Table of contents
April 2007, Volume 14 No 4 pp251-351
About the coverEditorial
Some more equal than others - p251
doi:10.1038/nsmb0407-251
Abstract - Some more equal than others | Full Text - Some more equal than others | PDF (77 KB) - Some more equal than others
News and Views
The expanding world of histone lysine demethylases - pp252 - 254
Eric Metzger & Roland Schüle
doi:10.1038/nsmb0407-252
Full Text - The expanding world of histone lysine demethylases | PDF (246 KB) - The expanding world of histone lysine demethylases
See also: Brief Communication by Lee et al. | Brief Communication by Eissenberg et al.
How HIV-1 hijacks ALIX - pp254 - 256
Heinrich G Göttlinger
doi:10.1038/nsmb0407-254
Full Text - How HIV-1 hijacks ALIX | PDF (303 KB) - How HIV-1 hijacks ALIX
Under DNA stress, gyrase makes the sign of the cross - pp256 - 258
N Patrick Higgins
doi:10.1038/nsmb0407-256
Full Text - Under DNA stress, gyrase makes the sign of the cross | PDF (307 KB) - Under DNA stress, gyrase makes the sign of the cross
See also: Article by Nöllmann et al.
A marked end - pp259 - 260
Xuemei Chen
doi:10.1038/nsmb0407-259
Full Text - A marked end | PDF (308 KB) - A marked end
See also: Brief Communication by Kirino & Mourelatos | Brief Communication by Ohara et al.
La sets the tone for telomerase assembly - pp261 - 262
M Teresa Teixeira & Eric Gilson
doi:10.1038/nsmb0407-261
Full Text - La sets the tone for telomerase assembly | PDF (284 KB) - La sets the tone for telomerase assembly
Research highlights - p263
doi:10.1038/nsmb0407-263
Full Text - Research highlights | PDF (71 KB) - Research highlights
Articles
Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque - pp264 - 271
Marcelo Nöllmann, Michael D Stone, Zev Bryant, Jeff Gore, Nancy J Crisona, Seok-Cheol Hong, Sylvain Mitelheiser, Anthony Maxwell, Carlos Bustamante & Nicholas R Cozzarelli
doi:10.1038/nsmb1213
Abstract - Multiple modes of : Escherichia coli: DNA gyrase activity revealed by force and torque | Full Text - Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque | PDF (1,899 KB) - Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque | Supplementary information
See also: News and Views by Higgins
Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea - pp272 - 279
Ryuya Fukunaga & Shigeyuki Yokoyama
doi:10.1038/nsmb1219
Abstract - Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea | Full Text - Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea | PDF (1,093 KB) - Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea | Supplementary information
GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop - pp280 - 286
Gustavo Fenalti, Ruby H P Law, Ashley M Buckle, Christopher Langendorf, Kellie Tuck, Carlos J Rosado, Noel G Faux, Khalid Mahmood, Christiane S Hampe, J Paul Banga, Matthew Wilce, Jason Schmidberger, Jamie Rossjohn, Ossama El-Kabbani, Robert N Pike, A Ian Smith, Ian R Mackay, Merrill J Rowley & James C Whisstock
doi:10.1038/nsmb1228
Abstract - GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop | Full Text - GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop | PDF (919 KB) - GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop | Supplementary information
Potent effect of target structure on microRNA function - pp287 - 294
Dang Long, Rosalind Lee, Peter Williams, Chi Yu Chan, Victor Ambros & Ye Ding
doi:10.1038/nsmb1226
Abstract - Potent effect of target structure on microRNA function | Full Text - Potent effect of target structure on microRNA function | PDF (308 KB) - Potent effect of target structure on microRNA function | Supplementary information
Structural basis for autoinhibition of Notch - pp295 - 300
Wendy R Gordon, Didem Vardar-Ulu, Gavin Histen, Cheryll Sanchez-Irizarry, Jon C Aster & Stephen C Blacklow
doi:10.1038/nsmb1227
PDB code
3D view
Abstract - Structural basis for autoinhibition of Notch | Full Text - Structural basis for autoinhibition of Notch | PDF (414 KB) - Structural basis for autoinhibition of Notch | Supplementary information
Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions - pp301 - 307
Albert Ribes-Zamora, Ivana Mihalek, Olivier Lichtarge & Alison A Bertuch
doi:10.1038/nsmb1214
Abstract - Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions | Full Text - Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions | PDF (507 KB) - Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions | Supplementary information
A riboswitch selective for the queuosine precursor preQ1 contains an unusually small aptamer domain - pp308 - 317
Adam Roth, Wade C Winkler, Elizabeth E Regulski, Bobby W K Lee, Jinsoo Lim, Inbal Jona, Jeffrey E Barrick, Ankita Ritwik, Jane N Kim, Rüdiger Welz, Dirk Iwata-Reuyl & Ronald R Breaker
doi:10.1038/nsmb1224
Abstract - A riboswitch selective for the queuosine precursor preQ: 1: contains an unusually small aptamer domain | Full Text - A riboswitch selective for the queuosine precursor preQ1 contains an unusually small aptamer domain | PDF (369 KB) - A riboswitch selective for the queuosine precursor preQ1 contains an unusually small aptamer domain | Supplementary information
Spontaneous reverse movement of mRNA-bound tRNA through the ribosome - pp318 - 324
Andrey L Konevega, Niels Fischer, Yuri P Semenkov, Holger Stark, Wolfgang Wintermeyer & Marina V Rodnina
doi:10.1038/nsmb1221
Abstract - Spontaneous reverse movement of mRNA-bound tRNA through the ribosome | Full Text - Spontaneous reverse movement of mRNA-bound tRNA through the ribosome | PDF (311 KB) - Spontaneous reverse movement of mRNA-bound tRNA through the ribosome
Sequence-specific dynamics modulate recognition specificity in WW domains - pp325 - 331
Tao Peng, John S Zintsmaster, Andrew T Namanja & Jeffrey W Peng
doi:10.1038/nsmb1207
Abstract - Sequence-specific dynamics modulate recognition specificity in WW domains | Full Text - Sequence-specific dynamics modulate recognition specificity in WW domains | PDF (485 KB) - Sequence-specific dynamics modulate recognition specificity in WW domains | Supplementary information
A toxic monomeric conformer of the polyglutamine protein - pp332 - 340
Yoshitaka Nagai, Takashi Inui, H Akiko Popiel, Nobuhiro Fujikake, Kazuhiro Hasegawa, Yoshihiro Urade, Yuji Goto, Hironobu Naiki & Tatsushi Toda
doi:10.1038/nsmb1215
Abstract - A toxic monomeric conformer of the polyglutamine protein | Full Text - A toxic monomeric conformer of the polyglutamine protein | PDF (422 KB) - A toxic monomeric conformer of the polyglutamine protein
Brief Communications
The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase - pp341 - 343
Nara Lee, Junyu Zhang, Robert J Klose, Hediye Erdjument-Bromage, Paul Tempst, Richard S Jones & Yi Zhang
doi:10.1038/nsmb1216
Abstract - The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase | Full Text - The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase | PDF (268 KB) - The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase | Supplementary information
See also: News and Views by Metzger & Schüle
The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase - pp344 - 346
Joel C Eissenberg, Min Gyu Lee, Jessica Schneider, Anne Ilvarsonn, Ramin Shiekhattar & Ali Shilatifard
doi:10.1038/nsmb1217
Abstract - The trithorax-group gene in : Drosophila little imaginal discs: encodes a trimethylated histone H3 Lys4 demethylase | Full Text - The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase | PDF (310 KB) - The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase | Supplementary information
See also: News and Views by Metzger & Schüle
Mouse Piwi-interacting RNAs are 2'-O-methylated at their 3' termini - pp347 - 348
Yohei Kirino & Zissimos Mourelatos
doi:10.1038/nsmb1218
Abstract - Mouse Piwi-interacting RNAs are 2[prime]-O-methylated at their 3[prime] termini | Full Text - Mouse Piwi-interacting RNAs are 2'-O-methylated at their 3' termini | PDF (177 KB) - Mouse Piwi-interacting RNAs are 2'-O-methylated at their 3' termini | Supplementary information
See also: News and Views by Chen
The 3' termini of mouse Piwi-interacting RNAs are 2'-O-methylated - pp349 - 350
Tomoya Ohara, Yuriko Sakaguchi, Takeo Suzuki, Hiroki Ueda, Kenjyo Miyauchi & Tsutomu Suzuki
doi:10.1038/nsmb1220
Abstract - The 3[prime] termini of mouse Piwi-interacting RNAs are 2[prime]-O-methylated | Full Text - The 3' termini of mouse Piwi-interacting RNAs are 2'-O-methylated | PDF (208 KB) - The 3' termini of mouse Piwi-interacting RNAs are 2'-O-methylated | Supplementary information
See also: News and Views by Chen
Errata
Erratum: Histone merry-go-round - p351
doi:10.1038/nsmb0407-351a
Full Text - Erratum: Histone merry-go-round | PDF (62 KB) - Erratum: Histone merry-go-round
Erratum: Structural basis for the control of translation initiation during stress - p351
Antón Vila-Sanjurjo, Barbara-S Schuwirth, Cathy W Hau & Jamie H D Cate
doi:10.1038/nsmb0407-351b
Full Text - Erratum: Structural basis for the control of translation initiation during stress | PDF (62 KB) - Erratum: Structural basis for the control of translation initiation during stress
Erratum: Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase - p351
Gaoyang Liang, Robert J Klose, Kathryn E Gardner & Yi Zhang
doi:10.1038/nsmb0407-351c
Full Text - Erratum: Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase | PDF (62 KB) - Erratum: Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase
