ライフサイエンスコーパス: NEAT

1 NEAT can be applied not only to undirected, but to direc

2 NEAT domains 1, 3, 4, and 5 all bind heme, with domain 5

3 NEAT domains are protein modules that partake in several

4 NEAT is a flexible and efficient test for network enrich

5 NEAT provides biologists and bioinformaticians with a ro

6 EAT is run on the institution's cluster; (3) NEAT allows users to visualize and summarize NGS data ra

7 s is the first report of haem reduction by a NEAT protein.

8 beta-haemolytic human pathogen, expresses a NEAT protein, Shr, which binds several haemoproteins and

9 s S-layer homology (SLH) protein harboring a NEAT domain binds and directionally transfers heme to th

10 and directionally transfers heme to IsdC, a NEAT protein covalently attached to the cell wall, as we

11 This is the first structure of a NEAT domain and reveals that they adopt a beta sandwich

12 eserve leanness and that failure to activate NEAT may result in ready fat gain.

13 All NEATs associate with hemoglobin, but only NEAT1 and -5 c

14 s physical activity, energy expenditure, and NEAT in a dose-dependent manner in both DR and DIO rats,

15 r heme to IsdC, a cell wall-anchored anthrax NEAT protein.

16 Anti-NEAT antibodies promote opsonophagocytosis of bacilli by

17 ter-specific parameters can be customized as NEAT is run on the institution's cluster; (3) NEAT allow

18 Frameworks such as NEAT not only allow novice users to overcome the increas

19 ligand-binding pocket of other haem-binding NEAT domains.

20 omain, positions the C-terminal heme-binding NEAT domain perfectly for heme transfer.

21 > 1.86 observed copies per cell for BR9601, NEAT, Belgian, and DBCG89D trials and > 2.25 for the MA.

22 Moreover, the small-sized files produced by NEAT allow users to easily manipulate, consolidate and s

23 opies of a recently discovered domain called NEAT (NEAr Transporter) that has been shown to mediate p

24 determined crystal structures of its central NEAT domain (Hbp2(N2); residues 183-303) in its free and

25 prisingly, our work reveals that the central NEAT domain in Hbp2 binds hemin even though its primary

26 s used by all other previously characterized NEAT domains to coordinate iron in the hemin molecule.

27 ese results indicate that we should consider NEAT proteins in the development of an improved antianth

28 we demonstrate that both of the constituent NEAT domains of Shr are responsible for binding haem, al

29 at it will also employ functionally distinct NEAT domains to bind heme and Hb.

30 To examine NEAT's role in obesity, we recruited 10 lean and 10 mild

31 development of double-clickable executables, NEAT is efficient (completes within <24 hours), easy to

32 n fragment containing the NTD plus the first NEAT domain was found to be sufficient to sequester haem

33 , we investigated the properties of the five-NEAT domain hemophore IsdX2.

34 ral requirements and mechanism of action for NEAT-mediated heme extraction remains unknown.

35 y publicly available tools including Galaxy, NEAT provides three main advantages: (1) Through the dev

36 Binding studies indicate that two IsdH/HarA NEAT domains bind a single molecule of methemoglobin, wh

37 ficance of harboring multiple, non-identical NEAT domains, we purified each individual NEAT domain of

38 In NEAT, we compared four cycles of epirubicin followed by

39 Changes in NEAT accounted for the 10-fold differences in fat storag

40 e side chain in this position is observed in NEAT domains of several genera of gram-positive pathogen

41 al NEAT domains, we purified each individual NEAT domain of IsdX2 as a GST fusion and analyzed the sp

42 (pM) antibodies that neutralize the two IsdB NEAT domains, IGHV4-39 for NEAT1 and IGHV1-69 for NEAT2.

43 We also demonstrate that the IsdC NEAT domain can capture heme directly from Hb, suggestin

44 a spectroscopic analysis to show that IsdX2 NEAT domains only scavenge heme from methemoglobin (metH

45 gated dumbbell-shaped structure in which its NEAT domains are properly positioned by a helical linker

46 oglobin using proteins that contain multiple NEAT domains and other domains whose functions are poorl

47 ure Hb using receptors that contain multiple NEAT domains, suggesting that they use a conserved mecha

48 European AIDS Treatment Network (NEAT).

49 uggest that as humans overeat, activation of NEAT dissipates excess energy to preserve leanness and t

50 We discuss applications of NEAT to network analyses in yeast by testing for enrichm

51 rtant, yet seldom investigated, component of NEAT is the energy expenditure of fidgeting-like activit

52 that Shr is the prototype of a new group of NEAT composite proteins involved in haem uptake found in

53 plasticity in the hemin binding mechanism of NEAT domains and provide insight into how L. monocytogen

54 Understanding the mechanism of NEAT-mediated iron transport into pathogenic Gram-positi

55 rly, respectively, with a mixed composite of NEATs.

56 me in the extracellular milieu and relies on NEAT-NEAT interactions to deliver the bound heme to the

57 the hemoglobin and heme binding surfaces on NEAT domains.

58 rce of iron, and indicates that at least one NEAT domain is necessary for the utilization of methaemo

59 ngly, this site is quite malleable, as other NEAT domains use it to bind heme.

60 We propose NEAT, a test for network enrichment analysis.

61 f methemoglobin, while the distantly related NEAT domain from the S. aureus IsdC protein binds only h

62 o guide the development of inactive and safe NEAT antigens, we also report the crystal structure of o

63 Shr NEAT domains, however, do not contribute significantly t

64 IsdX1 contains a single NEAT domain, whereas IsdX2 has five, a novel property am

65 An N-terminal NEAT domain binds alpha/beta globin through a site dista

66 ry sequence level, our results indicate that NEAT domains belong to the immunoglobulin superfamily.

67 Our simulations indicate that NEAT is considerably faster than alternative resampling-

68 The NEAT domain also binds hemoglobin and can acquire heme f

69 The NEAT domain binds heme, despite lacking a stabilizing ty

70 The NEAT/BR9601 trial showed benefit for addition of anthrac

71 If obese individuals adopted the NEAT-enhanced behaviors of their lean counterparts, they

72 elated with an antibody response against the NEAT domains and a decrease in the numbers of bacteria i

73 amide side chain reduces the affinity of the NEAT domain for metHb.

74 three-dimensional solution structure of the NEAT domain from the IsdH/HarA protein, which is the hem

75 amide side chain within the 310-helix of the NEAT domain.

76 he aliphatic heme-binding environment of the NEAT domain.

77 o report the crystal structure of one of the NEAT domains (Hal) and identify critical residues mediat

78 METHODS AND In this ancillary study of the NEAT-HFpEF trial (Nitrate's Effects on Activity Toleranc

79 lacking a stabilizing tyrosine common to the NEAT superfamily of hemoproteins.

80 anges in nonexercise activity thermogenesis (NEAT) mediate resistance to weight gain with overfeeding

81 ncreased nonexercise activity thermogenesis (NEAT), which is associated with fidgeting, maintenance o

82 called non-exercise activity thermogenesis (NEAT).

83 [called nonexercise activity thermogenesis (NEAT)].

84 stions concerning the relative role of these NEAT proteins, relative to hemophores and the Isd system

85 It contains three NEAT (NEAr Transporter) domains: IsdH(N1), IsdH(N2), and

86 1941 tumours from 2391 women recruited to NEAT/BR9601 were analysed on tissue microarrays for HER2

87 resent the NExt generation Analysis Toolbox (NEAT) that allows non-expert users including wet-lab sci

88 0520 encodes a single near-iron transporter (NEAT) domain and several leucine-rich repeats.

89 Remarkably, two near iron transporter (NEAT) domains in IsdH perform very different functions.

90 e using two conserved near iron transporter (NEAT) domains that function synergistically.

91 genic bacteria employ near-iron transporter (NEAT) domains to acquire heme from hemoglobin during inf

92 ontaining one or more near-iron transporter (NEAT) domains.

93 ain genes that encode near iron transporter (NEAT) proteins that are genomically distant from the gen

94 inds this molecule using a NEAr Transporter (NEAT) domain.

95 uence, Hbp2 contains three NEAr transporter (NEAT) domains of unknown function.

96 or secreted proteins with NEAr Transporter (NEAT) domains play a central role in haem acquisition an

97 A and IsdC bind heme using NEAr Transporter (NEAT) domains that are conserved in many species of path

98 f a conserved domain (near-iron transporter [NEAT]), common in Gram-positive pathogens, elicits prote

99 The National Epirubicin Adjuvant Trial (NEAT) and the BR9601 trial examined the efficacy of anth

100 ith a unique N-terminal domain (NTD) and two NEAT domains separated by a central leucine-rich repeat

101 conserved tri-domain unit consisting of two NEAT (near iron transporter) domains connected by a heli

102 e agent of the disease anthrax, secretes two NEAT (near iron transporter) proteins, IsdX1 and IsdX2,

103 B. anthracis secretes two NEAT hemophores, IsdX1 and IsdX2.

104 that, rather than acting as isolated units, NEAT domains may be integrated into higher order archite

105 Unlike Staphylococcus aureus, whose NEAT proteins acquire heme from hemoglobin directly at t

106 To simplify the control of the workflow, NEAT projects are built around a unique and centralized