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10.1139/bcb-2018-0394 http://scihub22266oqcxt.onion/10.1139/bcb-2018-0394 30943371!ä!30943371 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Cell+Biol 2019 ; 97 (6): 758-766 Nephropedia Template TP {{tp|p=30943371|t=2019. SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex |pdf=|usr=}}{{30943371}} gab.com Text SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex JO: Biochem Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=30943371 #FOAvip Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport. Twit Text FOAVip SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex ????Biochem Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=30943371 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30943371 #FOAvip English Wikipedia <ref>{{Cite pmid|30943371}}</ref> SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex #MMPMID30943371 Gomez GN; Abrar F; Dodhia MP; Gonzalez FG; Nag A Biochem Cell Biol 2019[Dec]; 97 (6): 758-766 PMID30943371show ga Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport. |Cells, Cultured[MESH] |Cytoplasm/genetics/metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Nuclear Pore Complex Proteins/genetics/*metabolism[MESH] |Nuclear Pore/genetics/*metabolism[MESH] |Nucleolin[MESH] |Phosphoproteins/genetics/metabolism[MESH] |RNA-Binding Proteins/genetics/metabolism[MESH] |RNA-Dependent RNA Polymerase/genetics/*metabolism[MESH]SARS coronavirus protein nsp1 disrupts localization of Nup93 from the (epmc).pdf DeepDyve Pubget Overpricing