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Daniel L. Crimmins

Researcher at Washington University in St. Louis

Publications -  9
Citations -  683

Daniel L. Crimmins is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Glymphatic system & Gel electrophoresis. The author has an hindex of 7, co-authored 9 publications receiving 582 citations.

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Neurogranin as a Cerebrospinal Fluid Biomarker for Synaptic Loss in Symptomatic Alzheimer Disease

TL;DR: Neurogranin is a promising biomarker for AD because levels were elevated in patients with AD compared with cognitively normal participants and predicted progression from MCI to AD, and within-person levels of NGRN increased in cognitivelynormal participants but not in Patients with later stage MCI or AD, which suggests that N GRN may reflect presymptomatic synaptic dysfunction or loss.
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Recommendations for the Generation, Quantification, Storage, and Handling of Peptides Used for Mass Spectrometry–Based Assays

TL;DR: The Clinical Proteomic Tumor Analysis Consortium of the National Cancer Institute has collaborated with clinical laboratorians, peptide manufacturers, metrologists, representatives of the pharmaceutical industry, and other professionals to develop a consensus set of recommendations for peptide procurement, characterization, storage, and handling.
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Obstructive sleep apnea decreases central nervous system-derived proteins in the cerebrospinal fluid.

TL;DR: It is hypothesized that one mechanism underlying the association between obstructive sleep apnea (OSA) and Alzheimer's disease is OSA leading to decreased slow wave activity (SWA), increased synaptic activity, decreased glymphatic clearance, and increased amyloid‐β.
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Decay Accelerating Activity of Complement Receptor Type 1 (CD35): TWO ACTIVE SITES ARE REQUIRED FOR DISSOCIATING C5 CONVERTASES *

TL;DR: Results indicate that, for the C5 convertases, decay accelerating activity is mediated primarily by site 1, and a properly spaced site 2 has an important auxiliary role, which may involve its C3b binding capacity.
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A simple in situ cyanogen bromide cleavage method to obtain internal amino acid sequence of proteins electroblotted to polyvinyldifluoride membranes

TL;DR: A simple method to obtain internal amino acid sequences from larger proteins electroblotted to polyvinyldifluoride membranes and subjected to gas-phase microsequence analysis is reported.