Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P05109 (S100A8)
 1,212 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The authors determined the sequences of the LTR region of Ethiopian HIV-1 subtype C strains and compared them with Swedish HIV-1 subtype B strains and earlier published data. Peripheral blood mononuclear cells (PBMCs) were obtained from seven randomly chosen HIV-1 infected Ethiopian patients, all with pre-AIDS or AIDS. PBMCs were also obtained from three Swedish HIV-1 subtype B-infected patients. Extraction of HIV-1 DNA was performed with the phenol-chloroform plus ethanol precipitation method. In all the Ethiopian HIV-1 subtype C strains, the first five nucleotides were changed to (G/A)CAGA, a finding not observed in the Swedish subtype B strains sequenced at the same time. The most remarkable feature of the Ethiopian NF-KB region was the presence of what appears to be an extra site located upstream of the usual sites I and II. At the same time, the core enhancer sequence GGGACTTTCC at site I was modified by a deletion of the A nucleotide and a change of the first T to a G. The gross LTR organization may be radically different in "African" subtype HIV-1 isolates compared to the American/European HIV-1 subtype B prototype strains. These data from the Ethiopian strains reinforce the validity of this conclusion.
 ...
PMID:Multiple enhancer motifs in HIV type 1 strains from Ethiopia. 757 37

Antibacterial peptides were isolated from human peripheral granulocytes of a healthy donor who had been treated with granulocyte-colony stimulating factor (G-CSF) and cortisol. Peptides were solubilized in acidified chloroform/methanol, and partitioned in chloroform/methanol/water. Water- soluble polypeptides were separated by cation-exchange and reversed-phase chromatography. Several previously characterized antibacterial polypeptides were identified; defensins 1-3, defensin 4, lysozyme, eosinophil cationic protein, and calgranulin A. In addition, several histone fragments were isolated and exhibited activity against the Gram- positive bacterium Bacillus megaterium strain Bm11. These fragments included two C-terminal fragments of histone H1A, three C-terminal fragments of histone H1D, one fragment of histone H1B, and two fragments of histone H4. The molecular masses of both histone H1A fragments, as determined by electrospray (ES) MS, were 270 Da higher than those calculated from their amino acid sequences. The two histone H1A fragments corresponded to Lys152-Lys222 (7527 +/- 1 Da) and Lys167-Lys222 (6023 +/- 1 Da). Tandem MS (MS/MS) of the 7.5 kDa and 6.0 kDa fragments indicated that the post-translational modification is on Lys222, the epsilon-amino group of which was conjugated with the alpha-carboxyl group of the tripeptide Arg-Gly-Gly. This finding was substantiated by digestion of the 7.5-kDa polypeptide with trypsin and analysis of the resulting peptides by ES MS and MS/MS. The tripeptide Arg-Gly-Gly corresponded uniquely to the three C-terminal residues of ubiquitin, demonstrating the presence of ubiquitinated histone H1A.
 ...
PMID:Antibacterial peptides in stimulated human granulocytes: characterization of ubiquitinated histone H1A. 1185 9