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Items: 1 to 20 of 30

1.
Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein–protein interactions in the human cell
Tara K. Bartolec, Xabier Vázquez-Campos, Alexander Norman, Clement Luong, Marcus Johnson, Richard J. Payne, Marc R. Wilkins, Joel P. Mackay, Jason K. K. Low
Proc Natl Acad Sci U S A. 2023 Apr 25; 120(17): e2219418120. Published online 2023 Apr 18. doi: 10.1073/pnas.2219418120
PMCID:
PMC10151615
AbstractArticlePDF–2.9M
2.
Two-Dimensional Fractionation Method for Proteome-Wide Cross-Linking Mass Spectrometry Analysis
Fenglong Jiao, Clinton Yu, Andrew Wheat, Xiaorong Wang, Scott D. Rychnovsky, Lan Huang
Anal Chem. Author manuscript; available in PMC 2022 Apr 30.
Published in final edited form as: Anal Chem. 2022 Mar 15; 94(10): 4236–4242. Published online 2022 Mar 2. doi: 10.1021/acs.analchem.1c04485
PMCID:
PMC9056026
AbstractArticlePDF–1.0M
3.
Protein interaction landscapes revealed by advanced in vivo cross-linking–mass spectrometry
Andrew Wheat, Clinton Yu, Xiaorong Wang, Anthony M. Burke, Ilan E. Chemmama, Robyn M. Kaake, Peter Baker, Scott D. Rychnovsky, Jing Yang, Lan Huang
Proc Natl Acad Sci U S A. 2021 Aug 10; 118(32): e2023360118. Published online 2021 Aug 4. doi: 10.1073/pnas.2023360118
PMCID:
PMC8364181
AbstractArticlePDF–3.0M
4.
Dual Proteome-scale Networks Reveal Cell-specific Remodeling of the Human Interactome
Edward L. Huttlin, Raphael J. Bruckner, Jose Navarrete-Perea, Joe R. Cannon, Kurt Baltier, Fana Gebreab, Melanie P. Gygi, Alexandra Thornock, Gabriela Zarraga, Stanley Tam, John Szpyt, Brandon M. Gassaway, Alexandra Panov, Hannah Parzen, Sipei Fu, Arvene Golbazi, Eila Maenpaa, Keegan Stricker, Sanjukta Guha Thakurta, Tian Zhang, Ramin Rad, Joshua Pan, David P. Nusinow, Joao A. Paulo, Devin K. Schweppe, Laura Pontano Vaites, J. Wade Harper, Steven P. Gygi
Cell. Author manuscript; available in PMC 2022 May 27.
Published in final edited form as: Cell. 2021 May 27; 184(11): 3022–3040.e28. Published online 2021 May 6. doi: 10.1016/j.cell.2021.04.011
PMCID:
PMC8165030
AbstractArticlePDF–2.2M
5.
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
Lotte van Beek, Éilís McClay, Saleha Patel, Marianne Schimpl, Laura Spagnolo, Taiana Maia de Oliveira
Int J Mol Sci. 2021 May; 22(10): 5112. Published online 2021 May 12. doi: 10.3390/ijms22105112
PMCID:
PMC8150716
AbstractArticlePDF–5.0M
6.
A reference map of the human binary protein interactome
Katja Luck, Dae-Kyum Kim, Luke Lambourne, Kerstin Spirohn, Bridget E. Begg, Wenting Bian, Ruth Brignall, Tiziana Cafarelli, Francisco J. Campos-Laborie, Benoit Charloteaux, Dongsic Choi, Atina G. Coté, Meaghan Daley, Steven Deimling, Alice Desbuleux, Amélie Dricot, Marinella Gebbia, Madeleine F. Hardy, Nishka Kishore, Jennifer J. Knapp, István A. Kovács, Irma Lemmens, Miles W. Mee, Joseph C. Mellor, Carl Pollis, Carles Pons, Aaron D. Richardson, Sadie Schlabach, Bridget Teeking, Anupama Yadav, Mariana Babor, Dawit Balcha, Omer Basha, Christian Bowman-Colin, Suet-Feung Chin, Soon Gang Choi, Claudia Colabella, Georges Coppin, Cassandra D’Amata, David De Ridder, Steffi De Rouck, Miquel Duran-Frigola, Hanane Ennajdaoui, Florian Goebels, Liana Goehring, Anjali Gopal, Ghazal Haddad, Elodie Hatchi, Mohamed Helmy, Yves Jacob, Yoseph Kassa, Serena Landini, Roujia Li, Natascha van Lieshout, Andrew MacWilliams, Dylan Markey, Joseph N. Paulson, Sudharshan Rangarajan, John Rasla, Ashyad Rayhan, Thomas Rolland, Adriana San-Miguel, Yun Shen, Dayag Sheykhkarimli, Gloria M. Sheynkman, Eyal Simonovsky, Murat Taşan, Alexander Tejeda, Vincent Tropepe, Jean-Claude Twizere, Yang Wang, Robert J. Weatheritt, Jochen Weile, Yu Xia, Xinping Yang, Esti Yeger-Lotem, Quan Zhong, Patrick Aloy, Gary D. Bader, Javier De Las Rivas, Suzanne Gaudet, Tong Hao, Janusz Rak, Jan Tavernier, David E. Hill, Marc Vidal, Frederick P. Roth, Michael A. Calderwood
Nature. Author manuscript; available in PMC 2020 Oct 8.
Published in final edited form as: Nature. 2020 Apr; 580(7803): 402–408. Published online 2020 Apr 8. doi: 10.1038/s41586-020-2188-x
PMCID:
PMC7169983
AbstractArticlePDF–5.4M
7.
PARP3, a new therapeutic target to alter Rictor/mTORC2 signaling and tumor progression in BRCA1-associated cancers
Carole Beck, José Manuel Rodriguez-Vargas, Christian Boehler, Isabelle Robert, Vincent Heyer, Najat Hanini, Laurent R. Gauthier, Agnès Tissier, Valérie Schreiber, Mikael Elofsson, Bernardo Reina San Martin, Françoise Dantzer
Cell Death Differ. 2019 Sep; 26(9): 1615–1630. Published online 2018 Nov 15. doi: 10.1038/s41418-018-0233-1
PMCID:
PMC6748154
AbstractArticlePDF–1.6M
8.
Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation
Gabriella Zarkovic, Ekaterina A Belousova, Ibtissam Talhaoui, Christine Saint-Pierre, Mikhail M Kutuzov, Bakhyt T Matkarimov, Denis Biard, Didier Gasparutto, Olga I Lavrik, Alexander A Ishchenko
Nucleic Acids Res. 2018 Mar 16; 46(5): 2417–2431. Published online 2018 Jan 18. doi: 10.1093/nar/gkx1318
PMCID:
PMC5861426
AbstractArticlePDF–4.4M
9.
Dna is a New Target of Parp3
E. A. Belousova, А. A. Ishchenko, O. I. Lavrik
Sci Rep. 2018; 8: 4176. Published online 2018 Mar 8. doi: 10.1038/s41598-018-22673-3
PMCID:
PMC5843604
AbstractArticlePDF–2.8M
10.
Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS J. 2017 Dec; 284(23): 4002–4016. Published online 2017 Nov 8. doi: 10.1111/febs.14297
PMCID:
PMC5725667
AbstractArticlePDF–836K
11.
PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis
Olga Karicheva, José Manuel Rodriguez-Vargas, Nadège Wadier, Kathline Martin-Hernandez, Romain Vauchelles, Najat Magroun, Agnès Tissier, Valérie Schreiber, Françoise Dantzer
Oncotarget. 2016 Sep 27; 7(39): 64109–64123. Published online 2016 Aug 26. doi: 10.18632/oncotarget.11627
PMCID:
PMC5325429
AbstractArticlePDF–3.8M
12.
PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2BGlu2
Gabrielle J. Grundy, Luis M. Polo, Zhihong Zeng, Stuart L. Rulten, Nicolas C. Hoch, Pathompong Paomephan, Yingqi Xu, Steve M. Sweet, Alan W. Thorne, Antony W. Oliver, Steve J. Matthews, Laurence H. Pearl, Keith W. Caldecott
Nat Commun. 2016; 7: 12404. Published online 2016 Aug 17. doi: 10.1038/ncomms12404
PMCID:
PMC4992063
AbstractArticlePDF–3.1M
13.
MiR-630 inhibits proliferation by targeting CDC7 kinase, but maintains the apoptotic balance by targeting multiple modulators in human lung cancer A549 cells
J-X Cao, Y Lu, J-J Qi, G-S An, Z-B Mao, H-T Jia, S-Y Li, J-H Ni
Cell Death Dis. 2014 Sep; 5(9): e1426. Published online 2014 Sep 25. doi: 10.1038/cddis.2014.386
PMCID:
PMC4225225
AbstractArticlePDF–2.3M
14.
Family-wide analysis of poly(ADP-ribose) polymerase activity
Sejal Vyas, Ivan Matic, Lilen Uchima, Jenny Rood, Roko Zaja, Ronald T. Hay, Ivan Ahel, Paul Chang
Nat Commun. Author manuscript; available in PMC 2015 Jan 21.
Published in final edited form as: Nat Commun. 2014; 5: 4426. Published online 2014 Jul 21. doi: 10.1038/ncomms5426
PMCID:
PMC4123609
AbstractArticlePDF–1.9M
15.
PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways
Carole Beck, Christian Boehler, Josée Guirouilh Barbat, Marie-Elise Bonnet, Giuditta Illuzzi, Philippe Ronde, Laurent R. Gauthier, Najat Magroun, Anbazhagan Rajendran, Bernard S. Lopez, Ralph Scully, François D. Boussin, Valérie Schreiber, Françoise Dantzer
Nucleic Acids Res. 2014 May 1; 42(9): 5616–5632. Published online 2014 Mar 5. doi: 10.1093/nar/gku174
PMCID:
PMC4027158
AbstractArticlePDF–6.1M
16.
Poly (ADP-ribose) polymerase 3 (PARP3), a potential repressor of telomerase activity
Tamara Fernández-Marcelo, Cristina Frías, Irene Pascua, Carmen de Juan, Jacqueline Head, Ana Gómez, Florentino Hernando, Jose-Ramon Jarabo, Eduardo Díaz-Rubio, Antonio-Jose Torres, Michèle Rouleau, Manuel Benito, Pilar Iniesta
J Exp Clin Cancer Res. 2014; 33(1): 19. Published online 2014 Feb 15. doi: 10.1186/1756-9966-33-19
PMCID:
PMC3937032
AbstractArticlePDF–3.4M
17.
The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair
Amanda L. Fenton, Purnata Shirodkar, Chloe J. Macrae, Li Meng, C. Anne Koch
Nucleic Acids Res. 2013 Apr; 41(7): 4080–4092. Published online 2013 Feb 28. doi: 10.1093/nar/gkt134
PMCID:
PMC3627606
AbstractArticlePDF–2.5M
18.
Genetic Susceptibility to Distinct Bladder Cancer Subphenotypes
Lin T. Guey, Montserrat García-Closas, Cristiane Murta-Nascimento, Josep Lloreta, Laia Palencia, Manolis Kogevinas, Nathaniel Rothman, Gemma Vellalta, Malu Calle, Gaëlle Marenne, Adonina Tardón, Alfredo Carrato, Reina García-Closas, Consol Serra, Debra T Silverman, Stephen Chanock, Francisco X. Real, Núria Malats
Eur Urol. Author manuscript; available in PMC 2011 Nov 18.
Published in final edited form as: Eur Urol. 2010 Feb; 57(2): 283–292. Published online 2009 Aug 12. doi: 10.1016/j.eururo.2009.08.001
PMCID:
PMC3220186
AbstractArticlePDF–595K
19.
Interactions of Pathological Hallmark Proteins: TUBULIN POLYMERIZATION PROMOTING PROTEIN/p25, β-AMYLOID, AND α-SYNUCLEIN
Judit Oláh, Orsolya Vincze, Dezső Virók, Dóra Simon, Zsolt Bozsó, Natália Tőkési, István Horváth, Emma Hlavanda, János Kovács, Anna Magyar, Mária Szűcs, Ferenc Orosz, Botond Penke, Judit Ovádi
J Biol Chem. 2011 Sep 30; 286(39): 34088–34100. Published online 2011 Aug 8. doi: 10.1074/jbc.M111.243907
PMCID:
PMC3190826
AbstractArticlePDF–5.7M
20.
Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium
Pascale Gaudet, Michael S. Livstone, Suzanna E. Lewis, Paul D. Thomas
Brief Bioinform. 2011 Sep; 12(5): 449–462. Published online 2011 Aug 27. doi: 10.1093/bib/bbr042
PMCID:
PMC3178059
AbstractArticlePDF–1.0M

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