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PDBsum entry 2c1n
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Signaling protein
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PDB id
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2c1n
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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3
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Structure:
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14-3-3 protein zeta/delta. Chain: a, b. Synonym: protein kinasE C inhibitor protein 1, kcip-1. Engineered: yes. Histone h3 acetylphosphopeptide. Chain: c, e. Fragment: 14-3-3, histone h3 acetylphosphopeptide residues 7-14. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.00Å
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R-factor:
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0.258
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R-free:
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0.296
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Authors:
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J.P.I.Welburn,N.Macdonald,M.E.M.Noble,A.Nguyen,M.B.Yaffe,D.Clynes, J.G.Moggs,G.Orphanides,S.Thomson,J.W.Edmunds,A.L.Clayton, J.A.Endicott,L.C.Mahadevan
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Key ref:
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N.Macdonald
et al.
(2005).
Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.
Mol Cell,
20,
199-211.
PubMed id:
DOI:
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Date:
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16-Sep-05
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Release date:
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02-Nov-05
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PROCHECK
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Headers
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References
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P63104
(1433Z_HUMAN) -
14-3-3 protein zeta/delta from Homo sapiens
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Seq:
Struc:
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245 a.a.
225 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Mol Cell
20:199-211
(2005)
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PubMed id:
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Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.
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N.Macdonald,
J.P.Welburn,
M.E.Noble,
A.Nguyen,
M.B.Yaffe,
D.Clynes,
J.G.Moggs,
G.Orphanides,
S.Thomson,
J.W.Edmunds,
A.L.Clayton,
J.A.Endicott,
L.C.Mahadevan.
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ABSTRACT
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Phosphorylation of histone H3 is implicated in transcriptional activation and
chromosome condensation, but its immediate molecular function has remained
obscure. By affinity chromatography of nuclear extracts against modified H3 tail
peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a
strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does
not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3
is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation,
concomitant with H3 phosphoacetylation. We have determined the structures of
14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3
peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and
provide a structural understanding for the lack of effect of acetylation at
lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of
proteins that mediate the effect of histone phosphorylation at inducible genes.
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Selected figure(s)
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Figure 3.
Figure 3. Binding Studies of H3 Tail Peptides to 14-3-3
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Figure 5.
Figure 5. Structure of 14-3-3 Complexed with Histone H3
Peptide Phosphorylated at Serine 10
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
20,
199-211)
copyright 2005.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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Z.Xu,
H.Zan,
E.J.Pone,
T.Mai,
and
P.Casali
(2012).
Immunoglobulin class-switch DNA recombination: induction, targeting and beyond.
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Nat Rev Immunol,
12,
517-531.
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A.J.Bannister,
and
T.Kouzarides
(2011).
Regulation of chromatin by histone modifications.
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Cell Res,
21,
381-395.
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B.Pérez-Cadahía,
B.Drobic,
and
J.R.Davie
(2011).
Activation and function of immediate-early genes in the nervous system.
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Biochem Cell Biol,
89,
61-73.
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M.Yun,
J.Wu,
J.L.Workman,
and
B.Li
(2011).
Readers of histone modifications.
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Cell Res,
21,
564-578.
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S.S.Oliver,
and
J.M.Denu
(2011).
Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".
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Chembiochem,
12,
299-307.
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B.Drobic,
B.Pérez-Cadahía,
J.Yu,
S.K.Kung,
and
J.R.Davie
(2010).
Promoter chromatin remodeling of immediate-early genes is mediated through H3 phosphorylation at either serine 28 or 10 by the MSK1 multi-protein complex.
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Nucleic Acids Res,
38,
3196-3208.
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C.S.Karam,
W.A.Kellner,
N.Takenaka,
A.W.Clemmons,
and
V.G.Corces
(2010).
14-3-3 mediates histone cross-talk during transcription elongation in Drosophila.
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PLoS Genet,
6,
e1000975.
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J.M.Higgins
(2010).
Haspin: a newly discovered regulator of mitotic chromosome behavior.
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Chromosoma,
119,
137-147.
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K.L.Yap,
and
M.M.Zhou
(2010).
Keeping it in the family: diverse histone recognition by conserved structural folds.
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Crit Rev Biochem Mol Biol,
45,
488-505.
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L.Cui,
and
J.Miao
(2010).
Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum.
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Eukaryot Cell,
9,
1138-1149.
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M.Kaiser,
and
C.Ottmann
(2010).
The first small-molecule inhibitor of 14-3-3s: modulating the master regulator.
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Chembiochem,
11,
2085-2087.
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M.Wang,
M.W.Mok,
H.Harper,
W.H.Lee,
J.Min,
S.Knapp,
U.Oppermann,
B.Marsden,
and
M.Schapira
(2010).
Structural genomics of histone tail recognition.
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Bioinformatics,
26,
2629-2630.
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S.Winter,
and
W.Fischle
(2010).
Epigenetic markers and their cross-talk.
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Essays Biochem,
48,
45-61.
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A.Zippo,
R.Serafini,
M.Rocchigiani,
S.Pennacchini,
A.Krepelova,
and
S.Oliviero
(2009).
Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation.
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Cell,
138,
1122-1136.
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B.Pérez-Cadahía,
B.Drobic,
and
J.R.Davie
(2009).
H3 phosphorylation: dual role in mitosis and interphase.
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Biochem Cell Biol,
87,
695-709.
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G.Reid,
R.Gallais,
and
R.Métivier
(2009).
Marking time: the dynamic role of chromatin and covalent modification in transcription.
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Int J Biochem Cell Biol,
41,
155-163.
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J.Savickiene,
G.Treigyte,
K.E.Magnusson,
and
R.Navakauskiene
(2009).
Response of retinoic acid-resistant KG1 cells to combination of retinoic acid with diverse histone deacetylase inhibitors.
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Ann N Y Acad Sci,
1171,
321-333.
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K.L.Dunn,
S.He,
L.Wark,
G.P.Delcuve,
J.M.Sun,
H.Yu Chen,
S.Mai,
and
J.R.Davie
(2009).
Increased genomic instability and altered chromosomal protein phosphorylation timing in HRAS-transformed mouse fibroblasts.
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Genes Chromosomes Cancer,
48,
397-409.
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M.Lin,
C.D.Morrison,
S.Jones,
N.Mohamed,
J.Bacher,
and
C.Plass
(2009).
Copy number gain and oncogenic activity of YWHAZ/14-3-3zeta in head and neck squamous cell carcinoma.
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Int J Cancer,
125,
603-611.
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P.J.Hurd,
A.J.Bannister,
K.Halls,
M.A.Dawson,
M.Vermeulen,
J.V.Olsen,
H.Ismail,
J.Somers,
M.Mann,
T.Owen-Hughes,
I.Gout,
and
T.Kouzarides
(2009).
Phosphorylation of histone h3 thr-45 is linked to apoptosis.
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J Biol Chem,
284,
16575-16583.
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R.J.Loomis,
Y.Naoe,
J.B.Parker,
V.Savic,
M.R.Bozovsky,
T.Macfarlan,
J.L.Manley,
and
D.Chakravarti
(2009).
Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation.
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Mol Cell,
33,
450-461.
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A.Eberlin,
C.Grauffel,
M.Oulad-Abdelghani,
F.Robert,
M.E.Torres-Padilla,
R.Lambrot,
D.Spehner,
L.Ponce-Perez,
J.M.Würtz,
R.H.Stote,
S.Kimmins,
P.Schultz,
A.Dejaegere,
and
L.Tora
(2008).
Histone H3 tails containing dimethylated lysine and adjacent phosphorylated serine modifications adopt a specific conformation during mitosis and meiosis.
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Mol Cell Biol,
28,
1739-1754.
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C.J.Oldfield,
J.Meng,
J.Y.Yang,
M.Q.Yang,
V.N.Uversky,
and
A.K.Dunker
(2008).
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners.
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BMC Genomics,
9,
S1.
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E.Borrelli,
E.J.Nestler,
C.D.Allis,
and
P.Sassone-Corsi
(2008).
Decoding the epigenetic language of neuronal plasticity.
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Neuron,
60,
961-974.
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G.P.Delcuve,
S.He,
and
J.R.Davie
(2008).
Mitotic partitioning of transcription factors.
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J Cell Biochem,
105,
1-8.
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J.W.Edmunds,
L.C.Mahadevan,
and
A.L.Clayton
(2008).
Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation.
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EMBO J,
27,
406-420.
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R.Bierings,
M.Beato,
and
M.J.Edel
(2008).
An endothelial cell genetic screen identifies the GTPase Rem2 as a suppressor of p19ARF expression that promotes endothelial cell proliferation and angiogenesis.
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J Biol Chem,
283,
4408-4416.
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S.Misri,
S.Pandita,
R.Kumar,
and
T.K.Pandita
(2008).
Telomeres, histone code, and DNA damage response.
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Cytogenet Genome Res,
122,
297-307.
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S.Winter,
E.Simboeck,
W.Fischle,
G.Zupkovitz,
I.Dohnal,
K.Mechtler,
G.Ammerer,
and
C.Seiser
(2008).
14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation.
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EMBO J,
27,
88-99.
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W.Walter,
D.Clynes,
Y.Tang,
R.Marmorstein,
J.Mellor,
and
S.L.Berger
(2008).
14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.
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Mol Cell Biol,
28,
2840-2849.
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F.Lottersberger,
A.Panza,
G.Lucchini,
and
M.P.Longhese
(2007).
Functional and physical interactions between yeast 14-3-3 proteins, acetyltransferases, and deacetylases in response to DNA replication perturbations.
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Mol Cell Biol,
27,
3266-3281.
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K.Heo,
B.Kim,
K.Kim,
J.Choi,
H.Kim,
Y.Zhan,
J.A.Ranish,
and
W.An
(2007).
Isolation and characterization of proteins associated with histone H3 tails in vivo.
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J Biol Chem,
282,
15476-15483.
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M.R.Parthun
(2007).
Hat1: the emerging cellular roles of a type B histone acetyltransferase.
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Oncogene,
26,
5319-5328.
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M.S.Ivaldi,
C.S.Karam,
and
V.G.Corces
(2007).
Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in Drosophila.
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Genes Dev,
21,
2818-2831.
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S.D.Taverna,
H.Li,
A.J.Ruthenburg,
C.D.Allis,
and
D.J.Patel
(2007).
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers.
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Nat Struct Mol Biol,
14,
1025-1040.
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S.Lall
(2007).
Primers on chromatin.
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Nat Struct Mol Biol,
14,
1110-1115.
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S.P.Baker,
and
P.A.Grant
(2007).
The SAGA continues: expanding the cellular role of a transcriptional co-activator complex.
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Oncogene,
26,
5329-5340.
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T.Kouzarides
(2007).
Chromatin modifications and their function.
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Cell,
128,
693-705.
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W.Yahyaoui,
M.Callejo,
G.B.Price,
and
M.Zannis-Hadjopoulos
(2007).
Deletion of the cruciform binding domain in CBP/14-3-3 displays reduced origin binding and initiation of DNA replication in budding yeast.
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BMC Mol Biol,
8,
27.
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A.Aitken
(2006).
14-3-3 proteins: a historic overview.
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Semin Cancer Biol,
16,
162-172.
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A.K.Gardino,
S.J.Smerdon,
and
M.B.Yaffe
(2006).
Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms.
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Semin Cancer Biol,
16,
173-182.
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B.T.Seet,
I.Dikic,
M.M.Zhou,
and
T.Pawson
(2006).
Reading protein modifications with interaction domains.
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Nat Rev Mol Cell Biol,
7,
473-483.
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E.R.Lee,
K.W.McCool,
F.E.Murdoch,
and
M.K.Fritsch
(2006).
Dynamic changes in histone H3 phosphoacetylation during early embryonic stem cell differentiation are directly mediated by mitogen- and stress-activated protein kinase 1 via activation of MAPK pathways.
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J Biol Chem,
281,
21162-21172.
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M.B.Omary,
and
N.O.Ku
(2006).
Cell biology: skin care by keratins.
|
| |
Nature,
441,
296-297.
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N.Suka,
E.Nakashima,
K.Shinmyozu,
M.Hidaka,
and
H.Jingami
(2006).
The WD40-repeat protein Pwp1p associates in vivo with 25S ribosomal chromatin in a histone H4 tail-dependent manner.
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Nucleic Acids Res,
34,
3555-3567.
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P.O.Hassa,
S.S.Haenni,
M.Elser,
and
M.O.Hottiger
(2006).
Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
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Microbiol Mol Biol Rev,
70,
789-829.
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R.L.Rich,
and
D.G.Myszka
(2006).
Survey of the year 2005 commercial optical biosensor literature.
|
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J Mol Recognit,
19,
478-534.
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T.Kino,
E.Souvatzoglou,
E.Charmandari,
T.Ichijo,
P.Driggers,
C.Mayers,
A.Alatsatianos,
I.Manoli,
H.Westphal,
G.P.Chrousos,
and
J.H.Segars
(2006).
Rho family Guanine nucleotide exchange factor Brx couples extracellular signals to the glucocorticoid signaling system.
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J Biol Chem,
281,
9118-9126.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
