Cyclized Peptide derived from Myelin P2   Open Access Molecule: peptide derived from myelin P2
Cyclized Peptide derived from CRABP   Open Access Molecule: peptide derived from CRABP
picornavirus correlates   Monograph: structural correlates of MS and paralysis
SEI cell entry binding domain and corresponding residues found in N10 and N11   Paper: cell entry domains in influenza neuraminidases

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Molecules MS-BLOCK compounds are Open Access Molecules.

MS-BLOCK peptides present the residues in the feature that are common to TMEV, myelin P2, and CRABP. These peptides are expected to bind antibodies to any of the myelin P2-like helices (the “MS Epitope”) or CRABP-like helices found on the diverse set of picornaviruses studied. Sequences are given for two MS-BLOCK cyclized peptides derived, separately, from myelin P2 protein and CRABP. Clinical applications for these MS-BLOCK peptides may potentially include detection and treatment of multiple sclerosis (MS) and amyotrophic lateral sclerosis (ALS).

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picornavirus correlates Common Features in Picornaviruses, Alpha-bungarotoxin, Myelin P2, and CRABP Suggest Structural Bases for Multiple Sclerosis, Guillain-Barré Syndrome, and Paralysis Induction (HTML)  (12 MB PDF)  (6 MB PDF)

We found the structural correlates of multiple sclerosis induction and paralysis induction in picornaviruses and proteins. We identified in picornaviruses what appears to be an ion channel and, separately, a diaphragm shutter-like pore. This study provides an analytic procedure for understanding the structural context of expanded tissue preferences and pathology in historical and emergent viruses.

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 Published Papers 

neuraminidase paper at Weininger A, Weininger S. (2015) Using Common Spatial Distributions of Atoms to Relate Functionally Divergent Influenza Virus N10 and N11 Protein Structures to Functionally Characterized Neuraminidase Structures, Toxin Cell Entry Domains, and Non-Influenza Virus Cell Entry Domains.

PloS One 10(2):e0117499. (


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Understanding the Basis of Disease and Finding Reliable, Druggable Targets Cambridge Cheminformatics Meeting
Cambridge University
7 December 2016

Understanding the Basis of Disease and Finding Reliable, Druggable Targets (PDF)

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