Objective. To investigate the validity of the 28-joint count for assessment of joint involvement in patients with rheumatoid arthritis (RA).Methods. Joint involvement as determined by the 28-and the 66/68-joint count was compared using data from 735 prospectively studied RA patients.Results. The joints included in the 28-joint count were more commonly involved than other joints, and findings from the 28-joint count correlated highly with those from the 66/68-joint count in all analyses.Conclusion. The 28-joint count is a reliable and valid measure for joint assessment. It is easier to perform than the 66/68-joint count, and it addresses the joints that are critically involved.

The traditional NMR-based method for determining oligomeric protein structure usually involves distinguishing and assigning intra-and intersubunit NOEs. This task becomes challenging when determining symmetric homo-dimer structures because NOE cross-peaks from a given pair of protons occur at the same position whether intra-or intersubunit in origin. While there are isotope-filtering strategies for distinguishing intra from intermolecular NOE interactions in these cases, they are laborious and often prove ineffectual in cases of weak dimers, where observation of intermolecular NOEs is rare. Here, we present an efficient procedure for weak dimer structure determination based on residual dipolar couplings (RDCs), chemical shift changes upon dilution, and paramagnetic surface perturbations. This procedure is applied to the Northeast Structural Genomics Consortium protein target, SeR13, a negatively charged Staphylococcus epidermidis dimeric protein (K d 3.4 6 1.4 mM) composed of 86 amino acids. A structure determination for the monomeric form using traditional NMR methods is presented, followed by a dimer structure determination using docking under orientation constraints from RDCs data, and scoring under residue pair potentials and shape-based predictions of RDCs. Validation using paramagnetic surface perturbation and chemical shift perturbation data acquired on sample dilution is also presented. The general utility of the dimer structure determination procedure and the possible relevance of SeR13 dimer formation are discussed.

Tenidap is a novel anti-rheumatic drug that combines cytokine modulation with cyclo-oxygenase inhibition. This 24-week, multicentre, double-blind, randomized study compared the clinical efficacy, biochemical effects and safety of tenidap 120 mg/day (once daily) with diclofenac 150 mg/day (50 mg t.i.d) in the treatment of 384 patients with active rheumatoid arthritis. After 24 weeks, improvement with tenidap was significantly greater than with diclofenac for all five primary efficacy parameters, two of the four secondary efficacy parameters and 11 of the 13 Arthritis Impact Measurement Scales assessments. The superior efficacy of tenidap was apparent after 4 weeks of treatment with further improvements observed by 24 weeks. The probability of discontinuation due to lack of efficacy was significantly greater in the diclofenac group. Tenidap but not diclofenac was associated with significant, rapid and sustained reductions in C-reactive protein and serum amyloid A levels and with a significant reduction in plasma interleukin-6. The nature and frequency of side-effects were similar in the two groups as was the discontinuation rate for treatment-related safety reasons. Tenidap was associated with an equal incidence of elevated transaminases, but a higher incidence of mild (> or = 500 mg/24 h < 1500 mg/24 h) non-progressive, proteinuria of proximal tubular origin compared with diclofenac.

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