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Items: 49

1.

FANally…A Structure Emerges of the Fanconi Anemia Core Complex.

Aguirre JD, Thomä NH.

Trends Biochem Sci. 2020 Apr;45(4):275-276. doi: 10.1016/j.tibs.2020.01.001. Epub 2020 Jan 24.

PMID:
31987666
2.

PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network.

Reichermeier KM, Straube R, Reitsma JM, Sweredoski MJ, Rose CM, Moradian A, den Besten W, Hinkle T, Verschueren E, Petzold G, Thomä NH, Wertz IE, Deshaies RJ, Kirkpatrick DS.

Mol Cell. 2020 Mar 5;77(5):1092-1106.e9. doi: 10.1016/j.molcel.2019.12.013. Epub 2020 Jan 20.

PMID:
31973889
3.

Taking the Brakes Off Targeted Protein Degradation.

Kozicka Z, Petzold G, Thomä NH.

Cell Chem Biol. 2020 Jan 16;27(1):16-18. doi: 10.1016/j.chembiol.2019.12.010.

PMID:
31951816
4.

Structural Basis of BRCC36 Function in DNA Repair and Immune Regulation.

Rabl J, Bunker RD, Schenk AD, Cavadini S, Gill ME, Abdulrahman W, Andrés-Pons A, Luijsterburg MS, Ibrahim AFM, Branigan E, Aguirre JD, Marceau AH, Guérillon C, Bouwmeester T, Hassiepen U, Peters AHFM, Renatus M, Gelman L, Rubin SM, Mailand N, van Attikum H, Hay RT, Thomä NH.

Mol Cell. 2019 Aug 8;75(3):483-497.e9. doi: 10.1016/j.molcel.2019.06.002. Epub 2019 Jun 25.

5.

Publisher Correction: DNA damage detection in nucleosomes involves DNA register shifting.

Matsumoto S, Cavadini S, Bunker RD, Grand RS, Potenza A, Rabl J, Yamamoto J, Schenk AD, Schübeler D, Iwai S, Sugasawa K, Kurumizaka H, Thomä NH.

Nature. 2019 Jul;571(7764):E6. doi: 10.1038/s41586-019-1343-8.

PMID:
31239520
6.

Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane.

Fontana GA, Hess D, Reinert JK, Mattarocci S, Falquet B, Klein D, Shore D, Thomä NH, Rass U.

Nat Commun. 2019 Jun 10;10(1):2535. doi: 10.1038/s41467-019-10349-z.

7.

DNA damage detection in nucleosomes involves DNA register shifting.

Matsumoto S, Cavadini S, Bunker RD, Grand RS, Potenza A, Rabl J, Yamamoto J, Schenk AD, Schübeler D, Iwai S, Sugasawa K, Kurumizaka H, Thomä NH.

Nature. 2019 Jul;571(7763):79-84. doi: 10.1038/s41586-019-1259-3. Epub 2019 May 29. Erratum in: Nature. 2019 Jun 26;:.

8.

Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN.

Sievers QL, Petzold G, Bunker RD, Renneville A, Słabicki M, Liddicoat BJ, Abdulrahman W, Mikkelsen T, Ebert BL, Thomä NH.

Science. 2018 Nov 2;362(6414). pii: eaat0572. doi: 10.1126/science.aat0572.

9.

Regulatory control of DNA end resection by Sae2 phosphorylation.

Cannavo E, Johnson D, Andres SN, Kissling VM, Reinert JK, Garcia V, Erie DA, Hess D, Thomä NH, Enchev RI, Peter M, Williams RS, Neale MJ, Cejka P.

Nat Commun. 2018 Oct 1;9(1):4016. doi: 10.1038/s41467-018-06417-5.

10.

Shepherding DNA ends: Rif1 protects telomeres and chromosome breaks.

Fontana GA, Reinert JK, Thomä NH, Rass U.

Microb Cell. 2018 May 17;5(7):327-343. doi: 10.15698/mic2018.07.639. Review.

11.

Activity-dependent neuroprotective protein recruits HP1 and CHD4 to control lineage-specifying genes.

Ostapcuk V, Mohn F, Carl SH, Basters A, Hess D, Iesmantavicius V, Lampersberger L, Flemr M, Pandey A, Thomä NH, Betschinger J, Bühler M.

Nature. 2018 May;557(7707):739-743. doi: 10.1038/s41586-018-0153-8. Epub 2018 May 23.

PMID:
29795351
12.

Rif1 maintains telomeres and mediates DNA repair by encasing DNA ends.

Mattarocci S, Reinert JK, Bunker RD, Fontana GA, Shi T, Klein D, Cavadini S, Faty M, Shyian M, Hafner L, Shore D, Thomä NH, Rass U.

Nat Struct Mol Biol. 2017 Jul;24(7):588-595. doi: 10.1038/nsmb.3420. Epub 2017 Jun 12.

PMID:
28604726
13.

Targeted protein degradation: You can glue it too!

Walczak MJ, Petzold G, Thomä NH.

Nat Chem Biol. 2017 Apr 13;13(5):452-453. doi: 10.1038/nchembio.2355. No abstract available.

PMID:
28406888
14.

Cullin-RING ubiquitin E3 ligase regulation by the COP9 signalosome.

Cavadini S, Fischer ES, Bunker RD, Potenza A, Lingaraju GM, Goldie KN, Mohamed WI, Faty M, Petzold G, Beckwith RE, Tichkule RB, Hassiepen U, Abdulrahman W, Pantelic RS, Matsumoto S, Sugasawa K, Stahlberg H, Thomä NH.

Nature. 2016 Mar 31;531(7596):598-603. doi: 10.1038/nature17416.

PMID:
27029275
15.

Structural basis of lenalidomide-induced CK1α degradation by the CRL4(CRBN) ubiquitin ligase.

Petzold G, Fischer ES, Thomä NH.

Nature. 2016 Apr 7;532(7597):127-30. doi: 10.1038/nature16979. Epub 2016 Feb 24.

PMID:
26909574
16.

SPLINTS: small-molecule protein ligand interface stabilizers.

Fischer ES, Park E, Eck MJ, Thomä NH.

Curr Opin Struct Biol. 2016 Apr;37:115-22. doi: 10.1016/j.sbi.2016.01.004. Epub 2016 Jan 30. Review.

17.

Structural basis of pyrimidine-pyrimidone (6-4) photoproduct recognition by UV-DDB in the nucleosome.

Osakabe A, Tachiwana H, Kagawa W, Horikoshi N, Matsumoto S, Hasegawa M, Matsumoto N, Toga T, Yamamoto J, Hanaoka F, Thomä NH, Sugasawa K, Iwai S, Kurumizaka H.

Sci Rep. 2015 Nov 17;5:16330. doi: 10.1038/srep16330.

18.

Functional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein.

Matsumoto S, Fischer ES, Yasuda T, Dohmae N, Iwai S, Mori T, Nishi R, Yoshino K, Sakai W, Hanaoka F, Thomä NH, Sugasawa K.

Nucleic Acids Res. 2015 Feb 18;43(3):1700-13. doi: 10.1093/nar/gkv038. Epub 2015 Jan 27.

19.

Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide.

Fischer ES, Böhm K, Lydeard JR, Yang H, Stadler MB, Cavadini S, Nagel J, Serluca F, Acker V, Lingaraju GM, Tichkule RB, Schebesta M, Forrester WC, Schirle M, Hassiepen U, Ottl J, Hild M, Beckwith RE, Harper JW, Jenkins JL, Thomä NH.

Nature. 2014 Aug 7;512(7512):49-53. doi: 10.1038/nature13527. Epub 2014 Jul 16.

20.

Crystal structure of the human COP9 signalosome.

Lingaraju GM, Bunker RD, Cavadini S, Hess D, Hassiepen U, Renatus M, Fischer ES, Thomä NH.

Nature. 2014 Aug 14;512(7513):161-5. doi: 10.1038/nature13566. Epub 2014 Jul 16.

PMID:
25043011
21.

Rif1 controls DNA replication timing in yeast through the PP1 phosphatase Glc7.

Mattarocci S, Shyian M, Lemmens L, Damay P, Altintas DM, Shi T, Bartholomew CR, Thomä NH, Hardy CF, Shore D.

Cell Rep. 2014 Apr 10;7(1):62-9. doi: 10.1016/j.celrep.2014.03.010. Epub 2014 Mar 27.

22.

Structural and mechanistic insight into Holliday-junction dissolution by topoisomerase IIIα and RMI1.

Bocquet N, Bizard AH, Abdulrahman W, Larsen NB, Faty M, Cavadini S, Bunker RD, Kowalczykowski SC, Cejka P, Hickson ID, Thomä NH.

Nat Struct Mol Biol. 2014 Mar;21(3):261-8. doi: 10.1038/nsmb.2775. Epub 2014 Feb 9.

23.

Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions.

Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH.

Cell. 2013 Jun 6;153(6):1340-53. doi: 10.1016/j.cell.2013.05.007.

24.

An N-terminal acidic region of Sgs1 interacts with Rpa70 and recruits Rad53 kinase to stalled forks.

Hegnauer AM, Hustedt N, Shimada K, Pike BL, Vogel M, Amsler P, Rubin SM, van Leeuwen F, Guénolé A, van Attikum H, Thomä NH, Gasser SM.

EMBO J. 2012 Sep 12;31(18):3768-83. doi: 10.1038/emboj.2012.195. Epub 2012 Jul 20.

25.

The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation.

Fischer ES, Scrima A, Böhm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thomä NH.

Cell. 2011 Nov 23;147(5):1024-39. doi: 10.1016/j.cell.2011.10.035.

26.

Determinants and dynamics of genome accessibility.

Bell O, Tiwari VK, Thomä NH, Schübeler D.

Nat Rev Genet. 2011 Jul 12;12(8):554-64. doi: 10.1038/nrg3017. Review.

PMID:
21747402
27.

Detecting UV-lesions in the genome: The modular CRL4 ubiquitin ligase does it best!

Scrima A, Fischer ES, Lingaraju GM, Böhm K, Cavadini S, Thomä NH.

FEBS Lett. 2011 Sep 16;585(18):2818-25. doi: 10.1016/j.febslet.2011.04.064. Epub 2011 May 6. Review.

28.

Histone methylation by PRC2 is inhibited by active chromatin marks.

Schmitges FW, Prusty AB, Faty M, Stützer A, Lingaraju GM, Aiwazian J, Sack R, Hess D, Li L, Zhou S, Bunker RD, Wirth U, Bouwmeester T, Bauer A, Ly-Hartig N, Zhao K, Chan H, Gu J, Gut H, Fischle W, Müller J, Thomä NH.

Mol Cell. 2011 May 6;42(3):330-41. doi: 10.1016/j.molcel.2011.03.025.

29.

Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex.

Scrima A, Konícková R, Czyzewski BK, Kawasaki Y, Jeffrey PD, Groisman R, Nakatani Y, Iwai S, Pavletich NP, Thomä NH.

Cell. 2008 Dec 26;135(7):1213-23. doi: 10.1016/j.cell.2008.10.045.

30.

Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment.

Blankenfeldt W, Thomä NH, Wray JS, Gautel M, Schlichting I.

Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17713-7. Epub 2006 Nov 9.

31.

Physical and functional mapping of the replication protein a interaction domain of the werner and bloom syndrome helicases.

Doherty KM, Sommers JA, Gray MD, Lee JW, von Kobbe C, Thoma NH, Kureekattil RP, Kenny MK, Brosh RM Jr.

J Biol Chem. 2005 Aug 19;280(33):29494-505. Epub 2005 Jun 17.

32.

Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54.

Thomä NH, Czyzewski BK, Alexeev AA, Mazin AV, Kowalczykowski SC, Pavletich NP.

Nat Struct Mol Biol. 2005 Apr;12(4):350-6. Epub 2005 Apr 3.

PMID:
15806108
33.

Werner syndrome protein contains three structure-specific DNA binding domains.

von Kobbe C, Thomä NH, Czyzewski BK, Pavletich NP, Bohr VA.

J Biol Chem. 2003 Dec 26;278(52):52997-3006. Epub 2003 Oct 8.

34.

Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase.

Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K.

Mol Cell. 2003 Feb;11(2):483-94.

35.

BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure.

Yang H, Jeffrey PD, Miller J, Kinnucan E, Sun Y, Thoma NH, Zheng N, Chen PL, Lee WH, Pavletich NP.

Science. 2002 Sep 13;297(5588):1837-48.

36.

In vitro assembly, purification, and crystallization of the rab geranylgeranyl transferase:substrate complex.

Rak A, Niculae A, Kalinin A, Thomä NH, Sidorovitch V, Goody RS, Alexandrov K.

Protein Expr Purif. 2002 Jun;25(1):23-30.

PMID:
12071695
37.

Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates.

Dursina B, Thomä NH, Sidorovitch V, Niculae A, Iakovenko A, Rak A, Albert S, Ceacareanu AC, Kölling R, Herrmann C, Goody RS, Alexandrov K.

Biochemistry. 2002 May 28;41(21):6805-16.

PMID:
12022885
38.

Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase.

Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K.

J Struct Biol. 2001 Nov;136(2):158-61.

PMID:
11886217
39.

Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1.

Thomä NH, Iakovenko A, Goody RS, Alexandrov K.

J Biol Chem. 2001 Dec 28;276(52):48637-43. Epub 2001 Oct 23.

40.

Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate.

Thomä NH, Niculae A, Goody RS, Alexandrov K.

J Biol Chem. 2001 Dec 28;276(52):48631-6. Epub 2001 Oct 8.

41.

Expression of mammalian geranylgeranyltransferase type-II in Escherichia coli and its application for in vitro prenylation of Rab proteins.

Kalinin A, Thomä NH, Iakovenko A, Heinemann I, Rostkova E, Constantinescu AT, Alexandrov K.

Protein Expr Purif. 2001 Jun;22(1):84-91.

PMID:
11388804
42.

Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II.

Thomä NH, Iakovenko A, Kalinin A, Waldmann H, Goody RS, Alexandrov K.

Biochemistry. 2001 Jan 9;40(1):268-74.

PMID:
11141079
43.

Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II.

Thomä NH, Iakovenko A, Owen D, Scheidig AS, Waldmann H, Goody RS, Alexandrov K.

Biochemistry. 2000 Oct 3;39(39):12043-52.

PMID:
11009619
44.

Protection of radical intermediates at the active site of adenosylcobalamin-dependent methylmalonyl-CoA mutase.

Thomä NH, Evans PR, Leadlay PF.

Biochemistry. 2000 Aug 8;39(31):9213-21.

PMID:
10924114
45.

Semi-synthetic Rab proteins as tools for studying intermolecular interactions.

Iakovenko A, Rostkova E, Merzlyak E, Hillebrand AM, Thomä NH, Goody RS, Alexandrov K.

FEBS Lett. 2000 Feb 25;468(2-3):155-8.

46.

Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.

Thomä NH, Meier TW, Evans PR, Leadlay PF.

Biochemistry. 1998 Oct 13;37(41):14386-93.

PMID:
9772164
47.

Mechanistic and structural studies on methylmalonyl-CoA mutase.

Thomä NH, Leadlay PF.

Biochem Soc Trans. 1998 Aug;26(3):293-8. Review. No abstract available.

PMID:
9765867
48.

Tritium isotope effects in adenosylcobalamin-dependent methylmalonyl-CoA mutase.

Meier TW, Thomä NH, Leadlay PF.

Biochemistry. 1996 Sep 10;35(36):11791-6.

PMID:
8794760

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