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Search results 1101 to 1200 out of 1200 for Mdm2

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Type Details Score
Publication
31012223 | J:295829
First Author: Lai YJ
Year: 2019
Journal: Aging Cell
Title: Estrogen receptor α promotes Cav1.2 ubiquitination and degradation in neuronal cells and in APP/PS1 mice.
Volume: 18
Issue: 4
Pages: e12961
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Publication
32900967 | J:296363
First Author: Moyer SM
Year: 2020
Journal: Proc Natl Acad Sci U S A
Title: p53 drives a transcriptional program that elicits a non-cell-autonomous response and alters cell state in vivo.
Volume: 117
Issue: 38
Pages: 23663-23673
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Publication
33486098 | J:304089
First Author: Zhu F
Year: 2021
Journal: Biochim Biophys Acta Mol Basis Dis
Title: Tubular Numb promotes renal interstitial fibrosis via modulating HIF-1α protein stability.
Volume: 1867
Issue: 5
Pages: 166081
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Publication
36940336 | J:340838
First Author: Xue Y
Year: 2023
Journal: Proc Natl Acad Sci U S A
Title: Proteasome inhibitor bortezomib stabilizes and activates p53 in hematopoietic stem/progenitors and double-negative T cells in vivo.
Volume: 120
Issue: 13
Pages: e2219978120
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Publication
38474404 | J:346068
 
First Author: Huang Y
Year: 2024
Journal: Cells
Title: Alcohol Exposure Induces Nucleolar Stress and Apoptosis in Mouse Neural Stem Cells and Late-Term Fetal Brain.
Volume: 13
Issue: 5
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Publication
12954336 | -
First Author: Lentzen G
Year: 2003
Journal: Chem Biol
Title: Structural basis for contrasting activities of ribosome binding thiazole antibiotics.
Volume: 10
Issue: 8
Pages: 769-78
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Publication
17169991 | -
First Author: Jonker HR
Year: 2007
Journal: Nucleic Acids Res
Title: L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy.
Volume: 35
Issue: 2
Pages: 441-54
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Publication
17095013 | -
First Author: Jenvert RM
Year: 2007
Journal: J Mol Biol
Title: The flexible N-terminal domain of ribosomal protein L11 from Escherichia coli is necessary for the activation of stringent factor.
Volume: 365
Issue: 3
Pages: 764-72
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Publication
17015650 | -
First Author: Kasai K
Year: 2006
Journal: J Bacteriol
Title: Physiological analysis of the stringent response elicited in an extreme thermophilic bacterium, Thermus thermophilus.
Volume: 188
Issue: 20
Pages: 7111-22
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Publication
16803902 | -
First Author: Dai MS
Year: 2006
Journal: J Biol Chem
Title: Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism.
Volume: 281
Issue: 34
Pages: 24304-13
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Publication
16371360 | -
First Author: Bouakaz L
Year: 2006
Journal: J Biol Chem
Title: The role of ribosomal protein L11 in class I release factor-mediated translation termination and translational accuracy.
Volume: 281
Issue: 7
Pages: 4548-56
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Publication
15492007 | -
First Author: Bowen WS
Year: 2005
Journal: J Biol Chem
Title: Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain.
Volume: 280
Issue: 4
Pages: 2934-43
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Publication
15152193 | -
First Author: Bhat KP
Year: 2004
Journal: EMBO J
Title: Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation.
Volume: 23
Issue: 12
Pages: 2402-12
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Protein Domain
IPR000911 | Ribosomal_L11/L12
Type: Family
Description: Ribosomal protein L11 is one of the proteins from the large ribosomal subunit. In Escherichia coli, L11 is known to bind directly to the 23S rRNA and plays a significant role during initiation, elongation, and termination of protein synthesis. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [], groups bacteria, plant chloroplast, red algal chloroplast, cyanelle and archaeabacterial L11; and mammalian, plant and yeast L12 (YL15). L11 is a protein of 140 to 165 amino-acid residues. L11 consists of a 23S rRNA binding C-terminal domain and an N-terminal domain that directly contacts protein synthesis factors. These two domains are joined by a flexible linker that allows inter-domain movement during protein synthesis. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA [, , , ]. In E. coli, the C-terminal half of L11 has been shown []to be in an extended and loosely folded conformation and is likely to be buried within the ribosomal structure.Ribosomal protein L11, together with proteins L10 and L7/L12, and 23S rRNA, form the L7/L12 stalk on the surface of the large subunit of the ribosome. The homologous eukaryotic cytoplasmic protein is also called 60S ribosomal protein L12, which is distinct from the L12 involved in the formation of the L7/L12 stalk. The C-terminal domain (CTD) of L11 is essential for binding 23S rRNA, while the N-terminal domain (NTD) contains the binding site for the antibiotics thiostrepton and micrococcin. L11 and 23S rRNA form an essential part of the GTPase-associated region (GAR). Based on differences in the relative positions of the L11 NTD and CTD during the translational cycle, L11 is proposed to play a significant role in the binding of initiation factors, elongation factors, and release factors to the ribosome. Several factors, including the class I release factors RF1 and RF2, are known to interact directly with L11. In eukaryotes, L11 has been implicated in regulating the levels of ubiquinated p53 and MDM2 in the MDM2-p53 feedback loop, which is responsible for apoptosis in response to DNA damage. In bacteria, the "stringent response"to harsh conditions allows bacteria to survive, and ribosomes that lack L11 are deficient in stringent factor stimulation [, , , , , , , , , , , ].
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Protein Domain
IPR003889 | FYrich_C
Type: Domain
Description: The "FY-rich"domain N-terminal (FYRN) and "FY-rich"domain C-terminal (FYRC) sequence motifs are two poorly characterised phenylalanine/tyrosine-rich regions of around 50 and 100 amino acids, respectively, that arefound in a variety of chromatin-associated proteins [, , , ]. They areparticularly common in histone H3K4 methyltransferases most notably in afamily of proteins that includes human mixed lineage leukemia (MLL) and theDrosophila melanogaster protein trithorax. Both of these enzymes play a keyrole in the epigenetic regulation of gene expression during development, andthe gene coding for MLL is frequently rearranged in infant and secondarytherapy-related acute leukemias. They are also found in transforming growthfactor beta regulator 1 (TBRG1), a growth inhibitory protein induced in cellsundergoing arrest in response to DNA damage and transforming growth factor(TGF)-beta1. As TBRG1 has been shown to bind to both the tumor suppressorp14ARF and MDM2, a key regulator of p53, it is also known as nuclearinteractor of ARF and MDM2 (NIAM). In most proteins, the FYRN and FYRC regionsare closely juxtaposed, however, in MLL and its homologues they are fardistant. To be fully active, MLL must be proteolytically processed bytaspase1, which cleaves the protein between the FYRN and FYRC regions []. TheN-terminal and C-terminal fragments remain associated after proteolysisapparently as a result of an interaction between the FYRN and FYRC regions.How proteolytic processing regulates the activity of MLL is not known.Intriguingly, the FYRN and FYRC motifs of a second family of histone H3K4methyltransferases, represented by MLL2 and MLL4 in humans and TRR inDrosophila melanogaster, are closely juxtaposed. FYRN and FYRC motifs arefound in association with modules that create or recognise histonemodifications in proteins from a wide range of eukaryotes, and it is likelythat in these proteins they have a conserved role related to some aspect ofchromatin biology [].The FYRN and FYRC regions are not separate independently folded domains, butare components of a distinct protein module, The FYRN and FYRC motifs bothform part of a single folded module (the FYR domain), which adopts an alpha+beta fold consisting of a six-stranded antiparallel β-sheet followed byfour consecutive α-helices. The FYRN region correspondsto β-strands 1-4 and their connecting loops, whereas the FYRC motif maps toβ-strand 5, β-strand 6 and helices alpha1 to alpha4. Most of theconserved tyrosine and phenylalanine residues, after which these motifs arenamed are involved in interactions that stabilise the fold. Proteins such asMLL, in which the FYRN and FYRC regions are separated by hundreds of aminoacids, are expected to contain FYR domains with a large insertion between twoof the strands of the β-sheet (strands 4 and 5) [].
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Protein Domain
IPR003888 | FYrich_N
Type: Domain
Description: The "FY-rich"domain N-terminal (FYRN) and "FY-rich"domain C-terminal (FYRC) sequence motifs are two poorly characterised phenylalanine/tyrosine-rich regions of around 50 and 100 amino acids, respectively, that arefound in a variety of chromatin-associated proteins [, , , ]. They areparticularly common in histone H3K4 methyltransferases most notably in afamily of proteins that includes human mixed lineage leukemia (MLL) and theDrosophila melanogaster protein trithorax. Both of these enzymes play a keyrole in the epigenetic regulation of gene expression during development, andthe gene coding for MLL is frequently rearranged in infant and secondarytherapy-related acute leukemias. They are also found in transforming growthfactor beta regulator 1 (TBRG1), a growth inhibitory protein induced in cellsundergoing arrest in response to DNA damage and transforming growth factor(TGF)-beta1. As TBRG1 has been shown to bind to both the tumor suppressorp14ARF and MDM2, a key regulator of p53, it is also known as nuclearinteractor of ARF and MDM2 (NIAM). In most proteins, the FYRN and FYRC regionsare closely juxtaposed, however, in MLL and its homologues they are fardistant. To be fully active, MLL must be proteolytically processed bytaspase1, which cleaves the protein between the FYRN and FYRC regions []. TheN-terminal and C-terminal fragments remain associated after proteolysisapparently as a result of an interaction between the FYRN and FYRC regions.How proteolytic processing regulates the activity of MLL is not known.Intriguingly, the FYRN and FYRC motifs of a second family of histone H3K4methyltransferases, represented by MLL2 and MLL4 in humans and TRR inDrosophila melanogaster, are closely juxtaposed. FYRN and FYRC motifs arefound in association with modules that create or recognise histonemodifications in proteins from a wide range of eukaryotes, and it is likelythat in these proteins they have a conserved role related to some aspect ofchromatin biology [].The FYRN and FYRC regions are not separate independently folded domains, butare components of a distinct protein module, The FYRN and FYRC motifs bothform part of a single folded module (the FYR domain), which adopts an alpha+beta fold consisting of a six-stranded antiparallel β-sheet followed byfour consecutive α-helices. The FYRN region correspondsto β-strands 1-4 and their connecting loops, whereas the FYRC motif maps toβ-strand 5, β-strand 6 and helices alpha1 to alpha4. Most of theconserved tyrosine and phenylalanine residues, after which these motifs arenamed are involved in interactions that stabilise the fold. Proteins such asMLL, in which the FYRN and FYRC regions are separated by hundreds of aminoacids, are expected to contain FYR domains with a large insertion between twoof the strands of the β-sheet (strands 4 and 5) [].
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Publication
21084607 | J:182379
First Author: Zhong Z
Year: 2010
Journal: J Neurosci
Title: Protein S protects neurons from excitotoxic injury by activating the TAM receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway through its sex hormone-binding globulin-like region.
Volume: 30
Issue: 46
Pages: 15521-34
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Publication
25742798 | J:220470
First Author: Hayano S
Year: 2015
Journal: Development
Title: Augmented BMP signaling in the neural crest inhibits nasal cartilage morphogenesis by inducing p53-mediated apoptosis.
Volume: 142
Issue: 7
Pages: 1357-67
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Publication
28265066 | J:298026
First Author: Chapeau EA
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Resistance mechanisms to TP53-MDM2 inhibition identified by in vivo piggyBac transposon mutagenesis screen in an Arf-/- mouse model.
Volume: 114
Issue: 12
Pages: 3151-3156
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Publication
17989286 | J:127443
First Author: Uo T
Year: 2007
Journal: J Neurosci
Title: Apoptotic actions of p53 require transcriptional activation of PUMA and do not involve a direct mitochondrial/cytoplasmic site of action in postnatal cortical neurons.
Volume: 27
Issue: 45
Pages: 12198-210
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Publication
28892044 | J:254250
First Author: Comiskey DF Jr
Year: 2018
Journal: Oncogene
Title: A novel mouse model of rhabdomyosarcoma underscores the dichotomy of MDM2-ALT1 function in vivo.
Volume: 37
Issue: 1
Pages: 95-106
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Publication
26915821 | J:231514
First Author: Yan W
Year: 2016
Journal: Genes Dev
Title: Mice deficient in poly(C)-binding protein 4 are susceptible to spontaneous tumors through increased expression of ZFP871 that targets p53 for degradation.
Volume: 30
Issue: 5
Pages: 522-34
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Publication
17602169 | J:126703
First Author: Iida K
Year: 2007
Journal: Carcinogenesis
Title: Nrf2 and p53 cooperatively protect against BBN-induced urinary bladder carcinogenesis.
Volume: 28
Issue: 11
Pages: 2398-403
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Publication
28842295 | J:268767
First Author: Nakamura K
Year: 2017
Journal: J Hepatol
Title: Macrophage heme oxygenase-1-SIRT1-p53 axis regulates sterile inflammation in liver ischemia-reperfusion injury.
Volume: 67
Issue: 6
Pages: 1232-1242
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Publication
18285661 | J:347124
First Author: Sugihara T
Year: 2008
Journal: J Radiat Res
Title: Inverse dose-rate-effects on the expressions of extra-cellular matrix-related genes in low-dose-rate gamma-ray irradiated murine cells.
Volume: 49
Issue: 3
Pages: 231-40
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Publication
23209436 | J:194670
First Author: Saldivar JC
Year: 2012
Journal: PLoS Genet
Title: Initiation of genome instability and preneoplastic processes through loss of Fhit expression.
Volume: 8
Issue: 11
Pages: e1003077
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Publication
10894886 | J:63577
First Author: Zhuang S
Year: 2000
Journal: Mutat Res
Title: Genetic analysis of Raf1, Mdm2, c-Myc, Cdc25a and Cdc25b proto-oncogenes in 2',3'-dideoxycytidine- and 1,3-butadiene-induced lymphomas in B6C3F1 mice.
Volume: 452
Issue: 1
Pages: 19-26
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Publication
12750288 | J:83493
First Author: Phelps M
Year: 2003
Journal: Cancer Res
Title: p53-independent activation of the hdm2-P2 promoter through multiple transcription factor response elements results in elevated hdm2 expression in estrogen receptor alpha-positive breast cancer cells.
Volume: 63
Issue: 10
Pages: 2616-23
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Publication
15865930 | J:98174
First Author: Levav-Cohen Y
Year: 2005
Journal: Biochem Biophys Res Commun
Title: C-Abl as a modulator of p53.
Volume: 331
Issue: 3
Pages: 737-49
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Publication
24647531 | J:215072
First Author: Martinelli VC
Year: 2014
Journal: PLoS One
Title: ZASP interacts with the mechanosensing protein Ankrd2 and p53 in the signalling network of striated muscle.
Volume: 9
Issue: 3
Pages: e92259
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Publication
24336083 | J:320704
 
First Author: Valentino T
Year: 2013
Journal: Cell Death Dis
Title: PATZ1 interacts with p53 and regulates expression of p53-target genes enhancing apoptosis or cell survival based on the cellular context.
Volume: 4
Pages: e963
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Publication
27750399 | J:330468
First Author: Kooi IE
Year: 2017
Journal: Genes Chromosomes Cancer
Title: Genomic landscape of retinoblastoma in Rb-/- p130-/- mice resembles human retinoblastoma.
Volume: 56
Issue: 3
Pages: 231-242
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Protein
P54729
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
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Protein
Q3UYM1
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
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Protein
A0JLP6
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
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Protein
A0A0G2JGQ4
Organism: Mus musculus/domesticus
Length: 638  
Fragment?: false
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Protein
A0PJ90
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
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Publication
20506279 | -
First Author: García-Alai MM
Year: 2010
Journal: Protein Sci
Title: The structure of the FYR domain of transforming growth factor beta regulator 1.
Volume: 19
Issue: 7
Pages: 1432-8
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Protein
O08918
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
P51945
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Q6LC40
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
Q5D0F7
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: true
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Protein
Q3U5X0
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Q3TG40
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
Q5HZK4
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
Q3TCL9
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
Q3TX40
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Q3TV43
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Q8C9K5
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
Q3TKC9
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Q5NC86
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Publication
32727874 | J:299853
 
First Author: Kutle I
Year: 2020
Journal: J Virol
Title: Murine Cytomegalovirus M25 Proteins Sequester the Tumor Suppressor Protein p53 in Nuclear Accumulations.
Volume: 94
Issue: 20
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Publication
32768595 | J:305371
First Author: Tiwari A
Year: 2020
Journal: Gastroenterology
Title: Loss of HIF1A From Pancreatic Cancer Cells Increases Expression of PPP1R1B and Degradation of p53 to Promote Invasion and Metastasis.
Volume: 159
Issue: 5
Pages: 1882-1897.e5
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Publication
9247308 | J:42245
First Author: Prasad R
Year: 1997
Journal: Oncogene
Title: Structure and expression pattern of human ALR, a novel gene with strong homology to ALL-1 involved in acute leukemia and to Drosophila trithorax.
Volume: 15
Issue: 5
Pages: 549-60
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Publication
12482972 | -
First Author: Hsieh JJ
Year: 2003
Journal: Mol Cell Biol
Title: Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization.
Volume: 23
Issue: 1
Pages: 186-94
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Protein
Q3TPB7
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
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Publication
10838566 | -
First Author: Balciunas D
Year: 2000
Journal: Trends Biochem Sci
Title: Evidence of domain swapping within the jumonji family of transcription factors.
Volume: 25
Issue: 6
Pages: 274-6
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Publication
11779830 | -
First Author: Doerks T
Year: 2002
Journal: Genome Res
Title: Systematic identification of novel protein domain families associated with nuclear functions.
Volume: 12
Issue: 1
Pages: 47-56
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Protein
Q3UWY2
Organism: Mus musculus/domesticus
Length: 865  
Fragment?: true
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Protein
G3UWZ3
Organism: Mus musculus/domesticus
Length: 1524  
Fragment?: true
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Protein
Q3TU00
Organism: Mus musculus/domesticus
Length: 563  
Fragment?: true
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Protein
G3UY45
Organism: Mus musculus/domesticus
Length: 1748  
Fragment?: true
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Protein
Q6ZPP4
Organism: Mus musculus/domesticus
Length: 1520  
Fragment?: true
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Protein
Q6P6H8
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: true
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Publication
17599351 | -
First Author: Kavran JM
Year: 2007
Journal: J Mol Biol
Title: Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements.
Volume: 371
Issue: 4
Pages: 1047-59
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Protein
Q6DI58
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
Q8CHH1
Organism: Mus musculus/domesticus
Length: 1744  
Fragment?: true
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Publication
12910258 | -
First Author: Galderisi U
Year: 2003
Journal: Oncogene
Title: Cell cycle regulation and neural differentiation.
Volume: 22
Issue: 33
Pages: 5208-19
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Protein
A0A494B9H5
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: true
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Protein
A0A494B915
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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Publication
15184028 | -
First Author: Klein DJ
Year: 2004
Journal: J Mol Biol
Title: The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit.
Volume: 340
Issue: 1
Pages: 141-77
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Protein
P55200
Organism: Mus musculus/domesticus
Length: 3966  
Fragment?: false
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Protein
Q6PDK2
Organism: Mus musculus/domesticus
Length: 5588  
Fragment?: false
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Protein
Q8BRH4
Organism: Mus musculus/domesticus
Length: 4903  
Fragment?: false
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Protein
O08550
Organism: Mus musculus/domesticus
Length: 2713  
Fragment?: false
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Protein
F8WJ40
Organism: Mus musculus/domesticus
Length: 2721  
Fragment?: false
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Protein
A0A0A0MQ73
Organism: Mus musculus/domesticus
Length: 5588  
Fragment?: false
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Protein
Q6PHU4
Organism: Mus musculus/domesticus
Length: 2013  
Fragment?: true
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Protein
F8WI37
Organism: Mus musculus/domesticus
Length: 4904  
Fragment?: false
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Protein
F6W623
Organism: Mus musculus/domesticus
Length: 2014  
Fragment?: true
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Protein
P35979
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
Q9CQF0
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
Q5BLK0
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
A0A494B9R3
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
Q5DTR3
Organism: Mus musculus/domesticus
Length: 762  
Fragment?: true
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Protein
Q8C2K0
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
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Protein
Q3TIQ2
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Publication
2483975 | -
First Author: Choli T
Year: 1989
Journal: Biochem Int
Title: Structural properties of ribosomal protein L11 from Escherichia coli.
Volume: 19
Issue: 6
Pages: 1323-38
•
•
•
•
•
Publication
2167467 | -
First Author: Pucciarelli MG
Year: 1990
Journal: Nucleic Acids Res
Title: The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae.
Volume: 18
Issue: 15
Pages: 4409-16
•
•
•
•
•
Publication
10338213 | -
First Author: Wimberly BT
Year: 1999
Journal: Cell
Title: A detailed view of a ribosomal active site: the structure of the L11-RNA complex.
Volume: 97
Issue: 4
Pages: 491-502
•
•
•
•
•
Publication
17215866 | -
First Author: Demirci H
Year: 2007
Journal: EMBO J
Title: Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA.
Volume: 26
Issue: 2
Pages: 567-77
•
•
•
•
•
Publication
18406324 | -
First Author: Harms JM
Year: 2008
Journal: Mol Cell
Title: Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.
Volume: 30
Issue: 1
Pages: 26-38
•
•
•
•
•
Publication
18611379 | -
First Author: Demirci H
Year: 2008
Journal: Structure
Title: Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
Volume: 16
Issue: 7
Pages: 1059-66
•
•
•
•
•
Publication
11042159 | J:68323
First Author: Carninci P
Year: 2000
Journal: Genome Res
Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.
Volume: 10
Issue: 10
Pages: 1617-30
•
•
•
•
•
Publication
10349636 | J:80645
 
First Author: Carninci P
Year: 1999
Journal: Methods Enzymol
Title: High-efficiency full-length cDNA cloning.
Volume: 303
Pages: 19-44
•
•
•
•
•
Publication
11076861 | J:68324
First Author: Shibata K
Year: 2000
Journal: Genome Res
Title: RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer.
Volume: 10
Issue: 11
Pages: 1757-71
•
•
•
•
•
Publication
16141073 | -
First Author: Katayama S
Year: 2005
Journal: Science
Title: Antisense transcription in the mammalian transcriptome.
Volume: 309
Issue: 5740
Pages: 1564-6
•
•
•
•
•
Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
•
•
•
•
•
Publication
21183079 | J:292518
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
•
•
•
•
•
Publication
19468303 | -
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112
•
•
•
•
•




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