Explore the vast range of titles available.

Introduction This study endeavors to evaluate the frequency of programmed death-ligand 1 (PD-L1) expression in oral squamous cell carcinoma (OSCC) specimens and to correlate these findings with clinicopathological features of established prognostic significance. Methodology The study included paired pre-surgical biopsy and resection specimens from 35 patients with OSCC. Immunohistochemistry was performed for PD-L1 (clone SP263) with 51.4% tumor proportion score (TPS) and 77.1% combined proportion score (CPS), which was assessed at a cut-off of ≥1%. The association of the mean expression of the biomarker with clinicopathological parameters has been evaluated. Results TPS of PD-L1 expression at the cut-offs of ≥1%, ≥10%, ≥25%, and ≥50%, and the positivity rates were 20% (7/35), 8.6% (3/35), 8.6% (3/35), and 14.3% (5/35), respectively. The CPS at the same cut-offs were 22.9%, 31.4%, 17.1%, 11.4%, and 17.1%, respectively. TPS was significantly correlated with stage ( = 0.01), while CPS was associated with perineural invasion ( = 0.04) and showed increased expression in the male population ( < 0.05). Conclusions This study highlights the significance of a larger/resection specimen over a small biopsy for PD-L1 evaluation. Increased PD-L1 expression observed in higher-stage disease, perineural invasion (PNI), and male patients can be validated in a larger cohort and potentially guide the use of anti-PD-L1 therapy in OSCC.

The fidelity of the folding pathways being encoded in the amino acid sequence is met with challenge in instances where proteins with no sequence homology, performing different functions and no apparent evolutionary linkage, adopt a similar fold. The problem stated otherwise is that a limited fold space is available to a repertoire of diverse sequences. The key question is what factors lead to the formation of a fold from diverse sequences. Here, with the NAD(P)-binding Rossmann fold domains as a case study and using the concepts of network theory, we have unveiled the consensus structural features that drive the formation of this fold. We have proposed a graph theoretic formalism to capture the structural details in terms of the conserved atomic interactions in global milieu, and hence extract the essential topological features from diverse sequences. A unified mathematical representation of the different structures together with a judicious concoction of several network parameters enabled us to probe into the structural features driving the adoption of the NAD(P)-binding Rossmann fold. The atomic interactions at key positions seem to be better conserved in proteins, as compared to the residues participating in these interactions. We propose a \"spatial motif\" and several \"fold specific hot spots\" that form the signature structural blueprints of the NAD(P)-binding Rossmann fold domain. Excellent agreement of our data with previous experimental and theoretical studies validates the robustness and validity of the approach. Additionally, comparison of our results with statistical coupling analysis (SCA) provides further support. The methodology proposed here is general and can be applied to similar problems of interest.

The fidelity of the folding pathways being encoded in the amino acid sequence is met with challenge in instances where proteins with no sequence homology, performing different functions and no apparent evolutionary linkage, adopt a similar fold. The problem stated otherwise is that a limited fold space is available to a repertoire of diverse sequences. The key question is what factors lead to the formation of a fold from diverse sequences. Here, with the NAD(P)-binding Rossmann fold domains as a case study and using the concepts of network theory, we have unveiled the consensus structural features that drive the formation of this fold. We have proposed a graph theoretic formalism to capture the structural details in terms of the conserved atomic interactions in global milieu, and hence extract the essential topological features from diverse sequences. A unified mathematical representation of the different structures together with a judicious concoction of several network parameters enabled us to probe into the structural features driving the adoption of the NAD(P)-binding Rossmann fold. The atomic interactions at key positions seem to be better conserved in proteins, as compared to the residues participating in these interactions. We propose a \"spatial motif\" and several \"fold specific hot spots\" that form the signature structural blueprints of the NAD(P)-binding Rossmann fold domain. Excellent agreement of our data with previous experimental and theoretical studies validates the robustness and validity of the approach. Additionally, comparison of our results with statistical coupling analysis (SCA) provides further support. The methodology proposed here is general and can be applied to similar problems of interest.