A citation-based method for searching scientific literature

Kristina Uzunova, Kerstin Göttsche, Maria Miteva, Stefan R Weisshaar, Christoph Glanemann, Marion Schnellhardt, Michaela Niessen, Hartmut Scheel, Kay Hofmann, Erica S Johnson, Gerrit J K Praefcke, R Jürgen Dohmen. J Biol Chem 2007
Times Cited: 247







List of co-cited articles
1281 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
43

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
41

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
37

SUMO-targeted ubiquitin ligases.
Annie M Sriramachandran, R Jürgen Dohmen. Biochim Biophys Acta 2014
178
34



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
26

Function and regulation of SUMO proteases.
Christopher M Hickey, Nicole R Wilson, Mark Hochstrasser. Nat Rev Mol Cell Biol 2012
415
25

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
25

Sumoylation: a regulatory protein modification in health and disease.
Annette Flotho, Frauke Melchior. Annu Rev Biochem 2013
728
25

Protein modification by SUMO.
Erica S Johnson. Annu Rev Biochem 2004
24

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
23

A SIM-ultaneous role for SUMO and ubiquitin.
J Jefferson P Perry, John A Tainer, Michael N Boddy. Trends Biochem Sci 2008
177
23

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
23

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
21


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
20

The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast.
Gwendolyn R Bylebyl, Irina Belichenko, Erica S Johnson. J Biol Chem 2003
194
20



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
321
18

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
18


SUMO playing tag with ubiquitin.
Gerrit J K Praefcke, Kay Hofmann, R Jürgen Dohmen. Trends Biochem Sci 2012
123
17

SUMO: a history of modification.
Ronald T Hay. Mol Cell 2005
17

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
16

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
16



Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae.
Chaoying Zhang, Tania M Roberts, Jay Yang, Ridhdhi Desai, Grant W Brown. DNA Repair (Amst) 2006
81
19

An additional role for SUMO in ubiquitin-mediated proteolysis.
Marie-Claude Geoffroy, Ronald T Hay. Nat Rev Mol Cell Biol 2009
202
16

SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation.
J M Desterro, M S Rodriguez, R T Hay. Mol Cell 1998
879
16

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.
Jaclyn R Gareau, Christopher D Lima. Nat Rev Mol Cell Biol 2010
822
16

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
15

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
22


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
15


Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase.
Shigeki Nagai, Karine Dubrana, Monika Tsai-Pflugfelder, Marta B Davidson, Tania M Roberts, Grant W Brown, Elisa Varela, Florence Hediger, Susan M Gasser, Nevan J Krogan. Science 2008
327
14

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
14

Modification in reverse: the SUMO proteases.
Debaditya Mukhopadhyay, Mary Dasso. Trends Biochem Sci 2007
433
14

The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination.
Rebecca C Burgess, Sadia Rahman, Michael Lisby, Rodney Rothstein, Xiaolan Zhao. Mol Cell Biol 2007
118
14

Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae.
Zheng Wang, Grace Marie Jones, Gregory Prelich. Genetics 2006
65
20


Global analysis of SUMO chain function reveals multiple roles in chromatin regulation.
Tharan Srikumar, Megan C Lewicki, Michael Costanzo, Johnny M Tkach, Harm van Bakel, Kyle Tsui, Erica S Johnson, Grant W Brown, Brenda J Andrews, Charles Boone,[...]. J Cell Biol 2013
47
27

Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions.
Minghua Nie, Aaron Aslanian, John Prudden, Johanna Heideker, Ajay A Vashisht, James A Wohlschlegel, John R Yates, Michael N Boddy. J Biol Chem 2012
66
19

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
15

Concepts in sumoylation: a decade on.
Ruth Geiss-Friedlander, Frauke Melchior. Nat Rev Mol Cell Biol 2007
13


Proteome-wide identification of SUMO2 modification sites.
Triin Tammsalu, Ivan Matic, Ellis G Jaffray, Adel F M Ibrahim, Michael H Tatham, Ronald T Hay. Sci Signal 2014
147
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.