ライフサイエンスコーパス: staphylococcal protein A

1 involvement of wall teichoic acid but not of staphylococcal protein A.

2 of the common model protein, the B domain of staphylococcal protein A.

3 tal NOESY data on the 58-residue Z domain of staphylococcal protein A.

4 with the binding of von Willebrand factor to staphylococcal protein A.

5 2 plus CH3) to facilitate purification using staphylococcal protein A.

6 ach containing a VH domain and a B domain of staphylococcal protein A.

7 inhibited by fibronectin and did not bind to staphylococcal protein A.

8 ts the 46-residue segment from fragment B of staphylococcal protein A.

9 sferase, to IgG binding domains derived from staphylococcal protein A.

10 ons were further characterized by binding to staphylococcal protein A.

11 lococcal strains also secreted extracellular staphylococcal protein A.

12 tudy the folding pathways of the B-domain of staphylococcal protein A (1BDD (alpha; 46 residues)).

13 omains of streptococcal protein G (G(B)) and staphylococcal protein A (A(B)).

14 Thus, staphylococcal protein A, alpha-toxin, and superantigeni

15 of surface proteins, we analyzed variants of staphylococcal protein A, an immunoglobulin binding prot

16 nce of the VH-restricted Fab binding site on staphylococcal protein A and demonstrate the diverse eff

17 Targeting staphylococcal protein A and stimulating the T-helper 17

18 t gC1qR as a novel cellular binding site for staphylococcal protein A and suggest an additional mecha

19 The B domain of staphylococcal protein A (BdpA) is a small helical prote

20 A and B, and exfoliative toxin-A, as well as staphylococcal protein A, did not induce significant cyt

21 applied here to compute folding pathways of staphylococcal protein A, fragment B.

22 Staphylococcal protein A gene (spa) typing identified sp

23 cluded multilocus sequence typing (MLST) and staphylococcal protein A gene (spa) typing results as we

24 ace of the 10-55 fragment of the B-domain of staphylococcal protein A has been investigated by using

25 The folding of the B-domain of staphylococcal protein A has been studied by coarse-grai

26 utations on binding of Fc hinge fragments to staphylococcal protein A have also been analyzed and dem

27 In this study we show that staphylococcal protein A induces T cell-independent huma

28 l, but not complete, overlap of the FcRn and staphylococcal protein A interaction sites on mouse IgG1

29 The E-domain of staphylococcal protein A is one of five homologous IgG-b

30 Microcolumns of staphylococcal protein A linked to Sepharose were used t

31 treated neonatal BALB/c mice with a form of staphylococcal protein A (MS) devoid of Fcgamma binding

32 he sGM-CSFRalpha-Fc was bound to immobilized staphylococcal protein A on the biosensor surface, and b

33 ied to the 10-55 fragment of the B-domain of staphylococcal protein A (protein A) and to a 75-residue

34 ion studies performed on serum samples using staphylococcal protein A-Sepharose indicated that antibo

35 The antibody binding properties of staphylococcal protein A (SpA) can be attributed to the

36 The staphylococcal protein A (spa) gene was sequenced for al

37 Staphylococcal protein A (SPA) is a B cell superantigen

38 Staphylococcal protein A (SpA) is a cell-surface compone

39 Staphylococcal protein A (SpA) is a cell-wall-bound path

40 Staphylococcal protein A (Spa) is an important virulence

41 Staphylococcal protein A (SpA) is an important virulence

42 Staphylococcal protein A (SpA) is anchored to the cell w

43 Staphylococcal protein A (SpA) is representative of a ne

44 Staphylococcal protein A (SpA) is representative of a ne

45 lls and a murine model of RA, the ability of staphylococcal protein A (SPA) to interact with and modu

46 bility testing and characterization of their staphylococcal protein A (spa) type.

47 All S. aureus isolates were genotyped by staphylococcal protein A (spa) typing and with multilocu

48 enotype by pulsed-field gel electrophoresis, staphylococcal protein A (spa) typing, multilocus sequen

49 ntibiotic susceptibility, biofilm formation, Staphylococcal protein A (spa) typing, SCCmec typing, an

50 FGE), multilocus sequence typing (MLST), and staphylococcal protein A (spa) typing.

51 Staphylococcal protein A (SPA) was used to modify the si

52 3, V(H)3-30, or V(H)3-30.3), and/or modified staphylococcal protein A (SpA), a 45-kilodalton bacteria

53 Staphylococcal protein A (SpA), a bacterial membrane pro

54 d antigen presentation to CD4(+) T cells and staphylococcal protein A (SpA), a cell wall-anchored sur

55 Staphylococcal protein A (SpA), acting as a B cell super

56 the lactose operon (lac) and genes encoding staphylococcal protein A (spa), gamma hemolysin (hlg), a

57 The envelope of S. aureus is decorated with staphylococcal protein A (SpA), which captures the Fcgam

58 g salivary immunoglobulins was identified as staphylococcal protein A (SpA).

59 eins, including the lung inflammatory factor staphylococcal protein A (Spa).

60 e polypeptide (ELP) and the antibody-binding staphylococcal protein A (SpA).

61 duct was a fusion protein with a B domain of Staphylococcal protein A (SPA).

62 4 fused to the soluble IgG-binding domain of staphylococcal protein A) suggest that the transmembrane

63 lates were found to express higher levels of staphylococcal protein A than the TSS isolates, another

64 as for the 46-residue N-terminal fragment of staphylococcal protein A, the native-like conformation w

65 s(-1)), the involvement of platelet gpIb and staphylococcal protein A through von Willebrand factor b

66 We have characterized the in vivo effect of staphylococcal protein A treatment on peripheral B cells

67 Injection of homogenous staphylococcal protein A-V antigen fusion peptide into m

68 eviously showed that injection of homogenous staphylococcal protein A-V antigen fusion peptide into m

69 ted-residue force field, for the B domain of staphylococcal protein A, we are able to (i) provide the

70 laxation kinetics studies of the B-domain of staphylococcal protein A were performed to characterize

71 al pathogens produce virulence factors, like staphylococcal protein A, which interact at high frequen