ライフサイエンスコーパス: aerolysin

1 aerolysin; thus, PNH cells are resistant to aerolysin.

2 amino acid inside the sensing region of the aerolysin.

3 s, are resistant to the cytotoxic effects of aerolysin.

4 hrax lethal toxin and the pore-forming toxin aerolysin.

5 xin, a protease, and the hole-forming toxin, aerolysin.

6 a nanometer-scale pore formed by the protein aerolysin.

7 in methylcellulose containing toxic doses of aerolysin (1 x 10(-9) M).

8 cells differed markedly in susceptibility to aerolysin (a bacterial toxin that binds to GPI-anchored

9 The mutant cells are also resistant to aerolysin, a channel-forming protein secreted by Aeromon

10 is vacuolation was related to that caused by aerolysin, a pore-forming toxin of Aeromonas; it involve

11 rsensitivity of baby hamster kidney cells to aerolysin, a pore-forming toxin that targets humans.

12 Importantly, the use of aerolysin allowed us to detect PNH populations that coul

13 Resistance of PNH cells to aerolysin allows for a simple, inexpensive assay for PNH

14 a protein, probed by two protein nanopores: aerolysin and alpha-hemolysin.

15 D is required for extracellular secretion of aerolysin and protease, indicating that tapD may play an

16 nanopore engineering for biosensing, making aerolysin applicable in genetic and epigenetic detection

17 which severely lowers the sensitivity of an aerolysin-based genetic biosensor.

18 We conclude that alpha toxin, like aerolysin, binds to GPI-anchored protein receptors.

19 s those of beta-pore-forming toxins, such as Aerolysin, but is devoid of a receptor-binding domain.

20 that distinct current blockades in wild-type aerolysin can be used to identify 13 of the 20 natural a

21 with the GPI-anchor-reactive bacterial toxin aerolysin enriched for the GPI-anchor- populations.

22 The percentage of lysis of PNH cells after aerolysin exposure paralleled the percentage of CD59(+)

23 Etx is a member of the aerolysin family of beta-PFTs (abeta-PFTs).

24 tebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes ma

25 the earthworm Eisenia fetida belongs to the aerolysin family of small beta-pore-forming toxins (beta

26 Examination of other members of the aerolysin family reveals high structural preservation in

27 nchor markers, CD59 and a GPI-binding toxin, aerolysin (FLAER), confirming the pathogenicity of the m

28 its functional and sequence similarity with aerolysin, for which the crystal structure has been dete

29 hat two other bacterial pore-forming toxins (aerolysin from Aeromonas species and alpha-toxin from St

30 r+ cells in the Mut lines and analyses using aerolysin in conjunction with flow cytometry yielded PIG

31 l-characterized bacterial pore-forming toxin aerolysin in single cells in real time to determine the

32 -operate approach to noncovalently transform aerolysin into a highly nucleic acids-sensitive nanopore

33 Aerolysin is a beta-pore-forming toxin produced by most

34 Aerolysin is a channel-forming toxin secreted by Aeromon

35 Aerolysin is a toxin secreted by the bacterial pathogen

36 Here, we show that aerolysin is capable of neutralizing HIV-1 in a dose-dep

37 y lower the pH on one side of the pore, then aerolysin is immediately "activated" and enabled to capt

38 al domain shows structural homology with the aerolysin-like beta-pore-forming family of proteins.

39 ium perfringens epsilon toxin belongs to the aerolysin-like family of pore-forming toxins and is one

40 stridium septicum that belongs to the unique aerolysin-like family of pore-forming toxins.

41 vated pore-forming toxin that belongs to the aerolysin-like family of toxins.

42 ucturally similar proteins, belonging to the aerolysin-like family, are present throughout all kingdo

43 the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represen

44 Megalopygid venoms consist of large aerolysin-like pore-forming toxins, which we have named

45 Megalopygids have recruited aerolysin-like proteins as venom toxins convergently wit

46 We illustrate this by optimizing an aerolysin mutant for computing applications.

47 The fragments identified with the aerolysin nanopore are consistent with the predicted fra

48 cular dynamics simulations revealed that the aerolysin nanopore has a built-in single-molecule trap t

49 f all twenty proteinogenic amino acids in an aerolysin nanopore with the help of a short polycationic

50 In this paper, taking aerolysin nanopores as an example, we calculate and comp

51 Through extensive mutation analysis of aerolysin nanopores, we demonstrate that open-pore recti

52 A protein of this same size was found in aerolysin overlays used to detect GPI-anchored proteins.

53 high-resolution atomic cryo-EM structures of aerolysin prepore and pore in a membrane-like environmen

54 Aerolysin protein pore has been widely used for sensing

55 eal isolate, SSU, of Aeromonas hydrophila is aerolysin related and crucial to the pathogenesis of Aer

56 An aerolysin-related cytotoxic enterotoxin (Act) of Aeromon

57 The frequency of aerolysin resistant CFC was 14.7 +/- 4.0 x 10(-6) in the

58 DNA was extracted from individual day-14 aerolysin-resistant CFCs and the PIG-A gene was sequence

59 Aerolysin-resistant CFCs from patients with PNH exhibite

60 Aerolysin should also be useful in studying PNH biology.

61 PI)-anchored proteins serve as receptors for aerolysin; thus, PNH cells are resistant to aerolysin.

62 Aerolysin variants with single amino acid changes that p

63 type III cells were completely resistant to aerolysin, whereas PNH type II cells displayed intermedi

64 ure by using two toxins, alpha-hemolysin and aerolysin, which differ in their shape, size, and charge