Results 151 to 160 of about 108,443 (306)
PHAGOCYTOSIS OF CRYPTOCOCCUS NEOFORMANS IN ANEMIC MICE [PDF]
H. H. Gadebusch
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Analysis of sphingolipids, sterols, and phospholipids in human pathogenic Cryptococcus strains[S]
Cryptococcus species cause invasive infections in humans. Lipids play an important role in the progression of these infections. Independent studies done by our group and others provide some detail about the functions of these lipids in Cryptococcus ...
Ashutosh Singh+3 more
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Microevolution of Serial Clinical Isolates of Cryptococcus neoformans var. grubii and C. gattii
The pathogenic species of Cryptococcus are a major cause of mortality owing to severe infections in immunocompromised as well as immunocompetent individuals.
Yuan Chen+13 more
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PREVALENCE OF CRYPTOCOCCAL MENINGITISINATERTIARY CARE CENTRE [PDF]
Background: Cryptococcal meningitis has emerged as an important opportunistic central nervous system (CNS) infection in Human Immunodeficiency Virus (HIV) positive patients. It is associated with a high mortality rate.
Ashish Bajaj1, Bibhabati Mishra2, Poonam S Loomba2, Archana Thakur3, Abha Sharma4, Prachala G Rathod1, Madhusmita Das1, Ashna Bhasin1
doaj
Present and Future Therapy of Cryptococcus Infections
Cryptococcal infections burden the immunocompromised population with unacceptably high morbidity and mortality. This population includes HIV-infected individuals and those undergoing organ transplants, as well as seemingly immunocompetent patients (non ...
A. Mourad, J. Perfect
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Cryptococcus and Phagocytes: Complex Interactions that Influence Disease Outcome
Cryptococcus neoformans and C. gattii are fungal pathogens that cause life-threatening disease. These fungi commonly enter their host via inhalation into the lungs where they encounter resident phagocytes, including macrophages and dendritic cells, whose
Chrissy M Leopold Wager+3 more
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Xylosyltransferases in Cryptococcus laurentii
Abstract A particle-bound enzyme preparation from the fungus imperfectus, Cryptococcus laurentii, contains at least two different xylosyltransferases. One of these catalyzes the transfer of xylosyl units from UDP-xylose to endogenous cell envelope glycoproteins.
John S. Schutzbach, Helmut Ankel
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