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10.1016/j.bbagen.2016.05.040 http://scihub22266oqcxt.onion/10.1016/j.bbagen.2016.05.040 C5610039!5610039 !27266343     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27266343 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Biochim+Biophys+Acta 2016 ; 1860 (11 Pt B ): 2672-81 Nephropedia Template TP {{tp|p=27266343 |t=2016. Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes |pdf=|usr=}}{{27266343 }} gab.com Text Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=27266343 #FOAvip BACKGROUND: The dominant feature in neurodegenerative diseases is protein aggregations that lead to neuronal loss. Immunotherapies using antibodies or antibody fragments to target the aggregations are a highly perused approach. The molecular mechanisms underlying the amyloid-based immunotherapy are complex. Deciphering the properties of amyloidogenic proteins responsible for these diseases is essential to obtain insights into antibody recognition of the amyloid antigens. SCOPE OF REVIEW: We systematically explore all available crystal structures of antibody-amyloid complexes related to neurodegenerative diseases, including antibodies that recognize the A? peptide, tau protein, prion protein, alpha-synuclein, huntingtin protein (mHTT), and polyglutamine. MAJOR CONCLUSIONS: We found that antibodies mostly use the conformational selection mechanism to recognize the highly flexible amyloid antigens. In particular, solanezumab bound to A?12-28 tripeptide motif conformation (F19F20A21), which is shared with the A?42 fibril. This motif, which is trapped by the antibody, may provide the missing link in amyloid formation. Water molecules often bridge between the antibody and amyloid, contributing to the recognition. GENERAL SIGNIFICANCE: This paper provides the structural basis for antibody recognition of amyloidogenic proteins. The analysis and discussion of known structures are expected to help in the design and optimization of antibodies in neurodegenerative diseases. This article is part of a Special Issue entitled "System Genetics" Guest Editor: Dr. Yudong Cai and Dr. Tao Huang. Twit Text FOAVip Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=27266343 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27266343 #FOAvip English Wikipedia <ref>{{Cite pmid|27266343 }}</ref> Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes #MMPMID27266343 Ma B ; Zhao J ; Nussinov R Biochim Biophys Acta 2016[Nov]; 1860 (11 Pt B ): 2672-81 PMID27266343 show ga BACKGROUND: The dominant feature in neurodegenerative diseases is protein aggregations that lead to neuronal loss. Immunotherapies using antibodies or antibody fragments to target the aggregations are a highly perused approach. The molecular mechanisms underlying the amyloid-based immunotherapy are complex. Deciphering the properties of amyloidogenic proteins responsible for these diseases is essential to obtain insights into antibody recognition of the amyloid antigens. SCOPE OF REVIEW: We systematically explore all available crystal structures of antibody-amyloid complexes related to neurodegenerative diseases, including antibodies that recognize the A? peptide, tau protein, prion protein, alpha-synuclein, huntingtin protein (mHTT), and polyglutamine. MAJOR CONCLUSIONS: We found that antibodies mostly use the conformational selection mechanism to recognize the highly flexible amyloid antigens. In particular, solanezumab bound to A?12-28 tripeptide motif conformation (F19F20A21), which is shared with the A?42 fibril. This motif, which is trapped by the antibody, may provide the missing link in amyloid formation. Water molecules often bridge between the antibody and amyloid, contributing to the recognition. GENERAL SIGNIFICANCE: This paper provides the structural basis for antibody recognition of amyloidogenic proteins. The analysis and discussion of known structures are expected to help in the design and optimization of antibodies in neurodegenerative diseases. This article is part of a Special Issue entitled "System Genetics" Guest Editor: Dr. Yudong Cai and Dr. Tao Huang. |Amino Acid Sequence [MESH] |Amyloid/*chemistry/metabolism [MESH] |Antibodies/*chemistry/metabolism [MESH] |Humans [MESH] |Immunotherapy/methods [MESH] |Neurodegenerative Diseases/metabolism [MESH]Conformational selection in amyloid-based immunotherapy: Survey of cry(epmc).pdf DeepDyve Pubget Overpricing