Published in J Cell Biol on December 01, 1989
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Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol Biol Cell (1992) 1.74
The efficiency of protein compartmentalization into the secretory pathway. Mol Biol Cell (2004) 1.74
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol (1991) 1.61
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Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA. J Cell Biol (1993) 1.37
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The signal sequence interacts with the methionine-rich domain of the 54-kD protein of signal recognition particle. J Cell Biol (1991) 1.35
Epithelial V-like antigen (EVA), a novel member of the immunoglobulin superfamily, expressed in embryonic epithelia with a potential role as homotypic adhesion molecule in thymus histogenesis. J Cell Biol (1998) 1.28
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The HOG pathway dictates the short-term translational response after hyperosmotic shock. Mol Biol Cell (2010) 1.21
A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J (1996) 1.19
The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Mol Biol Cell (1995) 1.18
The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent-polypeptide-associated complex. Proc Natl Acad Sci U S A (1995) 1.17
A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins. EMBO J (1995) 1.14
In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. EMBO J (2000) 1.09
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A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation. J Cell Biol (1991) 1.09
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle. Nucleic Acids Res (1997) 1.05
A highly efficient, cell-free translation/translocation system prepared from Xenopus eggs. Nucleic Acids Res (1991) 1.04
A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNA. Mol Cell Biol (1994) 1.01
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Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes. J Cell Biol (1993) 0.98
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Translation elongation regulates substrate selection by the signal recognition particle. J Biol Chem (2012) 0.92
Structures of the scanning and engaged states of the mammalian SRP-ribosome complex. Elife (2015) 0.87
The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe. Mol Cell Biol (1994) 0.86
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Escherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed. MBio (2010) 0.83
A mutation in the signal recognition particle 7S RNA of the yeast Yarrowia lipolytica preferentially affects synthesis of the alkaline extracellular protease: in vivo evidence for translational arrest. J Cell Biol (1992) 0.82
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions. Nat Struct Mol Biol (2015) 0.81
Down-regulation of the trypanosomatid signal recognition particle affects the biogenesis of polytopic membrane proteins but not of signal peptide-containing proteins. Eukaryot Cell (2007) 0.80
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction. Nucleic Acids Res (2016) 0.75
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Proteomic analysis of etiolated juvenile tetraploid Robinia pseudoacacia branches during different cutting periods. Int J Mol Sci (2014) 0.75
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Efficient cleavage and segregation of nascent presecretory proteins in a reticulocyte lysate supplemented with microsomal membranes. J Biol Chem (1978) 3.80
Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane. J Cell Biol (1985) 3.19
Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties. Methods Enzymol (1983) 2.87
Molecular cloning and characterization of the mRNA for cyclin from sea urchin eggs. EMBO J (1987) 2.71
Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. EMBO J (1987) 2.07
The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. EMBO J (1988) 2.00
Transfer of secretory proteins through the membrane of the endoplasmic reticulum. Int Rev Cytol (1986) 1.74
Protein translocation across wheat germ microsomal membranes requires an SRP-like component. EMBO J (1987) 1.51
Signal recognition particle (SRP) does not mediate a translational arrest of nascent secretory proteins in mammalian cell-free systems. EMBO J (1985) 1.43
Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membrane. J Mol Biol (1987) 1.26
Signal recognition particle arrests elongation of nascent secretory and membrane proteins at multiple sites in a transient manner. J Biol Chem (1987) 1.17
Signal recognition-like particles are present in maize. J Biol Chem (1988) 1.06
Wild type and mutant signal peptides of Escherichia coli outer membrane lipoprotein interact with equal efficiency with mammalian signal recognition particle. J Biol Chem (1987) 0.96
Signal recognition particle causes a transient arrest in the biosynthesis of prepromelittin and mediates its translocation across mammalian endoplasmic reticulum. J Cell Biol (1987) 0.90
Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell (2000) 13.44
Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature (1986) 11.35
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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell (1996) 8.17
Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature (1982) 7.80
Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol (1981) 7.40
Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci U S A (1980) 7.17
Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol (1983) 6.94
Protein translocation across the endoplasmic reticulum. Cell (1984) 6.69
The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell (1997) 6.26
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Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J (1996) 5.46
Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu Rev Cell Biol (1986) 5.28
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Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol (2001) 5.08
tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell (1996) 4.93
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In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor. Cell (1986) 4.59
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Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae. Mol Biol Cell (1999) 4.34
Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature (1989) 4.25
Tryptic dissection and reconstitution of translocation activity for nascent presecretory proteins across microsomal membranes. Proc Natl Acad Sci U S A (1979) 4.22
Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol (1982) 4.10
An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science (1990) 3.55
Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc Natl Acad Sci U S A (1986) 3.55
The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol Biol Cell (1997) 3.45
Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell (2001) 3.45
Disassembly and reconstitution of signal recognition particle. Cell (1983) 3.45
Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol (1996) 3.33
The signal recognition particle in S. cerevisiae. Cell (1991) 3.24
Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane. J Cell Biol (1985) 3.19
Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP. Cell (1988) 3.11
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The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol (1998) 2.48
Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell (1998) 2.44
Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm. J Cell Biol (1988) 2.41
Retinal side-effects of sildenafil. Lancet (1999) 2.40
Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor. Nature (1994) 2.37
The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J (1990) 2.35
Translational attenuation mediated by an mRNA intron. Curr Biol (1997) 2.32
Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain. Cell (1988) 2.31
A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science (1993) 2.28
Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Nature (1986) 2.21
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science (1995) 2.17
A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell (1999) 2.11
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Secretion requires a cytoplasmically disposed sulphydryl of the RER membrane. Nature (1980) 2.10
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Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA "footprinting". Proc Natl Acad Sci U S A (1988) 2.04
The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. EMBO J (1988) 2.00
The unfolded-protein-response pathway in yeast. Trends Cell Biol (1994) 2.00
Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J (1997) 1.99
A bacterial secretory protein requires signal recognition particle for translocation across mammalian endoplasmic reticulum. J Biol Chem (1982) 1.97
The signal recognition particle receptor is a complex that contains two distinct polypeptide chains. J Cell Biol (1986) 1.95
The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J Biol Chem (1988) 1.94
Influence of L-tryptophan and its metabolites on gluconeogenesis in the isolated, perfused liver. Biochemistry (1967) 1.92
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature (1993) 1.88
Crystal structures of coaxially stacked kissing complexes of the HIV-1 RNA dimerization initiation site. Nat Struct Biol (2001) 1.86
Effect of propranolol and phentolamine on myocardial necrosis after subarachnoid haemorrhage. Br Med J (1978) 1.84
Oxidants in mitochondria: from physiology to diseases. Biochim Biophys Acta (1995) 1.82
Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe. J Cell Biol (1983) 1.79
Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J (1994) 1.77
Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Cell Biol (1990) 1.76
Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol Biol Cell (1992) 1.74
Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel. J Cell Biol (1989) 1.70
Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth. J Cell Biol (1989) 1.62
SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Cell (1995) 1.62
Signal recognition protein is required for the integration of acetylcholine receptor delta subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane. J Cell Biol (1982) 1.62
Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores. Mol Cell Biol (1994) 1.61
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol (1991) 1.61
Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p. RNA (2001) 1.60
Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J Cell Biol (1992) 1.60
Regulation of organelle biogenesis. Cell (1996) 1.58
The crystal structure of the dimerization initiation site of genomic HIV-1 RNA reveals an extended duplex with two adenine bulges. Structure (1999) 1.51
Isolation and characterization of a cDNA clone encoding the 19 kDa protein of signal recognition particle (SRP): expression and binding to 7SL RNA. Nucleic Acids Res (1988) 1.47
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol (1999) 1.47
Evidence for an extended 7SL RNA structure in the signal recognition particle. EMBO J (1987) 1.44
ER membrane protein complex required for nuclear fusion. J Cell Biol (1996) 1.43
Small ribonucleoproteins in Schizosaccharomyces pombe and Yarrowia lipolytica homologous to signal recognition particle. Proc Natl Acad Sci U S A (1988) 1.39
The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome. Curr Biol (1996) 1.38
Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog. Proc Natl Acad Sci U S A (1993) 1.38
Role of signal recognition particle in the membrane assembly of Sindbis viral glycoproteins. Eur J Biochem (1984) 1.34
Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase. Proc Natl Acad Sci U S A (1983) 1.34
Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor. J Cell Biol (1989) 1.33
The anticodon triplet is not sufficient to confer methionine acceptance to a transfer RNA. Proc Natl Acad Sci U S A (1992) 1.32