A citation-based method for searching scientific literature


List of co-cited articles
1165 articles co-cited >1



Times Cited
  Times     Co-cited
Similarity


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
638
58

SUMO-targeted ubiquitin ligases in genome stability.
John Prudden, Stephanie Pebernard, Grazia Raffa, Daniela A Slavin, J Jefferson P Perry, John A Tainer, Clare H McGowan, Michael N Boddy. EMBO J 2007
274
53

Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway.
Valérie Lallemand-Breitenbach, Marion Jeanne, Shirine Benhenda, Rihab Nasr, Ming Lei, Laurent Peres, Jun Zhou, Jun Zhu, Brian Raught, Hugues de Thé. Nat Cell Biol 2008
542
40

RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair.
Yaron Galanty, Rimma Belotserkovskaya, Julia Coates, Stephen P Jackson. Genes Dev 2012
235
36

SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage.
Yili Yin, Anne Seifert, Joy Shijia Chua, Jean-François Maure, Filip Golebiowski, Ronald T Hay. Genes Dev 2012
182
36

Ubiquitin-dependent proteolytic control of SUMO conjugates.
Kristina Uzunova, Kerstin Göttsche, Maria Miteva, Stefan R Weisshaar, Christoph Glanemann, Marion Schnellhardt, Michaela Niessen, Hartmut Scheel, Kay Hofmann, Erica S Johnson,[...]. J Biol Chem 2007
247
35


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
631
32

The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation.
Yang Xie, Oliver Kerscher, Mary B Kroetz, Heather F McConchie, Patrick Sung, Mark Hochstrasser. J Biol Chem 2007
184
28

RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.
Catherine M Guzzo, Christopher E Berndsen, Jianmei Zhu, Vibhor Gupta, Ajit Datta, Roger A Greenberg, Cynthia Wolberger, Michael J Matunis. Sci Signal 2012
135
25

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.
Jing Song, Linda K Durrin, Thomas A Wilkinson, Theodore G Krontiris, Yuan Chen. Proc Natl Acad Sci U S A 2004
459
25

Sumoylation: a regulatory protein modification in health and disease.
Annette Flotho, Frauke Melchior. Annu Rev Biochem 2013
728
24

Sumoylation of MDC1 is important for proper DNA damage response.
Kuntian Luo, Haoxing Zhang, Liewei Wang, Jian Yuan, Zhenkun Lou. EMBO J 2012
120
23

Modification in reverse: the SUMO proteases.
Debaditya Mukhopadhyay, Mary Dasso. Trends Biochem Sci 2007
433
22

SUMO-targeted ubiquitin ligases.
Annie M Sriramachandran, R Jürgen Dohmen. Biochim Biophys Acta 2014
178
22

Function and regulation of SUMO proteases.
Christopher M Hickey, Nicole R Wilson, Mark Hochstrasser. Nat Rev Mol Cell Biol 2012
415
21

Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks.
Yaron Galanty, Rimma Belotserkovskaya, Julia Coates, Sophie Polo, Kyle M Miller, Stephen P Jackson. Nature 2009
404
21

RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response.
Sara L Poulsen, Rebecca K Hansen, Sebastian A Wagner, Loes van Cuijk, Gijsbert J van Belle, Werner Streicher, Mats Wikström, Chunaram Choudhary, Adriaan B Houtsmuller, Jurgen A Marteijn,[...]. J Cell Biol 2013
112
21

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
Ivan Matic, Joost Schimmel, Ivo A Hendriks, Maria A van Santen, Frans van de Rijke, Hans van Dam, Florian Gnad, Matthias Mann, Alfred C O Vertegaal. Mol Cell 2010
229
20

RNF4 is required for DNA double-strand break repair in vivo.
R Vyas, R Kumar, F Clermont, A Helfricht, P Kalev, P Sotiropoulou, I A Hendriks, E Radaelli, T Hochepied, C Blanpain,[...]. Cell Death Differ 2013
84
23

Protein modification by SUMO.
Erica S Johnson. Annu Rev Biochem 2004
20

System-wide changes to SUMO modifications in response to heat shock.
Filip Golebiowski, Ivan Matic, Michael H Tatham, Christian Cole, Yili Yin, Akihiro Nakamura, Jürgen Cox, Geoffrey J Barton, Matthias Mann, Ronald T Hay. Sci Signal 2009
377
20

Specification of SUMO1- and SUMO2-interacting motifs.
Christina-Maria Hecker, Matthias Rabiller, Kaisa Haglund, Peter Bayer, Ivan Dikic. J Biol Chem 2006
401
20

A SIM-ultaneous role for SUMO and ubiquitin.
J Jefferson P Perry, John A Tainer, Michael N Boddy. Trends Biochem Sci 2008
177
19



The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress.
Joanna R Morris, Chris Boutell, Melanie Keppler, Ruth Densham, Daniel Weekes, Amin Alamshah, Laura Butler, Yaron Galanty, Laurent Pangon, Tai Kiuchi,[...]. Nature 2009
323
18

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.
Jaclyn R Gareau, Christopher D Lima. Nat Rev Mol Cell Biol 2010
822
18

Purification and identification of endogenous polySUMO conjugates.
Roland Bruderer, Michael H Tatham, Anna Plechanovova, Ivan Matic, Amit K Garg, Ronald T Hay. EMBO Rep 2011
130
16

Regulation of DNA damage responses by ubiquitin and SUMO.
Stephen P Jackson, Daniel Durocher. Mol Cell 2013
439
16


Fission yeast Rnf4 homologs are required for DNA repair.
Ana Kosoy, Teresa M Calonge, Emily A Outwin, Matthew J O'Connell. J Biol Chem 2007
60
26

Concepts in sumoylation: a decade on.
Ruth Geiss-Friedlander, Frauke Melchior. Nat Rev Mol Cell Biol 2007
16

SUMO: a history of modification.
Ronald T Hay. Mol Cell 2005
16

Uncovering global SUMOylation signaling networks in a site-specific manner.
Ivo A Hendriks, Rochelle C J D'Souza, Bing Yang, Matty Verlaan-de Vries, Matthias Mann, Alfred C O Vertegaal. Nat Struct Mol Biol 2014
328
16

SUMO chain-induced dimerization activates RNF4.
Alejandro Rojas-Fernandez, Anna Plechanovová, Neil Hattersley, Ellis Jaffray, Michael H Tatham, Ronald T Hay. Mol Cell 2014
55
29

The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle.
Joost Schimmel, Katja M Larsen, Ivan Matic, Martijn van Hagen, Jürgen Cox, Matthias Mann, Jens S Andersen, Alfred C O Vertegaal. Mol Cell Proteomics 2008
121
15

In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy.
Ivan Matic, Martijn van Hagen, Joost Schimmel, Boris Macek, Stephen C Ogg, Michael H Tatham, Ronald T Hay, Angus I Lamond, Matthias Mann, Alfred C O Vertegaal. Mol Cell Proteomics 2008
220
15

The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice.
Karim Nacerddine, François Lehembre, Mantu Bhaumik, Jérôme Artus, Michel Cohen-Tannoudji, Charles Babinet, Pier Paolo Pandolfi, Anne Dejean. Dev Cell 2005
407
15

The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast.
Gwendolyn R Bylebyl, Irina Belichenko, Erica S Johnson. J Biol Chem 2003
194
14



Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex.
Hong Dou, Chao Huang, Melissa Singh, Phillip B Carpenter, Edward T H Yeh. Mol Cell 2010
146
14


Mechanism of ubiquitylation by dimeric RING ligase RNF4.
Anna Plechanovová, Ellis G Jaffray, Stephen A McMahon, Kenneth A Johnson, Iva Navrátilová, James H Naismith, Ronald T Hay. Nat Struct Mol Biol 2011
126
13

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.
Carsten Hoege, Boris Pfander, George-Lucian Moldovan, George Pyrowolakis, Stefan Jentsch. Nature 2002
13

Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation.
Yigit Erker, Helene Neyret-Kahn, Jacob S Seeler, Anne Dejean, Azeddine Atfi, Laurence Levy. Mol Cell Biol 2013
68
19


Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint.
Catherine A Cremona, Prabha Sarangi, Yan Yang, Lisa E Hang, Sadia Rahman, Xiaolan Zhao. Mol Cell 2012
150
13



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.