A citation-based method for searching scientific literature

Jean-François Couture, Raymond C Trievel. Curr Opin Struct Biol 2006
Times Cited: 65







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



Times Cited
  Times     Co-cited
Similarity



The language of covalent histone modifications.
B D Strahl, C D Allis. Nature 2000
23

Translating the histone code.
T Jenuwein, C D Allis. Science 2001
21

The SET-domain protein superfamily: protein lysine methyltransferases.
Shane C Dillon, Xing Zhang, Raymond C Trievel, Xiaodong Cheng. Genome Biol 2005
499
21

Crystal structure of the nucleosome core particle at 2.8 A resolution.
K Luger, A W Mäder, R K Richmond, D F Sargent, T J Richmond. Nature 1997
20

Structure and catalytic mechanism of the human histone methyltransferase SET7/9.
Bing Xiao, Chun Jing, Jonathan R Wilson, Philip A Walker, Nishi Vasisht, Geoff Kelly, Steven Howell, Ian A Taylor, G Michael Blackburn, Steven J Gamblin. Nature 2003
285
20


Regulation of chromatin structure by site-specific histone H3 methyltransferases.
S Rea, F Eisenhaber, D O'Carroll, B D Strahl, Z W Sun, M Schmid, S Opravil, K Mechtler, C P Ponting, C D Allis,[...]. Nature 2000
18

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers.
Sean D Taverna, Haitao Li, Alexander J Ruthenburg, C David Allis, Dinshaw J Patel. Nat Struct Mol Biol 2007
16

High-resolution profiling of histone methylations in the human genome.
Artem Barski, Suresh Cuddapah, Kairong Cui, Tae-Young Roh, Dustin E Schones, Zhibin Wang, Gang Wei, Iouri Chepelev, Keji Zhao. Cell 2007
16

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase.
Jean-François Couture, Evys Collazo, Joseph S Brunzelle, Raymond C Trievel. Genes Dev 2005
183
15

Regulation of p53 activity through lysine methylation.
Sergei Chuikov, Julia K Kurash, Jonathan R Wilson, Bing Xiao, Neil Justin, Gleb S Ivanov, Kristine McKinney, Paul Tempst, Carol Prives, Steven J Gamblin,[...]. Nature 2004
587
15

Structural basis for the methylation site specificity of SET7/9.
Jean-François Couture, Evys Collazo, Glenn Hauk, Raymond C Trievel. Nat Struct Mol Biol 2006
136
15

Structural basis for the product specificity of histone lysine methyltransferases.
Xing Zhang, Zhe Yang, Seema I Khan, John R Horton, Hisashi Tamaru, Eric U Selker, Xiaodong Cheng. Mol Cell 2003
253
15

SET domains and histone methylation.
Bing Xiao, Jonathan R Wilson, Steven J Gamblin. Curr Opin Struct Biol 2003
123
15


Gene-specific modulation of TAF10 function by SET9-mediated methylation.
Antigone Kouskouti, Elisabeth Scheer, Adrien Staub, Làszlò Tora, Iannis Talianidis. Mol Cell 2004
202
13

Specificity and mechanism of the histone methyltransferase Pr-Set7.
Bing Xiao, Chun Jing, Geoff Kelly, Philip A Walker, Frederick W Muskett, Thomas A Frenkiel, Stephen R Martin, Kavitha Sarma, Danny Reinberg, Steven J Gamblin,[...]. Genes Dev 2005
150
13

The diverse functions of histone lysine methylation.
Cyrus Martin, Yi Zhang. Nat Rev Mol Cell Biol 2005
12

Crystal structure and functional analysis of the histone methyltransferase SET7/9.
Jonathan R Wilson, Chun Jing, Philip A Walker, Stephen R Martin, Steven A Howell, G Michael Blackburn, Steven J Gamblin, Bing Xiao. Cell 2002
169
12

Histone demethylation mediated by the nuclear amine oxidase homolog LSD1.
Yujiang Shi, Fei Lan, Caitlin Matson, Peter Mulligan, Johnathan R Whetstine, Philip A Cole, Robert A Casero, Yang Shi. Cell 2004
12

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT.
Raymond C Trievel, E Megan Flynn, Robert L Houtz, James H Hurley. Nat Struct Biol 2003
94
9

Structure and catalytic mechanism of a SET domain protein methyltransferase.
Raymond C Trievel, Bridgette M Beach, Lynnette M A Dirk, Robert L Houtz, James H Hurley. Cell 2002
199
9

A bivalent chromatin structure marks key developmental genes in embryonic stem cells.
Bradley E Bernstein, Tarjei S Mikkelsen, Xiaohui Xie, Michael Kamal, Dana J Huebert, James Cuff, Ben Fry, Alex Meissner, Marius Wernig, Kathrin Plath,[...]. Cell 2006
9


Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.
Xing Zhang, Hisashi Tamaru, Seema I Khan, John R Horton, Lisa J Keefe, Eric U Selker, Xiaodong Cheng. Cell 2002
206
9

Histone demethylation by a family of JmjC domain-containing proteins.
Yu-ichi Tsukada, Jia Fang, Hediye Erdjument-Bromage, Maria E Warren, Christoph H Borchers, Paul Tempst, Yi Zhang. Nature 2006
9

Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks.
Stacey M Southall, Poon-Sheng Wong, Zain Odho, S Mark Roe, Jon R Wilson. Mol Cell 2009
162
9

Repression of p53 activity by Smyd2-mediated methylation.
Jing Huang, Laura Perez-Burgos, Brandon J Placek, Roopsha Sengupta, Mario Richter, Jean A Dorsey, Stefan Kubicek, Susanne Opravil, Thomas Jenuwein, Shelley L Berger. Nature 2006
451
7

Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.
Kenichi Nishioka, Sergei Chuikov, Kavitha Sarma, Hediye Erdjument-Bromage, C David Allis, Paul Tempst, Danny Reinberg. Genes Dev 2002
420
7

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.
M Lachner, D O'Carroll, S Rea, K Mechtler, T Jenuwein. Nature 2001
7

Histone H3 lysine 4 methylation patterns in higher eukaryotic genes.
Robert Schneider, Andrew J Bannister, Fiona A Myers, Alan W Thorne, Colyn Crane-Robinson, Tony Kouzarides. Nat Cell Biol 2004
590
7

Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9.
Makoto Tachibana, Jun Ueda, Mikiko Fukuda, Naoki Takeda, Tsutomu Ohta, Hiroko Iwanari, Toshiko Sakihama, Tatsuhiko Kodama, Takao Hamakubo, Yoichi Shinkai. Genes Dev 2005
569
7

Covalent modifications of histones during development and disease pathogenesis.
Sukesh R Bhaumik, Edwin Smith, Ali Shilatifard. Nat Struct Mol Biol 2007
472
7

Structural insights into histone demethylation by JMJD2 family members.
Zhongzhou Chen, Jianye Zang, Johnathan Whetstine, Xia Hong, Foteini Davrazou, Tatiana G Kutateladze, Michael Simpson, Qilong Mao, Cheol-Ho Pan, Shaodong Dai,[...]. Cell 2006
280
7

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Stanley S Ng, Kathryn L Kavanagh, Michael A McDonough, Danica Butler, Ewa S Pilka, Benoit M R Lienard, James E Bray, Pavel Savitsky, Opher Gileadi, Frank von Delft,[...]. Nature 2007
240
7

Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.
Jean-François Couture, Evys Collazo, Patricia A Ortiz-Tello, Joseph S Brunzelle, Raymond C Trievel. Nat Struct Mol Biol 2007
205
7

Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase.
Chengmin Qian, Xueqi Wang, Karishma Manzur, Sachchidanand, Amjad Farooq, Lei Zeng, Rong Wang, Ming-Ming Zhou. J Mol Biol 2006
49
10


The mammalian epigenome.
Bradley E Bernstein, Alexander Meissner, Eric S Lander. Cell 2007
7


Histones and histone modifications.
Craig L Peterson, Marc-André Laniel. Curr Biol 2004
833
7

[20] Processing of X-ray diffraction data collected in oscillation mode.
Zbyszek Otwinowski, Wladek Minor. Methods Enzymol 1997
7

Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase.
Krithika Subramanian, Da Jia, Priya Kapoor-Vazirani, Doris R Powell, Robert E Collins, Dipali Sharma, Junmin Peng, Xiaodong Cheng, Paula M Vertino. Mol Cell 2008
218
7

Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases.
Johnathan R Whetstine, Amanda Nottke, Fei Lan, Maite Huarte, Sarit Smolikov, Zhongzhou Chen, Eric Spooner, En Li, Gongyi Zhang, Monica Colaiacovo,[...]. Cell 2006
737
7


Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.
H Wang, R Cao, L Xia, H Erdjument-Bromage, C Borchers, P Tempst, Y Zhang. Mol Cell 2001
409
6



Dynamic regulation of histone lysine methylation by demethylases.
Yang Shi, Johnathan R Whetstine. Mol Cell 2007
484
6


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.