/j.str.2017.08.015<\/p>\n\n\n\n<p>Fonseca-Ornelas L, <strong>Schmidt C<\/strong>, Camacho-Zarco AR, Fernandez CO, Becker S, Zweckstetter M (2017) Small-Molecule-Induced Soluble Oligomers of \u03b1-Synuclein with Helical Structure. Chemistry 23(53):13010-13014, doi: 10.1002\/chem.201703001<\/p>\n\n\n\n<p>Haupt C*, Hofmann T*, Wittig S*, Politis A, <strong>Schmidt C<\/strong> (2017) Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies. J Vis Exp. 129, doi: 10.3791\/56747<\/p>\n\n\n\n<p>Ichikawa M, Liu D,<strong>&nbsp;Kastritis PL<\/strong>, Basu K, Hsu TC, Yang S, Bui KH (2017) Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins. Nat Commun. 8:15035, doi: 10.1038\/ncomms15035<\/p>\n\n\n\n<p><strong>Kastritis PL*<\/strong>, O\u2019Reilly FJ*, Bock T*, Li Y, Rogon MZ, Buczak K, Romanov N, Betts MJ, Bui KH, Hagen WJ, Hennrich ML, Mackmull MT, Rappsilber J, Russell RB, Bork P, Beck M, Gavin AC (2017) Capturing protein communities by structural proteomics in a thermophilic eukaryote. Mol Syst Biol. 13(7):936,<br>doi: 10.15252\/msb.20167412<\/p>\n\n\n\n<p>Kr\u00fcger D, Ebenhan J, Werner S, <strong>Bacia K<\/strong> (2017) Measuring Protein Binding to Lipid Vesicles by Fluorescence Cross-Corre-lation Spectroscopy. Biophys Journal. 113(6): 1311\u20131320, doi: 10.1016\/j.bpj.2017.06.023<\/p>\n\n\n\n<p>Kumar A, <strong>Balbach J<\/strong> (2017) Targeting the molecular chaperone SlyD to inhibit bacterial growth with a small molecule. Sci Rep. 7:42141, doi: 10.1038\/srep42141<\/p>\n\n\n\n<p>Nagarathinam K, Jaenecke F, Nakada-Nakura Y, Hotta Y, Liu K, Iwata S, <strong>Stubbs MT<\/strong>, Nomura N, Tanabe M (2017) The mul-tidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis. Acta Crystallogr F Struct Biol Commun. 73(Pt 7):423-430,<br>doi: 10.1107\/S2053230X17008500<\/p>\n\n\n\n<p>Piechotta A, Parthier C, Kleinschmidt M, Gnoth K, Pillot T, Lues I, Demuth HU, Schilling S, Rahfeld JU, <strong>Stubbs MT<\/strong> (2017) Structural and functional analyses of pyroglutamate-amyloid-\u03b2-specific antibodies as a basis for Alzheimer immunothe-rapy. J Biol Chem. 292(30):12713-12724, doi: 10.1074\/jbc.M117.777839<\/p>\n\n\n\n<p>Politis A#, <strong>Schmidt C#<\/strong> (2017) Structural characterisation of medically relevant protein assemblies by integrating mass spectrometry with computational modelling. J Proteomics pii: S1874-3919(17)30146-X, doi: 10.1016\/j.jprot.2017.04.019<\/p>\n\n\n\n<p>Scacioc A, <strong>Schmidt C*<\/strong>, Hofmann T, Urlaub H, K\u00fchnel K*, P\u00e9rez-Lara \u00c1* (2017) Structure based biophysical characterizati-on of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding. Sci Rep. 7(1):14008, doi: 10.1038\/s41598-017-14337-5<\/p>\n\n\n\n<p>Schaller-Laudel S, Latowski D, Jemio\u0142a-Rzemi\u0144ska M, Strza\u0142ka K, Daum S, <strong>Bacia K<\/strong>, Wilhelm C, Goss R (2017) Influence of thylakoid membrane lipids on the structure of aggregated light-harvesting complexes of the diatom Thalassiosira pseu-donana and the green alga Mantoniella squamata. Physiol Plant. 160(3):339-358, doi: 10.1111\/ppl.12565<\/p>\n\n\n\n<p><strong>Schmidt C<\/strong>, Urlaub H (2017) Combining Cross-linking Mass Spectrometry (CX-MS) and Cryo-electron Microscopy (cryo-EM) for Structural Elucidations of Large Protein Complexes. Curr Opin Struct Biol. 46:157-168, doi: 10.1016\/j.sbi.2017.10.005<\/p>\n\n\n\n<p><strong>Schmidt C<\/strong>, Robinson CV (2017) Biophysical methods: behind the scenes of the cryo-EM revolution. Curr Opin Struct Biol. Editorial. 46:ix-xi, doi: 10.1016\/j.sbi.2017.10.018<\/p>\n\n\n\n<p>Scacioc A, <strong>Schmidt C*<\/strong>, Hofmann T, Urlaub H, K\u00fchnel K*, P\u00e9rez-Lara \u00c1* (2017) Structure based biophysical characterizati-on of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding<\/p>\n\n\n\n<p>Vangone A, Rodrigues JP, Xue LC, van Zundert GC, Geng C, Kurkcuoglu Z, Nellen M, Narasimhan S, Karaca E, van Dijk M, Melquiond AS, Visscher KM, Trellet M,&nbsp;<strong>Kastritis PL<\/strong>, Bonvin AM (2017) Sense and simplicity in HADDOCK scoring: Lessons from CASP-CAPRI round 1. Proteins. 85(3):417-423, doi: 10.1002\/prot.25198<\/p>\n\n\n\n<p><strong><u>Publications 2016<\/u><\/strong><\/p>\n\n\n\n<p>*involved in equal shares, *co-corresponding author<\/p>\n\n\n\n<p>Adler J, Baumann M, Voigt B, Scheidt HA, Bhowmik D, H\u00e4upl T, Abel B, Madhu PK, <strong>Balbach J<\/strong>, Maiti S, Huster D (2016) A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid \u00df (1-40). Chemphyschem. 17(17):2744-53, doi: 10.1002\/cphc.201600413<\/p>\n\n\n\n<p>Achilles A, Baerenwald R, Lechner BD, Werner S, Ebert H, Tschierske C, Blume A, <strong>Bacia K<\/strong>, Saalwaechter K (2016) Self-Assembly of X-Shaped Bolapolyphiles in Lipid Membranes: Solid-State NMR Investigations. Langmuir, 32(3): 673-682, doi: 10.1021\/acs<\/p>\n\n\n\n<p>Daum B, Auerswald A, Gruber T, Hause G, <strong>Balbach J<\/strong>, K\u00fchlbrandt W, Meister A (2016) Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane. J Struct Biol. 194(3):375-82, doi: 10.1016\/j. jsb.2016.03.017<\/p>\n\n\n\n<p>Garvey M, Baumann M, Wulff M, Kumar ST, Markx D, Morgado I, Kn\u00fcpfer U, Horn U, Mawrin C, F\u00e4ndrich M, <strong>Balbach J<\/strong> (2016) Molecular architecture of A\u00df fibrils grown in cerebrospinal fluid solution and in a cell culture model of A\u00df plaque formation. Amyloids 23(2):76-85, doi: 10.3109\/13506129.2016.1146989<\/p>\n\n\n\n<p>Kr\u00fcger M, Kalbacher H, <strong>Kastritis PL<\/strong>, Bischof J, Barth H, Henne-Bruns D, Vorgias C, Sarno S, Pinna LA, Knippschild U (2016) New potential peptide therapeutics perturbing CK1d\/a-tubulin interaction. Cancer Lett. Jun 1;375(2):375-383, doi: 10.1016\/j.canlet.2016.03.021<\/p>\n\n\n\n<p>Kumar A, Baumann M, <strong>Balbach J<\/strong> (2016) Small Molecule Inhibited Parathyroid Hormone Mediated cAMP Response by N-Terminal Peptide Binding. Sci Rep. 6:22533, doi: 10.1038\/srep22533<\/p>\n\n\n\n<p>Lensink MF, Velankar S, Kryshtafovych A, Huang SY, Schneidman-Duhovny D, Sali A, Segura J, Fernandez-Fuentes N, Viswanath S, Elber R, Grudinin S, Popov P, Neveu E, Lee H, Baek M, Park S, Heo L, Rie Lee G, Seok C, Qin S, Zhou HX, Ritchie DW, Maigret B, Devignes MD, Ghoorah A, Torchala M, Chaleil RA, Bates PA, Ben-Zeev E, Eisenstein M, Negi SS, Weng Z, Vreven T, Pierce BG, Borrman TM, Yu J, Ochsenbein F, Guerois R, Vangone A, Rodrigues JP, van Zundert G, Nellen M, Xue L, Karaca E, Melquiond AS, Visscher K, <strong>Kastritis PL<\/strong>, Bonvin AM, Xu X, Qiu L, Yan C, Li J, Ma Z, Cheng J, Zou X, Shen Y, Peterson LX, Kim HR, Roy A, Han X, Esquivel-Rodriguez J, Kihara D, Yu X, Bruce NJ, Fuller JC, Wade RC, Anishchenko I, Kundrotas PJ, Vakser IA, Imai K, Yamada K, Oda T, Nakamura T, Tomii K, Pallara C, Romero-Durana M, Jim\u00e9nez-Garc\u00eda B, Moal IH, F\u00e9rnandez-Recio J, Joung JY, Kim JY, Joo K, Lee J, Kozakov D, Vajda S, Mottarella S, Hall DR, Beglov D, Mamonov A, Xia B, Bohnuud T, Del Carpio CA, Ichiishi E, Marze N, Kuroda D, Roy Burman SS, Gray JJ, Chermak E, Cavallo L, Oliva R, Tovchigrechko A, Wodak SJ. (2016) Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling: A CASP-CAPRI experiment. Proteins. 84 Suppl 1:323-48, doi: 10.1002\/prot.25007<\/p>\n\n\n\n<p>Liko I, Degiacomi MT, Mohammed S, Yoshikawa S, <strong>Schmidt C#<\/strong>, Robinson CV# (2016) Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding. Proc Natl Acad Sci U S A. 113(29):8230-5, doi: 10.1073\/pnas.1600354113<\/p>\n\n\n\n<p>Mazhab-Jafari MT, Rohou A, <strong>Schmidt C<\/strong>, Bueler SA, Benlekbir S, Robinson CV, Rubinstein JL (2016) Atomic model for the membrane-embedded V0 motor of a eukaryotic V-ATPase. Nature 539(7627):118-122,<br>doi: 10.1038\/nature19828<\/p>\n\n\n\n<p>Ori A, Iskar M, Buczak K, <strong>Kastritis PL<\/strong>, Parca L, Andr\u00e9s-Pons A, Singer S, Bork P, Beck M.<br>Spatiotemporal variation of mammalian protein complex stoichiometries. (2016) Genome Biol. 17:47,<br>doi: 10.1186\/s13059-016-0912-5<\/p>\n\n\n\n<p>Roos M, Ott M, Hofmann M, Link S, R\u00f6ssler E, <strong>Balbach J<\/strong>, Krushelnitsky A, Saalw\u00e4chter K. (2016) Coupling and Decoupling of Rotational and Translational Diffusion of Proteins under Crowding Conditions. J Am Chem Soc. 138(32):10365-72, doi: 10.1021\/jacs.6b06615<\/p>\n\n\n\n<p>Rothe M, Gruber T, Gr\u00f6ger S, <strong>Balbach J<\/strong>, Saalw\u00e4chter K, Roos M (2017) Transient binding accounts for apparent violation of the generalized Stokes-Einstein relation in crowded protein solutions. Phys Chem Chem Phys. 18(27):18006-14, doi: 10.1039\/c6cp01056c<\/p>\n\n\n\n<p>Silva-Martin N, Daud\u00e9n MI, Glatt S, Hoffmann NA, <strong>Kastritis PL<\/strong>, Bork P, Beck M, M\u00fcller CW.<br>The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1\/Rvb2 Complex. (2016) PLoS One. 11(1):e0146457,<br>doi: 10.1371\/journal.pone.0146457<\/p>\n\n\n\n<p>Spiliotopoulos D, <strong>Kastritis PL<\/strong>, Melquiond AS, Bonvin AM, Musco G, Rocchia W, Spitaleri A.<br>dMM-PBSA: A New HADDOCK Scoring Function for Protein-Peptide Docking. (2016) Front Mol Biosci. 3:46, doi: 10.3389\/fmolb.2016.00046<\/p>\n\n\n\n<p>Villmow M, Baumann M, Malesevic M, Sachs R, Hause G, F\u00e4ndrich M, <strong>Balbach J,<\/strong> Schiene-Fischer C (2016) Inhibition of A\u00df(1-40) fibril formation by cyclophilins. Biochem J. 473(10):1355-68,<br>doi: 10.1042\/BCJ20160098<\/p>\n\n\n\n<p>Wulff M, Baumann M, Th\u00fcmmler A, Yadav JK, Heinrich L, Kn\u00fcpfer U, Schlenzig D, Schierhorn A, Rahfeld JU, Horn U, <strong>Balbach J<\/strong>, Demuth HU, F\u00e4ndrich M. (2016) Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified A\u00df Peptides. Angew Chem Int Ed Engl. 55(16):5081-4,<br>doi: 10.1002\/anie.201511099<\/p>\n\n\n\n<p>Xue LC, Rodrigues JP,<strong> Kastritis PL<\/strong>, Bonvin AM, Vangone A. (2016)<br>PRODIGY: a web server for predicting the binding affinity of protein-protein complexes. Bioinformatics. 32(23):3676-3678, doi: 10.1093\/bioinformatics\/btw514<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Publications 2021 *co-first author *co-corresponding author Barth M, Schmidt C (2021) Quantitative Cross-Linking of Proteins and Protein Complexes. Methods Mol Biol. 2228:385-400, doi: 10.1007\/978-1-0716-1024-4_26 Rozanova S, Barkovits K, Nikolov M, Schmidt C, Urlaub H, Marcus K (2021) Quantitative Mass Spectrometry-Based Proteomics: An Overview. Methods Mol Biol. 2228:85-116, doi: 10.1007\/978-1-0716-1024-4_8 Bender J, Schmidt C (2021) Exploring [&hellip;]<\/p>\n","protected":false},"author":6144,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/pages\/28"}],"collection":[{"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/users\/6144"}],"replies":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/comments?post=28"}],"version-history":[{"count":1,"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/pages\/28\/revisions"}],"predecessor-version":[{"id":30,"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/pages\/28\/revisions\/30"}],"wp:attachment":[{"href":"https:\/\/blogs.urz.uni-halle.de\/halomem\/wp-json\/wp\/v2\/media?parent=28"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}