A citation-based method for searching scientific literature

Hae Ryung Chang, Anudari Munkhjargal, Myung-Jin Kim, Seon Young Park, Eunyoung Jung, Jae-Ha Ryu, Young Yang, Jong-Seok Lim, Yonghwan Kim. Mutat Res 2018
Times Cited: 33







List of co-cited articles
377 articles co-cited >1



Times Cited
  Times     Co-cited
Similarity


PML nuclear bodies.
Valérie Lallemand-Breitenbach, Hugues de Thé. Cold Spring Harb Perspect Biol 2010
356
33

A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.
Ellen Van Damme, Kris Laukens, Thanh Hai Dang, Xaveer Van Ostade. Int J Biol Sci 2010
127
30

Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies.
Rosa Bernardi, Pier Paolo Pandolfi. Nat Rev Mol Cell Biol 2007
635
30

PML nuclear bodies: from architecture to function.
Valérie Lallemand-Breitenbach, Hugues de Thé. Curr Opin Cell Biol 2018
71
27

Differential Roles of PML Isoforms.
Sébastien Nisole, Mohamed Ali Maroui, Xavier H Mascle, Muriel Aubry, Mounira K Chelbi-Alix. Front Oncol 2013
96
24

Compositional Control of Phase-Separated Cellular Bodies.
Salman F Banani, Allyson M Rice, William B Peeples, Yuan Lin, Saumya Jain, Roy Parker, Michael K Rosen. Cell 2016
394
24


Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins.
Umut Sahin, Omar Ferhi, Marion Jeanne, Shirine Benhenda, Caroline Berthier, Florence Jollivet, Michiko Niwa-Kawakita, Orestis Faklaris, Niclas Setterblad, Hugues de Thé,[...]. J Cell Biol 2014
115
21

PML protein isoforms and the RBCC/TRIM motif.
K Jensen, C Shiels, P S Freemont. Oncogene 2001
350
21

PML: Regulation and multifaceted function beyond tumor suppression.
Kuo-Sheng Hsu, Hung-Ying Kao. Cell Biosci 2018
38
21

The role of PML in tumor suppression.
Paolo Salomoni, Pier Paolo Pandolfi. Cell 2002
424
18

Biomolecular condensates: organizers of cellular biochemistry.
Salman F Banani, Hyun O Lee, Anthony A Hyman, Michael K Rosen. Nat Rev Mol Cell Biol 2017
18

Characterization of endogenous human promyelocytic leukemia isoforms.
Wilfried Condemine, Yuki Takahashi, Jun Zhu, Francine Puvion-Dutilleul, Sarah Guegan, Anne Janin, Hugues de Thé. Cancer Res 2006
114
18

C-terminal motifs in promyelocytic leukemia protein isoforms critically regulate PML nuclear body formation.
Chuang Li, Qiongfang Peng, Xiao Wan, Haili Sun, Jun Tang. J Cell Sci 2017
22
27

Dynamics of component exchange at PML nuclear bodies.
Stefanie Weidtkamp-Peters, Thorsten Lenser, Dmitri Negorev, Norman Gerstner, Thomas G Hofmann, Georg Schwanitz, Christian Hoischen, Gerd Maul, Peter Dittrich, Peter Hemmerich. J Cell Sci 2008
127
18

PML nuclear bodies: dynamic sensors of DNA damage and cellular stress.
Graham Dellaire, David P Bazett-Jones. Bioessays 2004
305
18

Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres.
Peter W Lewis, Simon J Elsaesser, Kyung-Min Noh, Sonja C Stadler, C David Allis. Proc Natl Acad Sci U S A 2010
491
18

PML and PML nuclear bodies: implications in antiviral defence.
Roger D Everett, Mounira K Chelbi-Alix. Biochimie 2007
325
18

PML nuclear body disruption impairs DNA double-strand break sensing and repair in APL.
A di Masi, D Cilli, F Berardinelli, A Talarico, I Pallavicini, R Pennisi, S Leone, A Antoccia, N I Noguera, F Lo-Coco,[...]. Cell Death Dis 2016
23
26

PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation.
Umut Sahin, Hugues de Thé, Valérie Lallemand-Breitenbach. Nucleus 2014
60
18

PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1.
A M Ishov, A G Sotnikov, D Negorev, O V Vladimirova, N Neff, T Kamitani, E T Yeh, J F Strauss, G G Maul. J Cell Biol 1999
642
18

Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR.
Graham Dellaire, Reagan W Ching, Kashif Ahmed, Farid Jalali, Kenneth C K Tse, Robert G Bristow, David P Bazett-Jones. J Cell Biol 2006
121
15

A role for PML and the nuclear body in genomic stability.
S Zhong, P Hu, T Z Ye, R Stan, N A Ellis, P P Pandolfi. Oncogene 1999
170
15

PML nuclear bodies are highly organised DNA-protein structures with a function in heterochromatin remodelling at the G2 phase.
Judith J Luciani, Danielle Depetris, Yves Usson, Catherine Metzler-Guillemain, Cecile Mignon-Ravix, Micheal J Mitchell, Andre Megarbane, Pierre Sarda, Huseyin Sirma, Anne Moncla,[...]. J Cell Sci 2006
96
15

Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1.
Graham Dellaire, Christopher H Eskiw, Hesam Dehghani, Reagan W Ching, David P Bazett-Jones. J Cell Sci 2006
73
15

Loss of the tumor suppressor PML in human cancers of multiple histologic origins.
Carmela Gurrieri, Paola Capodieci, Rosa Bernardi, Pier Paolo Scaglioni, Khedoudja Nafa, Laura J Rush, David A Verbel, Carlos Cordon-Cardo, Pier Paolo Pandolfi. J Natl Cancer Inst 2004
253
15

Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body.
T R Yeager, A A Neumann, A Englezou, L I Huschtscha, J R Noble, R R Reddel. Cancer Res 1999
497
15

Functional connection between Rad51 and PML in homology-directed repair.
Sergei Boichuk, Liang Hu, Kathleen Makielski, Pier Paolo Pandolfi, Ole V Gjoerup. PLoS One 2011
34
15

HSV-1 genome subnuclear positioning and associations with host-cell PML-NBs and centromeres regulate LAT locus transcription during latency in neurons.
Frédéric Catez, Christel Picard, Kathrin Held, Sylvain Gross, Antoine Rousseau, Diethilde Theil, Nancy Sawtell, Marc Labetoulle, Patrick Lomonte. PLoS Pathog 2012
49
15

PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX/DAXX.
Erwan Delbarre, Kristina Ivanauskiene, Jane Spirkoski, Akshay Shah, Kristin Vekterud, Jan Øivind Moskaug, Stig Ove Bøe, Lee H Wong, Thomas Küntziger, Philippe Collas. Genome Res 2017
28
17

Regulation of p53 activity in nuclear bodies by a specific PML isoform.
V Fogal, M Gostissa, P Sandy, P Zacchi, T Sternsdorf, K Jensen, P P Pandolfi, H Will, C Schneider, G Del Sal. EMBO J 2000
315
15

Cell cycle regulation of PML modification and ND10 composition.
R D Everett, P Lomonte, T Sternsdorf, R van Driel, A Orr. J Cell Sci 1999
145
15

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.
Michael H Tatham, Marie-Claude Geoffroy, Linnan Shen, Anna Plechanovova, Neil Hattersley, Ellis G Jaffray, Jorma J Palvimo, Ronald T Hay. Nat Cell Biol 2008
596
15

Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.
Ding-Yen Lin, Yen-Sung Huang, Jen-Chong Jeng, Hong-Yi Kuo, Che-Chang Chang, Ting-Ting Chao, Chun-Chen Ho, Yun-Ching Chen, Tong-Ping Lin, Hsin-I Fang,[...]. Mol Cell 2006
310
15

RING tetramerization is required for nuclear body biogenesis and PML sumoylation.
Pengran Wang, Shirine Benhenda, Haiyan Wu, Valérie Lallemand-Breitenbach, Tao Zhen, Florence Jollivet, Laurent Peres, Yuwen Li, Sai-Juan Chen, Zhu Chen,[...]. Nat Commun 2018
32
15

The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies.
Hugues de Thé, Morgane Le Bras, Valérie Lallemand-Breitenbach. J Cell Biol 2012
141
15

The nucleolus.
Thoru Pederson. Cold Spring Harb Perspect Biol 2011
206
12

Role of SUMO-1-modified PML in nuclear body formation.
S Zhong, S Müller, S Ronchetti, P S Freemont, A Dejean, P P Pandolfi. Blood 2000
420
12


PML induces compaction, TRF2 depletion and DNA damage signaling at telomeres and promotes their alternative lengthening.
Sarah Osterwald, Katharina I Deeg, Inn Chung, Daniel Parisotto, Stefan Wörz, Karl Rohr, Holger Erfle, Karsten Rippe. J Cell Sci 2015
49
12

New insights into the role of the subnuclear structure ND10 for viral infection.
Nina Tavalai, Thomas Stamminger. Biochim Biophys Acta 2008
132
12

The transcriptional role of PML and the nuclear body.
S Zhong, P Salomoni, P P Pandolfi. Nat Cell Biol 2000
464
12

The number of PML nuclear bodies increases in early S phase by a fission mechanism.
Graham Dellaire, Reagan W Ching, Hesam Dehghani, Ying Ren, David P Bazett-Jones. J Cell Sci 2006
74
12


Role of PML in cell growth and the retinoic acid pathway.
Z G Wang, L Delva, M Gaboli, R Rivi, M Giorgio, C Cordon-Cardo, F Grosveld, P P Pandolfi. Science 1998
428
12

PML is required for telomere stability in non-neoplastic human cells.
M Marchesini, R Matocci, L Tasselli, V Cambiaghi, A Orleth, L Furia, C Marinelli, S Lombardi, G Sammarelli, F Aversa,[...]. Oncogene 2016
18
22


Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.
M H Tatham, E Jaffray, O A Vaughan, J M Desterro, C H Botting, J H Naismith, R T Hay. J Biol Chem 2001
597
12

Live cell dynamics of promyelocytic leukemia nuclear bodies upon entry into and exit from mitosis.
Yi-Chun M Chen, Constantin Kappel, Joel Beaudouin, Roland Eils, David L Spector. Mol Biol Cell 2008
39
12

Three-dimensional organization of promyelocytic leukemia nuclear bodies.
Marion Lang, Thibaud Jegou, Inn Chung, Karsten Richter, Sandra Münch, Anikó Udvarhelyi, Christoph Cremer, Peter Hemmerich, Johann Engelhardt, Stefan W Hell,[...]. J Cell Sci 2010
74
12


Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.