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Penile fracture, resulting from trauma to an erect penis, is a rare urogenital injury with potentially serious complications including erectile dysfunction. This case report emphasizes the significance of prompt recognition, accurate diagnosis, and timely surgical management to optimize patient outcomes. The case involves a 34-year-old male presenting with acute pain, swelling, and a visibly deformed penis following sexual intercourse. Clinical examination confirmed the diagnosis of penile fracture, leading to surgical repair of the tunica albuginea. The patient had an uneventful post-operative recovery and received appropriate post-operative instructions. A penile fracture is a rare but serious injury occurs due to a tear in the tunica albuginea that can occur during vigorous sexual activity causing sudden pain, swelling, and produce a popping sound. Classical presentation often leads to establish a clinical diagnosis. However, immediate surgical exploration and repair is needed for better outcomes and to prevent long term complications such as erectile dysfunction or curvature of the penis that are associated with relying solely on conservative management. Delayed presentation also affects the optimal outcomes of surgery. This report highlights the importance of early surgical intervention, the impact of delayed presentation, and the need for increased awareness regarding penile fractures. This case adds to the existing surgical literature by providing insights into the clinical presentation and management of penile fractures. The comprehensive overview of the case contributes to a better understanding of penile fractures and their management, helping healthcare professionals, improves patient care and outcomes. • Prompt recognition and accurate diagnosis of penile fracture are crucial for optimal patient outcomes, emphasizing the importance of early surgical intervention. • This case report underscores the significance of timely surgical management and highlights the impact of delayed presentation on patient prognosis. • Insights from this case contribute to a better understanding of penile fractures, increasing awareness among healthcare professionals and improving patient care and outcomes. [ABSTRACT FROM AUTHOR]

The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn2+-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum. [ABSTRACT FROM AUTHOR]

The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn2+-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum. [ABSTRACT FROM AUTHOR]

Background: Lateral internal sphincterotomy (LIS) has been the gold standard for treating chronic anal fissure (CAF) that persists despite other measures. The authors aim to evaluate the effects of the close method (CLIS) of performing LIS as compared to the open method (OLIS)., Methods: Databases were searched for relevant studies and results were screened to identify eligible articles, and all concerned outcomes were pooled as odd ratio (OR) or mean difference (MD) with 95% CI in the meta-analysis models using RevMan 5.4., Results: Pooled data from 16 trials with 1,711 patients with idiopathic CAF showed that the CLIS has significant lower risk of delayed fissure healing [OR: 0.28, 95% CI (0.10, 0.77), P = 0.01], duration of hospital stay [MD: -0.82 with 95% CI (-1.07, -0.57), P < 0.00001] and postoperative visual analogue pain score (VAPS) at 24 h [MD: -0.30 with 95% CI (-0.39, -0.21), P < 0.00001]. Also, the risk of overall complications [OR: 0.33 with 95% CI (0.19, 0.55), P < 0.0001], incontinence [OR: 0.28 with 95% CI (0.20, 0.38), P < 0.00001], and postoperative pain [OR: 0.56 with 95% CI (0.35, 0.91), P = 0.02] was significantly lower with CLIS., Conclusion: CLIS is a safer option than OLIS for treating anal fissure. The risk of delayed fissure healing, incontinence, post-op pain and overall complication was significantly lower. However, the risk of surgical site infection, postoperative bleeding and recurrence did not differ. Future research with more prolonged follow-up is necessary to document recurrence reliably., Competing Interests: The author declared no conflicts of interest.Sponsorships or competing interests that may be relevant to content are disclosed at the end of this article., (Copyright © 2023 The Author(s). Published by Wolters Kluwer Health, Inc.)

The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn(2+)-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum.