Publications by authors named "G S Talluri"

Purpose: We evaluated the immunological response in patients with hormone sensitive and refractory prostate cancer, and untreated benign prostatic hyperplasia (BPH).

Materials And Methods: Serum levels of pro-inflammatory and anti-inflammatory cytokines were measured by enzyme-linked immunosorbent assay in 3 groups of patients. The groups included 18 men with a mean age of 79 years who had hormone sensitive prostate cancer, mean prostate specific antigen (PSA) plus or minus standard deviation 1.

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Article Synopsis
  • Immunocompromised patients, including premature infants, the elderly, and HIV patients, face a heightened risk of fungal infections, which contribute to 8% of hospital-acquired infections.
  • Candidal species are the most common fungal pathogens, but other species like Aspergillus and Cryptococcus are also significant threats.
  • Environmental fungi such as Blastomyces, Coccidioides, and Histoplasma are increasing in aggressiveness towards vulnerable patients experiencing disseminated fungal infections.
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Purpose: We evaluated the immunological response in patients with persistent candiduria with or without occult candidemia.

Materials And Methods: Levels of Thl (pro-inflammatory interleukin [IL]-1, IL-2 and tumor necrosis factor-alpha) and Th2 (anti-inflammatory IL-4 and IL-10) cytokines were measured in the sera of patients with persistent candiduria. Polymerase chain reaction assessment of the 158 base pair candidal actin gene was used to detect Candida albicans in blood to identify occult candidemia.

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Objectives: Candiduria has been shown to be an early marker of disseminated fungal infection in critically ill patients who have undergone surgery. The management of candidemia and disseminated candidiasis depends on rapid and definitive identification of Candida. Routine or fungus-specific blood cultures are unreliable and require a large quantity of blood for incubation.

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We compared the conformation of empty and peptide-loaded class I major histocompatibility complex (MHC) molecules at the cell surface. Molecular conformations were analyzed by fluorescence resonance energy transfer (FRET) between fluorescent-labeled Fab fragments bound to the alpha 2 domain of the MHC heavy chain and fluorescent-labeled Fab fragments bound to beta 2-microglobulin. No FRET was found between Fab fragments bound to empty H-2Kb, but FRET was detected when empty H-2Kb molecules were loaded with peptide.

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