Computational Prediction of Human Saliva-Secreted Proteins

2014 ◽  
pp. 92-101
Author(s):  
Ying Sun ◽  
Chunguang Zhou ◽  
Jiaxin Wang ◽  
Zhongbo Cao ◽  
Wei Du ◽  
...  
Keyword(s):  
Computational Prediction ◽  
Human Saliva ◽  
Secreted Proteins

scholarly journals Computational prediction of secreted proteins in gram-negative bacteria

2021 ◽  
Author(s):  
Xinjie Hui ◽  
Zewei Chen ◽  
Junya Zhang ◽  
Moyang Lu ◽  
Xuxia Cai ◽  
...  
Keyword(s):  
Computational Prediction ◽  
Secreted Proteins ◽  
Gram Negative Bacteria ◽  
Gram Negative

scholarly journals Computational prediction of type III secreted proteins from gram-negative bacteria

2010 ◽  
Vol 11 (Suppl 1) ◽  
pp. S47 ◽  
Author(s):  
Yang Yang ◽  
Jiayuan Zhao ◽  
Robyn L Morgan ◽  
Wenbo Ma ◽  
Tao Jiang
Keyword(s):  
Computational Prediction ◽  
Secreted Proteins ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Type Iii

Immunological Evidence for Prothrombin in Human Platelets

1986 ◽  
Vol 55 (02) ◽  
pp. 268-270
Author(s):  
R J Alexander
Keyword(s):  
Electrophoretic Mobility ◽  
Platelet Activation ◽  
Double Diffusion ◽  
Human Platelets ◽  
Secreted Proteins ◽  
Platelet Surface ◽  
Activated Platelets ◽  
Similar Protein ◽  
Diffusion Assay ◽  
Supernatant Solution

SummaryAn attempt was made to isolate from plasma the platelet surface substrate for thrombin, glycoprotein V (GPV), because a GPV antigen was reported to be present in plasma (3). Plasma fractionation based on procedures for purification of GPV from platelets revealed a thrombin-sensitive protein with appropriate electrophoretic mobility. The protein was purified; an antiserum against it i) reacted with detergent-solubilized platelet proteins or secreted proteins in a double diffusion assay, ii) adsorbed a protein from the supernatant solution of activated platelets, and iii) inhibited thrombin-induced platelet activation, but the antiserum did not adsorb labeled GPV. The purified protein was immunochemically related to prothrombin rather than to GPV. Other antibodies against prothrombin were also able to adsorb a protein from platelets. It is concluded that 1) plasma does not contain appreciable amounts of GPV, and 2) platelets contain prothrombin or an immunochemically similar protein.

Use of OPLC for quantitation of HCHO, as the dimedone adduct, in human saliva in different dental pathologies

2002 ◽  
Vol 15 (1) ◽  
pp. 19-22 ◽  
Author(s):  
T. Katarzyna Różyło ◽  
Anna Żabińska ◽  
Ingrid Różyło-Kalinowska
Keyword(s):  
Human Saliva

Human Saliva as a Liquid Biopsy for Detecting the SARS-CoV-2

2020 ◽  
Vol 29 (Special Supplement) ◽  
pp. S1-S3
Author(s):  
Zohaib Khurshid ◽  
◽  
Shahjahan Katpar ◽  
Keyword(s):  
Liquid Biopsy ◽  
Human Saliva

Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites

2019 ◽  
Author(s):  
Michael Olp ◽  
Daniel Sprague ◽  
Stefan Kathman ◽  
Ziyang Xu ◽  
Alexandar Statsyuk ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Site ◽  
Binding Sites ◽  
Computational Prediction ◽  
Chemical Probes ◽  
Computational Docking ◽  
Fragment Screening ◽  
Covalent Inhibitors ◽  
Bet Protein ◽  
Proof Of Principle

<p>Brd4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding sites and competitively inhibit BET protein interaction with acetylated chromatin. Alternative chemical probes that act orthogonally to the highly-conserved acetyl-lysine binding sites may exhibit selectivity within the BET family and avoid recently reported toxicity in clinical trials of BET bromodomain inhibitors. Here, we report the first identification of a ligandable site on a bromodomain outside the acetyl-lysine binding site. Inspired by our computational prediction of hotspots adjacent to non-homologous cysteine residues within the <i>C</i>-terminal Brd4 bromodomain (Brd4-BD2), we performed a mid-throughput mass spectrometry screen to identify cysteine-reactive fragments that covalently and selectively modify Brd4. Subsequent mass spectrometry, NMR and computational docking analyses of electrophilic fragment hits revealed a novel ligandable site near Cys356 that is unique to Brd4 among all human bromodomains. This site is orthogonal to the Brd4-BD2 acetyl-lysine binding site as Cys356 modification did not impact binding of the pan-BET bromodomain inhibitor JQ1 in fluorescence polarization assays. Finally, we tethered covalent fragments to JQ1 and performed NanoBRET assays to provide proof of principle that this orthogonal site can be covalently targeted in intact human cells. Overall, we demonstrate the potential of targeting sites orthogonal to bromodomain acetyl-lysine binding sites to develop bivalent and covalent inhibitors that displace Brd4 from chromatin.</p>

Sign in / Sign up

Export Citation Format

Share Document