BACKGROUND This study presents a case of rapidly developing respiratory failure due to antisynthetase syndrome(AS)following coronavirus disease 2019(COVID-19)in a 33-year-old man diagnosed with Klinefelter syndrome(KS...BACKGROUND This study presents a case of rapidly developing respiratory failure due to antisynthetase syndrome(AS)following coronavirus disease 2019(COVID-19)in a 33-year-old man diagnosed with Klinefelter syndrome(KS).CASE SUMMARY A 33-year-old man with a diagnosis of KS was admitted to the Department of Pulmonary and Critical Care Medicine of a tertiary hospital in China for fever and shortness of breath 2 wk after the onset of COVID-19.Computed tomography of both lungs revealed diffuse multiple patchy heightened shadows in both lungs,accompanied by signs of partial bronchial inflation.Metagenomic next-generation sequencing of the bronchoalveolar lavage fluid suggested absence of pathogen.A biopsy specimen revealed organizing pneumonia with alveolar septal thickening.Additionally,extensive auto-antibody tests showed strong positivity for anti-SSA,anti-SSB,anti-Jo-1,and anti-Ro-52.Following multidisciplinary discussions,the patient received a final diagnosis of AS,leading to rapidly progressing respiratory failure.CONCLUSION This study underscores the clinical progression of AS-associated interstitial lung disease subsequent to viral infections such as COVID-19 in patients diagnosed with KS.展开更多
Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,...Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,computational study,and X-ray structures.The turn loop of thisβ-hairpin motif accommodates different two-residueα-amino acid sequences from the highly flexible Gly-Gly,to the more restricted D-Pro-Gly.The presence ofα-amino acid side chains enhances the stabilities of theβ-hairpins with the exception of D-Pro-Gly-which results in destabilization.Based on this hairpin/turn motif,a variety of different dipeptide sequences ofα-amino acids which rarely occur inβ-turns can be introduced and presented as two-residue loops.展开更多
基金Supported by the Natural Science Foundation of Jiangxi Province,No.20202BAB206002 and No.20224BAB216084.
文摘BACKGROUND This study presents a case of rapidly developing respiratory failure due to antisynthetase syndrome(AS)following coronavirus disease 2019(COVID-19)in a 33-year-old man diagnosed with Klinefelter syndrome(KS).CASE SUMMARY A 33-year-old man with a diagnosis of KS was admitted to the Department of Pulmonary and Critical Care Medicine of a tertiary hospital in China for fever and shortness of breath 2 wk after the onset of COVID-19.Computed tomography of both lungs revealed diffuse multiple patchy heightened shadows in both lungs,accompanied by signs of partial bronchial inflation.Metagenomic next-generation sequencing of the bronchoalveolar lavage fluid suggested absence of pathogen.A biopsy specimen revealed organizing pneumonia with alveolar septal thickening.Additionally,extensive auto-antibody tests showed strong positivity for anti-SSA,anti-SSB,anti-Jo-1,and anti-Ro-52.Following multidisciplinary discussions,the patient received a final diagnosis of AS,leading to rapidly progressing respiratory failure.CONCLUSION This study underscores the clinical progression of AS-associated interstitial lung disease subsequent to viral infections such as COVID-19 in patients diagnosed with KS.
基金supported by the National Natural Science Foundation of China(No.21778012 to Z.L.Lu,21801020 to R.Liu)the American Chemical Society–Petroleum Research Fund(PRF#58364-ND7,to B.Gong)+1 种基金the Center for Computational Research(CCR)(to D.P.Miller and E.Zurek)Hofstra University(to D.P.Miller)。
文摘Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,computational study,and X-ray structures.The turn loop of thisβ-hairpin motif accommodates different two-residueα-amino acid sequences from the highly flexible Gly-Gly,to the more restricted D-Pro-Gly.The presence ofα-amino acid side chains enhances the stabilities of theβ-hairpins with the exception of D-Pro-Gly-which results in destabilization.Based on this hairpin/turn motif,a variety of different dipeptide sequences ofα-amino acids which rarely occur inβ-turns can be introduced and presented as two-residue loops.
