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List of co-cited articles
730 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
629
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
537
40

Specification of SUMO1- and SUMO2-interacting motifs.
Christina-Maria Hecker, Matthias Rabiller, Kaisa Haglund, Peter Bayer, Ivan Dikic. J Biol Chem 2006
401
32

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
457
30

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
626
30

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
30


Function and regulation of SUMO proteases.
Christopher M Hickey, Nicole R Wilson, Mark Hochstrasser. Nat Rev Mol Cell Biol 2012
407
26

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.
Jaclyn R Gareau, Christopher D Lima. Nat Rev Mol Cell Biol 2010
808
26

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
273
26

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
227
25

Sumoylation: a regulatory protein modification in health and disease.
Annette Flotho, Frauke Melchior. Annu Rev Biochem 2013
715
25

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
234
23

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
23

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
218
23

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
111
23


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
129
19

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
376
19


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
18

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
18



The fast-growing business of SUMO chains.
Helle D Ulrich. Mol Cell 2008
124
15

Comparative proteomic analysis identifies a role for SUMO in protein quality control.
Michael H Tatham, Ivan Matic, Matthias Mann, Ronald T Hay. Sci Signal 2011
138
15

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
15

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
134
15

A SIM-ultaneous role for SUMO and ubiquitin.
J Jefferson P Perry, John A Tainer, Michael N Boddy. Trends Biochem Sci 2008
177
15

Insights into high affinity small ubiquitin-like modifier (SUMO) recognition by SUMO-interacting motifs (SIMs) revealed by a combination of NMR and peptide array analysis.
Andrew T Namanja, Yi-Jia Li, Yang Su, Steven Wong, Jingjun Lu, Loren T Colson, Chenggang Wu, Shawn S C Li, Yuan Chen. J Biol Chem 2012
53
20

Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
Kirstin Keusekotten, Veronika N Bade, Katrin Meyer-Teschendorf, Annie Miriam Sriramachandran, Katrin Fischer-Schrader, Anke Krause, Christiane Horst, Günter Schwarz, Kay Hofmann, R Jürgen Dohmen,[...]. Biochem J 2014
30
36

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
321
15

An acetylation switch regulates SUMO-dependent protein interaction networks.
Rebecca Ullmann, Christopher D Chien, Maria Laura Avantaggiati, Stefan Muller. Mol Cell 2012
68
14

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
14

Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae.
J Thomas Hannich, Alaron Lewis, Mary B Kroetz, Shyr-Jiann Li, Heinrich Heide, Andrew Emili, Mark Hochstrasser. J Biol Chem 2005
320
14

Regulation of DNA damage responses by ubiquitin and SUMO.
Stephen P Jackson, Daniel Durocher. Mol Cell 2013
438
14

SUMO: a history of modification.
Ronald T Hay. Mol Cell 2005
14

Protein modification by SUMO.
Erica S Johnson. Annu Rev Biochem 2004
14


Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
Victor Bernier-Villamor, Deborah A Sampson, Michael J Matunis, Christopher D Lima. Cell 2002
443
14

Sumoylation of MDC1 is important for proper DNA damage response.
Kuntian Luo, Haoxing Zhang, Liewei Wang, Jian Yuan, Zhenkun Lou. EMBO J 2012
119
14

Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML.
Stefan R Weisshaar, Kirstin Keusekotten, Anke Krause, Christiane Horst, Helen M Springer, Kerstin Göttsche, R Jürgen Dohmen, Gerrit J K Praefcke. FEBS Lett 2008
85
14

SUMO-targeted ubiquitin ligases.
Annie M Sriramachandran, R Jürgen Dohmen. Biochim Biophys Acta 2014
177
14

A comprehensive compilation of SUMO proteomics.
Ivo A Hendriks, Alfred C O Vertegaal. Nat Rev Mol Cell Biol 2016
272
14

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
183
12


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
324
12

The mechanisms of PML-nuclear body formation.
Tian Huai Shen, Hui-Kuan Lin, Pier Paolo Scaglioni, Thomas M Yung, Pier Paolo Pandolfi. Mol Cell 2006
383
12

The ubiquitin code.
David Komander, Michael Rape. Annu Rev Biochem 2012
12

Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7.
Daizo Koinuma, Masahiko Shinozaki, Akiyoshi Komuro, Kouichiro Goto, Masao Saitoh, Aki Hanyu, Masahito Ebina, Toshihiro Nukiwa, Keiji Miyazawa, Takeshi Imamura,[...]. EMBO J 2003
174
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.