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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 is a promising tool for assessing asthma treatment
6 NEAT provides biologists and bioinformaticians with a ro
7 NEAT-LAMP leverages existing capabilities of diagnostic
8 EAT is run on the institution's cluster; (3) NEAT allows users to visualize and summarize NGS data ra
10 beta-haemolytic human pathogen, expresses a NEAT protein, Shr, which binds several haemoproteins and
11 s S-layer homology (SLH) protein harboring a NEAT domain binds and directionally transfers heme to th
12 and directionally transfers heme to IsdC, a NEAT protein covalently attached to the cell wall, as we
16 late Loop-mediated Isothermal Amplification (NEAT-LAMP) using cellular prion (PrP(C)) as a model prot
17 oth near-iron transporter motifs NEAT(1) and NEAT(2) of IsdB individually bound Vn in a saturable man
18 s physical activity, energy expenditure, and NEAT in a dose-dependent manner in both DR and DIO rats,
21 e vaccination correlated with increased anti-NEAT antibody reactivity and reduced bacterial levels in
23 ter-specific parameters can be customized as NEAT is run on the institution's cluster; (3) NEAT allow
25 The Network to control atherothrombosis (NEAT) registry is a national prospective observational s
26 ity was demonstrated by correlations between NEAT baseline and follow-up scores (eg, intra-class corr
29 > 1.86 observed copies per cell for BR9601, NEAT, Belgian, and DBCG89D trials and > 2.25 for the MA.
30 Moreover, the small-sized files produced by NEAT allow users to easily manipulate, consolidate and s
31 opies of a recently discovered domain called NEAT (NEAr Transporter) that has been shown to mediate p
32 determined crystal structures of its central NEAT domain (Hbp2(N2); residues 183-303) in its free and
33 prisingly, our work reveals that the central NEAT domain in Hbp2 binds hemin even though its primary
34 s used by all other previously characterized NEAT domains to coordinate iron in the hemin molecule.
37 ese results indicate that we should consider NEAT proteins in the development of an improved antianth
38 we demonstrate that both of the constituent NEAT domains of Shr are responsible for binding haem, al
42 development of double-clickable executables, NEAT is efficient (completes within <24 hours), easy to
43 n fragment containing the NTD plus the first NEAT domain was found to be sufficient to sequester haem
48 y publicly available tools including Galaxy, NEAT provides three main advantages: (1) Through the dev
49 Binding studies indicate that two IsdH/HarA NEAT domains bind a single molecule of methemoglobin, wh
50 ficance of harboring multiple, non-identical NEAT domains, we purified each individual NEAT domain of
53 e side chain in this position is observed in NEAT domains of several genera of gram-positive pathogen
54 al NEAT domains, we purified each individual NEAT domain of IsdX2 as a GST fusion and analyzed the sp
55 (pM) antibodies that neutralize the two IsdB NEAT domains, IGHV4-39 for NEAT1 and IGHV1-69 for NEAT2.
57 a spectroscopic analysis to show that IsdX2 NEAT domains only scavenge heme from methemoglobin (metH
58 gated dumbbell-shaped structure in which its NEAT domains are properly positioned by a helical linker
59 simulators-ART, DWGSIM, InSilicoSeq, Mason, NEAT, and wgsim-and discuss important considerations for
61 oglobin using proteins that contain multiple NEAT domains and other domains whose functions are poorl
62 ure Hb using receptors that contain multiple NEAT domains, suggesting that they use a conserved mecha
64 that contains its second (N2) and third (N3) NEAT domains joined by a helical linker, called IsdH(N2N
68 uggest that as humans overeat, activation of NEAT dissipates excess energy to preserve leanness and t
70 rtant, yet seldom investigated, component of NEAT is the energy expenditure of fidgeting-like activit
71 that Shr is the prototype of a new group of NEAT composite proteins involved in haem uptake found in
72 plasticity in the hemin binding mechanism of NEAT domains and provide insight into how L. monocytogen
75 me in the extracellular milieu and relies on NEAT-NEAT interactions to deliver the bound heme to the
77 rce of iron, and indicates that at least one NEAT domain is necessary for the utilization of methaemo
80 idence that a vaccine based upon recombinant NEAT proteins should be considered in the development of
81 f methemoglobin, while the distantly related NEAT domain from the S. aureus IsdC protein binds only h
83 o guide the development of inactive and safe NEAT antigens, we also report the crystal structure of o
88 ry sequence level, our results indicate that NEAT domains belong to the immunoglobulin superfamily.
94 elated with an antibody response against the NEAT domains and a decrease in the numbers of bacteria i
95 tients completed a survey which included the NEAT, the Asthma Control Test (ACT), the Asthma Quality
97 three-dimensional solution structure of the NEAT domain from the IsdH/HarA protein, which is the hem
100 o report the crystal structure of one of the NEAT domains (Hal) and identify critical residues mediat
101 METHODS AND In this ancillary study of the NEAT-HFpEF trial (Nitrate's Effects on Activity Toleranc
103 anges in nonexercise activity thermogenesis (NEAT) mediate resistance to weight gain with overfeeding
104 ncreased nonexercise activity thermogenesis (NEAT), which is associated with fidgeting, maintenance o
107 stions concerning the relative role of these NEAT proteins, relative to hemophores and the Isd system
109 The reduction of the formulation to three NEATs (IsdX1, IsdX2, and Bslk) was as effective as a fiv
110 1941 tumours from 2391 women recruited to NEAT/BR9601 were analysed on tissue microarrays for HER2
111 resent the NExt generation Analysis Toolbox (NEAT) that allows non-expert users including wet-lab sci
112 y linear regressions of changes in the total NEAT score and changes in AQLQ-S (beta = 0.21; P < 0.01)
114 ort system containing near-iron transporter (NEAT) domains and its efficacy as a vaccine for anthrax
117 genic bacteria employ near-iron transporter (NEAT) domains to acquire heme from hemoglobin during inf
119 ain genes that encode near iron transporter (NEAT) proteins that are genomically distant from the gen
122 or secreted proteins with NEAr Transporter (NEAT) domains play a central role in haem acquisition an
123 A and IsdC bind heme using NEAr Transporter (NEAT) domains that are conserved in many species of path
125 f a conserved domain (near-iron transporter [NEAT]), common in Gram-positive pathogens, elicits prote
126 ssess the Patient Needs in Asthma Treatment (NEAT) questionnaire's validity, responsiveness to change
127 The National Epirubicin Adjuvant Trial (NEAT) and the BR9601 trial examined the efficacy of anth
128 ith a unique N-terminal domain (NTD) and two NEAT domains separated by a central leucine-rich repeat
129 conserved tri-domain unit consisting of two NEAT (near iron transporter) domains connected by a heli
130 e agent of the disease anthrax, secretes two NEAT (near iron transporter) proteins, IsdX1 and IsdX2,
132 that, rather than acting as isolated units, NEAT domains may be integrated into higher order archite
134 GATA motif to a putative target gene, using NEAT-seq data to internally validate SNP impact on GATA3
137 To simplify the control of the workflow, NEAT projects are built around a unique and centralized