Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0038362 (
stomatitis
)
8,852
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
(-)-5'-noraristeromycin (1) has shown antiviral activity towards, particularly cytomegalovirus, vaccinia virus and measles while its (+)-enantiomer (2) is effective towards hepatitis B virus. To determine if the antiviral characteristics of 1 and 2 extended to the guanine analogues (3 and 4), these enantiomers were prepared and evaluated against herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2), cytomegalovirus (CMV), varicella zoster virus (VZV), Epstein-Barr virus (EBV), human herpes virus type 6 (HHV-6), human herpes virus type 8 (HHV-8), vaccinia virus (VV), cowpox virus (CV), vesicular
stomatitis
virus (VSV), respiratory syncytial virus (RSV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2). The only activity found for 3 was for Epstein-Barr virus in VCA Elisa (EC50 0.78 microg/mL), immunofluorescence assay for VCA or gp 350/250 (1.8-4.0 microg/mL) and DNA hybridization (EC50 0.82 microg/mL) assays with no accompanying toxicity seen in the host
Daudi
cells. No activity was noted for 4.
...
PMID:The enantiomers of carbocyclic 5'-norguanosine: activity towards Epstein-Barr virus. 1183 94
Interferon-alpha (IFNalpha), a cytokine with modulatory activities on many cell types, is useful for treating many types of cancer and infectious diseases. This study investigates whether modification of a protein, using IFNalpha as an example, with a lipophilic group can alter its distribution and kinetic properties in the body. Ser163 of IFNalpha2a was mutated to Cys to generate a free sulfhydryl group for site-specific chemical modification. IFNalpha2a(S163C) was conjugated by iodoacetamide derivatives of varying lengths, and the modified IFNalpha2a was purified by gel filtration chromatography. The biological activities of IFNalpha2a(S163C) and lipophilized IFNalpha2a(S163C) were similar to that of IFNalpha2a, as evidenced by their inhibitory effects on the growth of
Daudi
cells and on the replication of vesicular
stomatitis
virus in Madin-Darby bovine kidney cells. Lipophilized IFNalpha2a(S163C) bound to human serum albumin and cell membranes more readily than did IFNalpha2a. Future experiments will investigate whether lipophilized IFNalpha2a(S163C) has improved pharmacokinetic properties.
...
PMID:Site-specific lipophilic modification of interferon-alpha. 1249 47
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