|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 1 to 100 out of 122 for Rps2

<< First    < Previous  |  Next >    Last >>
0.045s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: rabbit, European
Gene
Type: gene
Organism: rat
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Swiercz R
Year: 2007
Journal: J Biol Chem
Title: Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice.
Volume: 282
Issue: 23
Pages: 16917-23
Publication
First Author: Swiercz R
Year: 2005
Journal: Biochem J
Title: Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3).
Volume: 386
Issue: Pt 1
Pages: 85-91
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Moore J
Year: 2021
Journal: Commun Biol
Title: Random errors in protein synthesis activate an age-dependent program of muscle atrophy in mice.
Volume: 4
Issue: 1
Pages: 703
Publication  
First Author: Moore J
Year: 2021
Journal: Cells
Title: Silencing of the ER and Integrative Stress Responses in the Liver of Mice with Error-Prone Translation.
Volume: 10
Issue: 11
Publication
First Author: Goomer RS
Year: 1999
Journal: J Orthop Res
Title: PT-12, a putative ras-activated proliferation-dependent gene, is expressed in patellar tendon and not in anterior cruciate ligament.
Volume: 17
Issue: 5
Pages: 745-7
Publication
First Author: Rovai LE
Year: 1998
Journal: J Leukoc Biol
Title: The murine neutrophil-chemoattractant chemokines LIX, KC, and MIP-2 have distinct induction kinetics, tissue distributions, and tissue-specific sensitivities to glucocorticoid regulation in endotoxemia.
Volume: 64
Issue: 4
Pages: 494-502
GXD Expression      
Probe: MGI:27989
Assay Type: Northern blot
Annotation Date: 2003-05-28
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1603916
Stage: TS16
Assay Id: MGI:2661181
Age: embryonic day 10.0
Specimen Label: 1
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:27989
Assay Type: Northern blot
Annotation Date: 2003-05-28
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1603920
Stage: TS20
Assay Id: MGI:2661181
Age: embryonic day 12.0
Specimen Label: 2
Detected: true
Specimen Num: 2
GXD Expression      
Probe: MGI:27989
Assay Type: Northern blot
Annotation Date: 2003-05-28
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1684628
Stage: TS28
Assay Id: MGI:2661181
Age: postnatal adult
Specimen Label: 3
Detected: true
Specimen Num: 3
GXD Expression
Probe: MGI:3834380
Assay Type: RNA in situ
Annotation Date: 2009-03-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1915728
Pattern: Regionally restricted
Stage: TS28
Assay Id: MGI:3834684
Age: postnatal day 14
Image: S7 wt P14
Note: Expression was detected in rods.
Specimen Label: S7 wt P14
Detected: true
Specimen Num: 1
GXD Expression
Probe: MGI:3834380
Assay Type: RNA in situ
Annotation Date: 2009-03-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1915728
Pattern: Regionally restricted
Stage: TS28
Assay Id: MGI:3834684
Age: postnatal day 14
Image: S7 Nr2e3-/- P14
Note: Expression was detected in rods as in wild type.
Specimen Label: S7 Nr2e3-/- P14
Detected: true
Specimen Num: 2
GXD Expression
Probe: MGI:3834380
Assay Type: RNA in situ
Annotation Date: 2009-03-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1915728
Pattern: Regionally restricted
Stage: TS28
Assay Id: MGI:3834684
Age: postnatal day 6
Image: S7 wt P6
Note: Expression was detected in rods.
Specimen Label: S7 wt P6
Detected: true
Specimen Num: 3
GXD Expression
Probe: MGI:3834380
Assay Type: RNA in situ
Annotation Date: 2009-03-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1915728
Pattern: Regionally restricted
Stage: TS28
Assay Id: MGI:3834684
Age: postnatal day 6
Image: S7 Nr2e3-/- P6
Note: Expression was detected in rods as in wild type.
Specimen Label: S7 Nr2e3-/- P6
Detected: true
Specimen Num: 4
Publication
First Author: Derigs HG
Year: 1994
Journal: Exp Hematol
Title: Granulocyte-macrophage colony-stimulating factor expression is regulated at transcriptional and posttranscriptional levels in a murine bone marrow stromal cell line.
Volume: 22
Issue: 9
Pages: 924-32
Publication
First Author: Heller DL
Year: 1988
Journal: Mol Cell Biol
Title: A highly conserved mouse gene with a propensity to form pseudogenes in mammals.
Volume: 8
Issue: 7
Pages: 2797-803
Publication
First Author: Park H
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation.
Volume: 98
Issue: 20
Pages: 11163-8
Publication
First Author: Perera EM
Year: 2001
Journal: Endocrinology
Title: Tescalcin, a novel gene encoding a putative EF-hand Ca(2+)-binding protein, Col9a3, and renin are expressed in the mouse testis during the early stages of gonadal differentiation.
Volume: 142
Issue: 1
Pages: 455-63
Publication
First Author: Yu C
Year: 2016
Journal: Nat Struct Mol Biol
Title: BTG4 is a meiotic cell cycle-coupled maternal-zygotic-transition licensing factor in oocytes.
Volume: 23
Issue: 5
Pages: 387-94
Publication
First Author: Su X
Year: 2018
Journal: Cell Death Dis
Title: Embryonic lethality in mice lacking Trim59 due to impaired gastrulation development.
Volume: 9
Issue: 3
Pages: 302
Publication  
First Author: Zengeler KE
Year: 2022
Journal: Brain Behav Immun
Title: SSRI treatment modifies the effects of maternal inflammation on in utero physiology and offspring neurobiology.
Volume: 108
Pages: 80-97
Publication
First Author: Chu CC
Year: 1998
Journal: Mol Immunol
Title: Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis.
Volume: 35
Issue: 8
Pages: 487-502
Publication
First Author: Lavado A
Year: 2018
Journal: Dev Cell
Title: The Hippo Pathway Prevents YAP/TAZ-Driven Hypertranscription and Controls Neural Progenitor Number.
Volume: 47
Issue: 5
Pages: 576-591.e8
Publication
First Author: Trinidad JC
Year: 2006
Journal: Mol Cell Proteomics
Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.
Volume: 5
Issue: 5
Pages: 914-22
Publication
First Author: Yu C
Year: 2016
Journal: Cell Res
Title: Oocyte-expressed yes-associated protein is a key activator of the early zygotic genome in mouse.
Volume: 26
Issue: 3
Pages: 275-87
Publication
First Author: Khatter H
Year: 2015
Journal: Nature
Title: Structure of the human 80S ribosome.
Volume: 520
Issue: 7549
Pages: 640-5
Publication
First Author: Li H
Year: 2022
Journal: Nature
Title: A male germ-cell-specific ribosome controls male fertility.
Volume: 612
Issue: 7941
Pages: 725-731
Publication
First Author: Takenaka M
Year: 1998
Journal: Kidney Int
Title: Isolation of genes identified in mouse renal proximal tubule by comparing different gene expression profiles.
Volume: 53
Issue: 3
Pages: 562-72
Publication
First Author: Corbo JC
Year: 2005
Journal: PLoS Genet
Title: A hybrid photoreceptor expressing both rod and cone genes in a mouse model of enhanced S-cone syndrome.
Volume: 1
Issue: 2
Pages: e11
Publication
First Author: Kondrashov N
Year: 2011
Journal: Cell
Title: Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning.
Volume: 145
Issue: 3
Pages: 383-397
Publication
First Author: Liu X
Year: 2016
Journal: BMC Immunol
Title: Decreased expression levels of Ifi genes is associated to the increased resistance to spontaneous arthritis disease in mice deficiency of IL-1RA.
Volume: 17
Issue: 1
Pages: 25
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
Publication
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication      
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication
First Author: Reuber TL
Year: 1996
Journal: Plant Cell
Title: Isolation of Arabidopsis genes that differentiate between resistance responses mediated by the RPS2 and RPM1 disease resistance genes.
Volume: 8
Issue: 2
Pages: 241-9
Publication
First Author: Shindo T
Year: 2008
Journal: Mol Plant Pathol
Title: Papain-like cysteine proteases: key players at molecular battlefields employed by both plants and their invaders.
Volume: 9
Issue: 1
Pages: 119-25
Publication
First Author: Mudgett MB
Year: 1999
Journal: Mol Microbiol
Title: Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: demonstration of secretion and processing during bacterial pathogenesis.
Volume: 32
Issue: 5
Pages: 927-41
Protein Domain
Type: Family
Description: This is a family of bacterial cysteine proteases. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis []. AvrRpt2 from Pseudomonas syringae pv tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2 [].
Publication
First Author: Antoine M
Year: 2005
Journal: Biochem Biophys Res Commun
Title: Fibroblast growth factor 3, a protein with a dual subcellular fate, is interacting with human ribosomal protein S2.
Volume: 338
Issue: 2
Pages: 1248-55
Protein Domain
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].Ribosomal S2 proteins have been shown to belong to a family that includes 40S ribosomal subunit 40kDa proteins, putative laminin-binding proteins, NAB-1 protein and 29.3kDa protein from Haloarcula marismortui [, ]. The laminin-receptor proteins are thus predicted to be the eukaryotic homologue of the eubacterial S2 risosomal proteins [].Ribosomal protein S2 (RPS2) are involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones [, , , , , , , , , , , , , ].
Protein Domain
Type: Homologous_superfamily
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].Ribosomal S2 proteins have been shown to belong to a family that includes 40S ribosomal subunit 40kDa proteins, putative laminin-binding proteins, NAB-1 protein and 29.3kDa protein from Haloarcula marismortui [, ]. The laminin-receptor proteins are thus predicted to be the eukaryotic homologue of the eubacterial S2 risosomal proteins [].Ribosomal protein S2 (RPS2) are involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones [, , , , , , , , , , , , , ].This entry represents a flavodoxin-like domain superfamily found in ribosomal protein S2.
Publication
First Author: Davis SC
Year: 1992
Journal: J Biol Chem
Title: Characterization of a yeast mitochondrial ribosomal protein structurally related to the mammalian 68-kDa high affinity laminin receptor.
Volume: 267
Issue: 8
Pages: 5508-14
Publication
First Author: Yusupova G
Year: 2006
Journal: Nature
Title: Structural basis for messenger RNA movement on the ribosome.
Volume: 444
Issue: 7117
Pages: 391-4
Publication
First Author: Jamieson KV
Year: 2008
Journal: J Biol Chem
Title: Crystal structure of the human laminin receptor precursor.
Volume: 283
Issue: 6
Pages: 3002-5