Single-row versus transosseous technique in the arthroscopic treatment of rotator cuff tears: a meta-analysis.

PURPOSE: This study aims to compare single-row suture-anchors (SA) versus transosseous arthroscopic (TO) technique in the treatment of patients with rotator cuff tears in terms of clinical structural outcomes at atleast 24 months of follow-up. METHODS: The systematic review was performed according to "PRISMA guidelines" (Preferred Reporting Items for Systematic Reviews and Meta-analyses), in order to identify all the studies comparing clinical, both subjective and objective, outcomes with 24 months follow-up minimum in patients undergoing arthroscopic RC repair with the SR and TO technique. OVID-MEDLINE®, Cochrane, SCOPUS and PubMed were searched from January 2010 to October 2022 to identify relevant studies, using the following key words, that were combined together to achieve maximum search strategy sensitivity: "Rotator cuff tear" OR "repair" OR "shoulder" OR "reconstruction" OR "suture" OR "arthroscopic" OR "single-row" OR "transosseous". RESULTS: Six papers were finally analyzed in this meta-analysis. The weighted mean difference on Constant scores and for ASES for studies considering suture-anchors (SA) group showed good outcomes. The weighted mean difference of Constant scores and of ASES for TO (transosseous) group showed good outcomes. The weighted mean difference of CONSTANT for TO versus SA groups showed no differences in the outcomes of SA and TO techniques for the repair of Rotator Cuff Tears at minimum 24 months follow-up. CONCLUSIONS: The Arthroscopic transosseous rotator cuff repair technique and SA (suture-anchor) technique both lead to significant short-term improvement and satisfactory subjective outcome scores with low complication/failure rates. No differences were found in the final outcome between the two techniques.

Heptad-repeat regions of respiratory syncytial virus F1 protein form a six-membered coiled-coil complex.

The Respiratory Syncytial Virus (RSV) fusogenic glycoprotein F(1) was characterized using biochemical and biophysical techniques. Two heptad-repeat (HR) regions within F(1) were shown to interact. Proteinase-K digestion experiments highlight the HR1 region (located proximal to the fusion peptide sequence) of the F(1) protein to which an HR2-derived (located proximal to the membrane-spanning domain) peptide binds, thus protecting both the protein and peptide from digestion. Solution-phase analysis of HR1-derived peptides shows that these peptides adopt helical secondary structure as measured by circular dichroism. Sedimentation equilibrium studies indicate that these HR1 peptides self-associate in a monomer/trimer equilibrium with an association constant of 5.2 x 10(8) M(-2). In contrast, HR2-derived peptides form random monomers in solution. CD analysis of mixtures containing peptides from the two regions demonstrate their propensity to interact and form a very stable (T(m) = 87 degrees C), helical (86% helicity) complex comprised of three HR1 and three HR2 members.