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Research diagnostic criteria for temporomandibular disorders: a calibration and reliability study

Schmitter, Marc; Ohlmann, Brigitte; John, Mike T; Hirsch, Christian; Rammelsberg, Peter
The aim of this study was to investigate the reliability between different examiners when using the axis I of the Research Diagnostic Criteria for Temporomandibular Disorders (RDC/TMD). The hypothesis was that the standardized RDC/TMD examination protocol enables calibrated examiners to evaluate all examination items reliably. After calibration training by the RDC/TMD calibration team including the calibration of palpation pressure and the performance of the standardized examination protocol, four examiners, blinded to the patients' medical histories examined 24 subjects in a randomized sequence. One experienced examiner was the standard (hierarchical calibration). The recorded measurements strictly followed the RDC/TMD. Intraclass correlation coefficients (ICC), bias and precision were calculated to estimate interrater reliability. Acceptable (0.75 > or = CC > 0.4) to excellent (ICC > 0.75) reliability was found for 20 of the 23 (87%) examinations. Only sub-retromandibular muscle palpation and joint sound vibration recordings on lateral excursion showed poor-results (ICC < or = 0.4). The RDC/TMD examination protocol enables calibrated examiners to perform most (87%) examination items with satisfactory reliability. Therefore multi-site studies based on the RDC/TMD examination protocol may become feasible, keeping in mind the unsatisfactory reliability of 13% of the items (clicking during laterotrusion to the ipsilateral side, palpation of the posterior and submandibular region).
PMID: 16128356
ISSN: 0886-9634
CID: 155586

Yeast N-glycanase distinguishes between native and non-native glycoproteins

Hirsch, Christian; Misaghi, Shahram; Blom, Daniël; Pacold, Michael E; Ploegh, Hidde L
N-glycanase from Saccharomyces cerevisiae (Png1) preferentially removes N-glycans from misfolded proteins. The ability of Png1 to distinguish between folded and misfolded glycoproteins is reminiscent of substrate recognition by UDP-glucose glycoprotein glucosyl transferase, an enzyme that possesses this trait. The only known in vivo substrates of Png1 are aberrant glycoproteins that originate in the endoplasmic reticulum, and arrive in the cytoplasm for proteasomal degradation. The substrate specificity of Png1 is admirably suited for this task.
PMCID:1298977
PMID: 14726951
ISSN: 1469-221x
CID: 2981442