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10.1093/nar/gkaa941 http://scihub22266oqcxt.onion/10.1093/nar/gkaa941 33137182!7778992!33137182     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleic+Acids+Res 2021 ; 49 (D1): D261-D265 Nephropedia Template TP {{tp|p=33137182|t=2021. ADPriboDB 2 0: an updated database of ADP-ribosylated proteins |pdf=|usr=}}{{33137182}} gab.com Text ADPriboDB 2 0: an updated database of ADP-ribosylated proteins JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=33137182 #FOAvip ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48 346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32 946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing. Twit Text FOAVip ADPriboDB 2 0: an updated database of ADP-ribosylated proteins ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=33137182 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33137182 #FOAvip English Wikipedia <ref>{{Cite pmid|33137182}}</ref> ADPriboDB 2 0: an updated database of ADP-ribosylated proteins #MMPMID33137182 Ayyappan V; Wat R; Barber C; Vivelo CA; Gauch K; Visanpattanasin P; Cook G; Sazeides C; Leung AKL Nucleic Acids Res 2021[Jan]; 49 (D1): D261-D265 PMID33137182show ga ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48 346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32 946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing. |ADP-Ribosylation[MESH] |Adenosine Diphosphate Ribose/*metabolism[MESH] |Binding Sites[MESH] |COVID-19/epidemiology/prevention & control/virology[MESH] |Computational Biology/methods/*statistics & numerical data[MESH] |Databases, Protein/*statistics & numerical data[MESH] |Humans[MESH] |Protein Domains[MESH] |Protein Processing, Post-Translational[MESH] |Proteins/chemistry/*metabolism[MESH] |SARS-CoV-2/metabolism/physiology[MESH]ADPriboDB 2 0: an updated database of ADP-ribosylated proteins (epmc).pdf DeepDyve Pubget Overpricing