منابع مشابه
Client-side cross-site scripting protection
Web applications are becoming the dominant way to provide access to online services. At the same time, web application vulnerabilities are being discovered and disclosed at an alarming rate. Web applications often make use of JavaScript code that is embedded into web pages to support dynamic client-side behavior. This script code is executed in the context of the user’s web browser. To protect ...
متن کاملIn silico Study of Toll-Like Receptor 4 Binding Site of FimH from Uropathogenic Escherichia coli
Introduction : The innate immune system as the first line of defense against the pathogens recognizes pathogen-associated molecular patterns (PAMPs) by Toll-Like Receptors (TLRs). Interaction of bacterial PAMPs by TLRs results in activation of innate and acquired immunity. FimH adhesin, a minor component of type 1 fimbriae encoded by Uropathogenic Escherichia coli (UPEC) is a PAMP of TLR4 tha...
متن کاملInvestigating Dynamic Properties of Residues of Warfarin-Azapropazone Binding Site in Human Serum Albumin
Introduction: Human Serum Albumin (HSA) is one of the most important proteins in blood that can bind a wide range of components and different drugs such as Warfarin and is also circulated in the body by HSA. Therefore, studying HSA is very significant in pharmacology. In this research, dynamic behavior of residues of Warfain binding site of HSA has been investigated. Methods: Firstly, PDB form...
متن کاملDisease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System
Receptor tyrosine kinase FGFR3 is involved in many signaling networks and is frequently mutated in developmental disorders and cancer. The Hsp90/Cdc37 chaperone system is essential for function of normal and neoplastic cells. Here we uncover the mechanistic inter-relationships between these proteins by combining approaches including NMR, HDX-MS, and SAXS. We show that several disease-linked mut...
متن کاملThe Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37
Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50(cdc37) acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via its C-terminal region. p50(cdc37) also has a regulatory activity, arresting Hsp90's ATPase cycle during client-protein loading. We have localized the binding site for p50(cdc37) to the N-terminal nucleotide binding...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2005
ISSN: 1742-464X,1742-4658
DOI: 10.1111/j.1742-4658.2005.04884.x