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A second serine protease associated with mannan-binding lectin that activates complement
MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway.
Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata
OmCI is the first lipocalin family member shown to inhibit C and also the first natural inhibitor that specifically targets the C5 activation step.
The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha.
- B. Berks, D. Richardson, A. Reilly, A. Willis, S. Ferguson
- Biology, ChemistryThe Biochemical journal
- 1 August 1995
The napEDABC locus coding for the periplasmic nitrate reductase of Thiosphaera pantotropha has been cloned and sequenced, and the DNA- and protein-derived primary sequence of NapB confirm that this protein is a dihaem c-type cytochrome and, together with spectroscopic data, indicate that both NapB haems have bis-histidine ligation.
The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL.
This is the first observation that a molecular chaperone has the capacity to stimulate the breakdown of connective tissue and the GroEL protein from E. coli showed activity in the bone resorption assay.
Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis
Using [gamma-32P]ATP to phosphorylate SpoIIAA, cleaving the protein proteolytically, and analyzing the one resulting radiolabelled peptide by the Edman degradation procedure, it is shown that the site of phosphorylation in SpoI IAA is Ser-58.
Structure and homology of human C1q receptor (collectin receptor).
The data obtained indicate that C1qR and the reported calreticulin/RoSSA component are similar but not identical molecules, which belong to the same protein superfamily.
Structure refinement of commensurately modulated bismuth titanate, Bi4Ti3O12
Bi 4 Ti 3 O 12 dont les parametres sont a=5,450, b=5,4059, c=32,832 A, β=90,00°, Z=4; affinement jusqu'a R=0,0177. Il peut se decrire comme une modulation commensurable d'une structure parent F.…
Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.
- S. Baker, N. Saunders, A. Willis, S. Ferguson, J. Hajdu, V. Fülöp
- ChemistryJournal of molecular biology
- 13 June 1997
From sequencing the nirS gene of Thiosphaera pantotropha, it is established that the amino acid sequence deduced previously in part from X-ray diffraction data at lower resolution was largely correct, as was the proposal that eight N-terminal amino acid residues were not seen in the structure.