ライフサイエンスコーパス: metalloprotein

1 y fractions, 158 did not match any predicted metalloprotein.

2 n of a bound Mg(2+) ion reveals that FB is a metalloprotein.

3 L lactonase from Bacillus sp. 240B1 is not a metalloprotein.

4 ) x 10(11) M(-)(1), consistent with a Zn(2+) metalloprotein.

5 lly oxidize the amino acids bound to Cu in a metalloprotein.

6 on, suggesting that the target is not a zinc metalloprotein.

7 there has been no suggestion that TAG was a metalloprotein.

8 experiments show that Nkd is a zinc-binding metalloprotein.

9 ially incorporated into the active site of a metalloprotein.

10 ally by harnessing its binding energy to the metalloprotein.

11 e electronic structure and the function of a metalloprotein.

12 pplementation suggested the involvement of a metalloprotein.

13 the Mn(II) ion in coordination complexes and metalloproteins.

14 centrations or in the maturation of secreted metalloproteins.

15 d that allows for robust characterization of metalloproteins.

16 is, metal tolerance, and the biosynthesis of metalloproteins.

17 ovide metals for the periplasmic assembly of metalloproteins.

18 transition metals, typically in the form of metalloproteins.

19 solvent-less (molten) liquids of functional metalloproteins.

20 ondria as a cofactor for several matrix zinc metalloproteins.

21 n to allow correct biochemical maturation of metalloproteins.

22 latter mechanism is especially possible with metalloproteins.

23 of how metalloproteins work is to design new metalloproteins.

24 ed investigations of paramagnetic centers of metalloproteins.

25 gated in a family of copper-containing redox metalloproteins.

26 conditions is performed for the suite of Fe-metalloproteins.

27 tivity is a novel mechanism of regulation in metalloproteins.

28 uantitative determination of iron-containing metalloproteins.

29 ation range of 0.1-100 microg/mL iron in the metalloproteins.

30 digm on a novel function of metal cluster in metalloproteins.

31 e(II)-, Co(II)-, and Ni(II)-binding sites of metalloproteins.

32 for studies of diamagnetic vanadium sites in metalloproteins.

33 d to determine the binding site of copper in metalloproteins.

34 ly one-third of all proteins estimated to be metalloproteins.

35 aryotic members of the PPP family, which are metalloproteins.

36 rameters that are applicable to redox-active metalloproteins.

37 r NO-induced release of Zn(2+) from cellular metalloproteins.

38 g the amino acid residues bound to copper in metalloproteins.

39 an be used to determine Fe-N-O geometries in metalloproteins.

40 S) to identify the binding site of copper in metalloproteins.

41 to mediate the transfer of hydrogen atoms in metalloproteins.

42 steine plays a key role as a metal ligand in metalloproteins.

43 ine-control of the structure and function of metalloproteins.

44 rtant properties of these prototypical redox metalloproteins.

45 reactions of NO with both model systems and metalloproteins.

46 on of possible evolutionary relationships of metalloproteins.

47 the carefully tuned amino acid framework in metalloproteins.

48 ssary for the proper functioning of numerous metalloproteins.

49 nt for locating metal-binding sites of other metalloproteins.

50 on-like reactions and mismetalation of other metalloproteins.

51 ation, leads to artifacts of metal loss from metalloproteins.

52 various biological functions of O2-utilizing metalloproteins.

53 ir occurrence as alpha-chiral amino acids in metalloproteins.

54 s an approach for simulating active sites of metalloproteins.

55 xperimentally accessing both redox states of metalloproteins.

56 g in many heme proteins, models, and related metalloproteins.

57 sical properties of the resulting artificial metalloproteins.

58 d highly structured ligands found in natural metalloproteins.

59 etry (MS) to identify Zn-bound histidines in metalloproteins.

60 f DNP in paramagnetically doped materials or metalloproteins.

61 f inhibitors that target clinically relevant metalloproteins.

62 ethod for identifying Zn-bound histidines in metalloproteins.

63 the vast majority, and the view is that most metalloproteins acquire their metals directly from cellu

64 Structure determination of the metalloprotein active site is obtained through a self-co

65 ic structure and coordination environment of metalloprotein active sites.

66 ifferent aspects of metal homeostasis and/or metalloprotein activity elicits distinct protective mech

67 tum clusters that are stabilized by the milk metalloprotein alpha-lactalbumin.

68 nd Fe-S proteins, two other classes of redox metalloproteins, also possess ESE rate constants of appr

69 prove the high efficiency of this method for metalloprotein analysis, we successfully identified a co

70 Both metalloprotein and flavin-linked sulfhydryl oxidases cat

71 e (NMR) spectroscopic shifts in paramagnetic metalloprotein and metalloporphyrin systems.

72 , these results indicate that NS5A is a zinc metalloprotein and that zinc coordination is likely requ

73 The discovery that Fur is a zinc metalloprotein and the use of surrogate metals for Fe(2+

74 These highly covalent ligands are found in metalloproteins and are also used as models for Fe-O2 sy

75 ructures of transition-metal active sites in metalloproteins and chemical catalysts.

76 iniscent of the strategy followed by several metalloproteins and highlight the possible implication o

77 Two general groups - metalloproteins and periplasmic proteins - show enrichme

78 ated as a result of interactions between the metalloproteins and the dye with no metal ion dissociati

79 e based on the radical processes mediated by metalloproteins and their synthetic analogs.

80 s that may be missing from studies of native metalloproteins and their variants, but also can result

81 n S = 0, (1)/(2), 1, (3)/(2), 2, and (5)/(2) metalloproteins and/or model systems.

82 Our results indicate that Abeta in vivo is a metalloprotein, and the loosening of the structure follo

83 idea that the intracellular form of the PerR metalloprotein, and therefore its hydrogen peroxide sens

84 Eukaryotic cells contain hundreds of metalloproteins, and ensuring that each protein receives

85 the glass pores, react with the encapsulated metalloproteins, and establish the interprotein electron

86 complex, iron-containing redox cofactors of metalloproteins, and manage a myriad of biochemical tran

87 scent cluster, traffic the cluster to target metalloproteins, and regulate the assembly machinery in

88 To leverage the experimental metalloprotein annotations, we used a sequence-based de

89 The implication is that mononuclear metalloproteins are common targets of H(2)O(2) and that

90 metal ions and the proper maturation of holo-metalloproteins are essential processes for all organism

91 e the structural details of TM ions bound to metalloproteins are generally well understood via experi

92 ility has remained an enigma, because copper metalloproteins are prevalent and essential throughout a

93 The metalloproteins are reduced both chemically and electroc

94 active site analysis on the genome scale for metalloproteins as a class, revealing new insights into

95 c mobilization, implicating DNA-binding zinc metalloproteins as critical targets of NO-related antimi

96 The interstitial collagenase matrix metalloprotein-ase-1 (MMP-1) is up-regulated in the lung

97 How each metalloprotein assembles the correct metal at the proper

98 , in principle, be used to nucleate specific metalloprotein assemblies if introduced into proteins su

99 trix proteoglycans/glycoproteins is a Zn(2+) metalloprotein at physiological Zn(2+) concentrations.

100 Interactions of a model Cu-metalloprotein, azurin, with 10-100 nm silver nanopartic

101 ectrophoresis method to isolate and identify metalloproteins, based on the molecular recognition of h

102 le chemical transformations accessible using metalloprotein-based catalysts.

103 substrate loading was achieved by means of a metalloprotein bearing an iron-containing heme subunit i

104 stead by cyanide ion until its toxicity with metalloproteins became a problem and primitive enzymes w

105 ve the reversible unfolding and refolding of metalloproteins because of a loss or decomposition of th

106 ied Zn metalloproteins to validate predicted metalloprotein binding site structures.

107 is one of the most complicated processes in metalloprotein biochemistry.

108 rguably one of the most complex processes in metalloprotein biochemistry.

109 for enzyme-based bioelectrochemical sensors, metalloprotein bioelectronics, and energy research.

110 epresents a novel organism in which to study metalloprotein biology in that this spirochete has uniqu

111 pillary electrophoresis to follow a globular metalloprotein--bovine carbonic anhydrase II (BCA, EC 4.

112 This binding mode is rare among metalloproteins but well suited for an ultrasensitive ge

113 S-nitrosylation of Cu(II)-bound cysteine in metalloproteins, but also shed light on the reaction mec

114 ns that could be used for the measurement of metalloproteins by on-line IDMS analysis.

115 Azurin is a member of a family of metalloproteins called cupredoxins.

116 s, misallocation of the wrong metal ion to a metalloprotein can have resounding and often detrimental

117 Paramagnetic metalloproteins can be effective MRI sensors due to the

118 od before structure-function correlations of metalloproteins can be made on the basis of high-resolut

119 results show that structural and functional metalloproteins can be rationally designed in silico.

120 The release of metal ions from metalloproteins can have significant biological conseque

121 prion protein (PrP) has been identified as a metalloprotein capable of binding multiple copper ions a

122 Metalloproteins catalyse some of the most complex and im

123 bene-mediated transformations accessible via metalloprotein catalysts and introduces a potentially ge

124 ould prove useful for further development of metalloprotein catalysts for abiotic carbene transfer re

125 The damage to metalloproteins caused by reactive oxygen species (ROS)

126 iew the molecular evolution of several human metalloproteins charged with restricting bacterial acces

127 Ss, including resolved (1)H PCSs, in a large metalloprotein, Co(2+)-substituted superoxide dismutase

128 istent with annealing of an initially formed metalloprotein complex (k anneal = 0.4 min(-1)).

129 The kinetic stability of the metalloprotein complex can be traced to stabilization by

130 ion of modes, (2) optimization of the ligand-metalloprotein complex geometry by combined quantum mech

131 00 nm in diameter and is the largest natural metalloprotein complex known.

132 nding the assembly of this integral membrane metalloprotein complex.

133 A series of metalloprotein complexes embedded in a mitochondrial or

134 roperties, and interactions of the resulting metalloprotein complexes with azide, hydrogen peroxide,

135 Metalloproteins comprise over one-third of proteins, wit

136 r proteome that lower the levels of abundant metalloproteins, conserving metal ions for more critical

137 2+) binding site within two de novo designed metalloprotein constructs using (111m)Cd perturbed angul

138 ts indicating that EutT was an oxygen-labile metalloprotein containing a redox-active metal.

139 Our structure reveals a new class of metalloprotein containing multinuclear iron clusters.

140 We also show that RsrA is a metalloprotein, containing near-stoichiometric amounts o

141 e was used as the plasmonic donor, while the metalloprotein cytochrome c was used as the acceptor mol

142 The Metalloprotein Database and Browser at The Scripps Resea

143 HDLP), using a modified scoring function for metalloproteins, demonstrate excellent agreement (R = 0.

144 atography separations of the iron-containing metalloproteins demonstrates the feasibility of the PB/H

145 Metalloprotein design and semiconductor nanoparticles ha

146 ersatility of alpha helices as scaffolds for metalloprotein design and the progress that is possible

147 De Novo metalloprotein design assesses the relationship between

148 While metalloprotein design has now yielded a number of succes

149 De novo metalloprotein design is a way to wipe the board clean a

150 A major goal in metalloprotein design is to build protein scaffolds from

151 This experiment is the first successful metalloprotein design that has a high coordination numbe

152 Metalloprotein design was used to generate a Pb(2+) ion

153 ed with regard to metalloprotein folding and metalloprotein design.

154 The metal binding preferences of most metalloproteins do not match their metal requirements.

155 n parallel with known metal substitutions of metalloproteins, driven by the Great Oxidation Event.

156 sibility of applications of this approach to metalloprotein drug targets, such as matrix metalloprote

157 in the four-helix bundle of de novo designed metalloprotein Duo Ferro 1.

158 is a good model for redox reactions between metalloproteins (electron carriers) and specific organic

159 ydrolase (PR-AMP cyclohydrolase) is a Zn(2+) metalloprotein encoded by the hisI gene.

160 ive metal required as a cofactor in multiple metalloproteins essential for a host of life processes.

161 ns and the redox activities of the resulting metalloprotein films.

162 itric oxide synthases (NOSs) are multidomain metalloproteins first identified in mammals as being res

163 The mechanism is discussed with regard to metalloprotein folding and metalloprotein design.

164 The metalloprotein follows the halogenation cycle, whereby c

165 environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection

166 Alkaline phosphatase (ALP) is a metalloprotein found naturally in raw milk samples and i

167 definition structure of the active site of a metalloprotein from a powder sample, by combining magic-

168 g a vector, we introduced an MRI reporter, a metalloprotein from the ferritin family, into specific h

169 rometry (ICP-MS) to characterize cytoplasmic metalloproteins from an exemplary microorganism (Pyrococ

170 Metalloproteins generated using this strategy uniformly

171 protein scaffold on the unique properties of metalloproteins has rarely been studied.

172 To overcome this limitation, artificial metalloproteins have been created by incorporating compl

173 Detailed pathways for metal ion release from metalloproteins have been difficult to elucidate by clas

174 ordination spheres of metal binding sites in metalloproteins have been investigated extensively, lead

175 uring thermodynamic metal ion selectivity of metalloproteins have been performed, and the major deter

176 Consequently, metalloproteins have key roles in most biological proces

177 Many metalloproteins have the capacity to bind diverse metals

178 nisms: 1) reduction and/or direct binding of metalloprotein heme centers, 2) serving as a potent anti

179 o the creation of high-performing functional metalloproteins; however, the impact of the overall stru

180 elationship between the activity of the zinc metalloprotein IDE and glucose homeostasis remains uncle

181 gate the structure-function relationships of metalloproteins in a minimal, well-defined and controlle

182 sensitive visualization and quantitation of metalloproteins in biological samples.

183 these biological assemblies by encapsulating metalloproteins in sol-gel silica glass and letting mobi

184 ssion protocols, sensitivity-enhanced NMR of metalloproteins in solution, the investigation of solven

185 owever, this technique cannot be extended to metalloproteins in solution.

186 actors represent the largest single class of metalloproteins in the human genome.

187 he first and second dimensions of PAGE, holo-metalloproteins in the original sample were completely i

188 Little is known about how metalloproteins in the secretory pathway obtain their me

189 sfer Fe-S clusters to the appropriate target metalloproteins in vivo.

190 llowed to determine epsilon values for other metalloproteins in which metal binding contributes to th

191 ded the Rosetta design methodology to design metalloproteins in which the amino acid (2,2'-bipyridin-

192 ginosa azurin is a 128-residue beta-sandwich metalloprotein; in vitro kinetic experiments have shown

193 For some metalloproteins (including all transferrin family member

194 ty during cofactor assembly for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-de

195 e of the reduction potential E degrees for a metalloprotein indicates that the protonation state of a

196 tegy for the discovery of lead fragments for metalloprotein inhibition.

197 at despite their ability to bind metal ions, metalloprotein inhibitors are not prone to widespread of

198 e selected as well as several other reported metalloprotein inhibitors in order to represent a broad

199 Representative ligand-metalloprotein interaction energies are obtained by subs

200 Metal centers in metalloproteins involve multiple metal-ligand bonds.

201 tantial variations in concentrations of iron metalloproteins involved in nitrogen fixation and photos

202 y definition, the release of metal ions from metalloproteins involves the disruption of multiple meta

203 An important feature of the designed metalloprotein is its two cationic redox centers embedde

204 Cyt c, a heme containing metalloprotein is located in the intermembrane space of

205 Quality computational description of metalloproteins is a great challenge due to the vast spa

206 of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bi

207 nition of biologically active amino acids of metalloproteins is elicited by the presence of specific

208 analyze accurately and precisely individual metalloproteins is of increasing importance.

209 ting that species-specific ID-MS analysis of metalloproteins is possible.

210 nalysis of unpaired electron spin density in metalloproteins is presented, which allows a fast and ro

211 structural determination of active sites of metalloproteins is presented.

212 , a product of catabolism of heme-containing metalloproteins, is a key inducer of ROS.

213 parison to recent successes in designing non-metalloproteins, it is even more challenging to rational

214 the problems in the receptor-based design of metalloprotein ligands due to inadequacies in the force-

215 ctive intermediates and transition states in metalloproteins may be widespread in nature.

216 Other metalloproteins may have similarly adapted to using mang

217 In metalloproteins, metal centers serve as active sites for

218 n the molecular recognition of holo- and apo-metalloproteins (metalbound and -free forms, respectivel

219 series of 24 inorganic, organometallic, and metalloprotein/metalloporphyrin model systems in S = 0,

220 bles validation and potential remediation of metalloprotein models, improving structural and, more im

221 Metalloproteins (MPs) comprise one-third of all known pr

222 allenging to design metalloproteins than non-metalloproteins, much progress has been made in this are

223 gn of a structural and functional model of a metalloprotein, nitric oxide reductase (NOR), by introdu

224 The two-component metalloprotein nitrogenase catalyzes the reductive fixat

225 als an organism assimilates and identify its metalloproteins on a genome-wide scale.

226 owever, existing MRI reporter genes based on metalloproteins or chemical exchange probes are limited

227 e show that the technique can be extended to metalloproteins or complex:protein interactions.

228 The degree by which metalloproteins partially regulate net charge (Z) upon e

229 opportunity to test our understanding of how metalloproteins perform difficult transformations.

230 n microcrystalline powders of a paramagnetic metalloprotein permit NMR crystallography.

231 ns in biological systems, and drug design in metalloprotein platforms.

232 rous strategies have been used to create new metalloproteins, pre-existing knowledge of the tertiary

233 ial and archaeal phyla genetically couple to metalloproteins related to beta-lactamases and nitric ox

234 tom-up design and construction of functional metalloproteins remains a formidable task in biomolecula

235 f CusF (log K = 14.3 +/- 0.1), a periplasmic metalloprotein required for the detoxification of elevat

236 h Institute is a web-accessible resource for metalloprotein research.

237 ting from in situ chemical manipulation of a metalloprotein sample.

238 xpressing NifEN, a complex, heteromultimeric metalloprotein sharing structural/functional homology wi

239 ectron paramagnetic resonance spectra of the metalloproteins show that encapsulation in sol-gel glass

240 -nitrosylation and denitrosylation involving metalloproteins, SNO lyase(s) and GSNO reductase.

241 nhance the understanding of similar sites in metalloproteins, specifically cobalt-substituted zinc en

242 butions of metal-protein interactions toward metalloprotein stability is largely due to an inability

243 ontribution of a Zn(II)-(S.Cys)4 site toward metalloprotein stability relevant to classic structural

244 Here we show that a de novo designed Zn(II) metalloprotein stabilizes a chemically reactive organic

245 n and evaluation of an isotopically enriched metalloprotein standard for use as a calibrant in specie

246 eins as a class, revealing new insights into metalloprotein structure and function.

247 n provide a reliable balanced description of metalloproteins' structure, dynamics, and electronic str

248 binding site that appears to be unique among metalloproteins studied to date.

249 Among them, there are four metalloprotein subunits, including a 113 kDa iron-sulfur

250 ins two histidine motifs resembling those of metalloproteins such as fatty acid desaturases.

251 ficking required for the assembly of complex metalloproteins such as nitrogenase.

252 te (67)Zn NMR spectra of model compounds for metalloproteins, such as [H(2)B(3,5-Me(2)pz)(2)](2)Zn (p

253 em that affected to the levels of metals and metalloproteins, such as MT, Cu/Zn-SOD, or Mn-CA, the br

254 for understanding the mechanism of important metalloproteins, such as photosystem II.

255 though it is much more challenging to design metalloproteins than non-metalloproteins, much progress

256 oxygen ((1)O(2)) is mediated by ChrR, a zinc metalloprotein that binds to and inhibits the activity o

257 Transferrin (Tf) is an enigmatic metalloprotein that exhibits a profound conformational c

258 for the assembly of periplasmic and secreted metalloproteins that are essential for survival in extre

259 metal ions, with emphasis on copper(II), to metalloproteins that are hallmarks of these diseases - a

260 Transferrins constitute a class of metalloproteins that are involved in circulatory iron tr

261 Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular syst

262 es to date are the AHL lactonases, which are metalloproteins that belong to the metallo-beta-lactamas

263 [FeFe]-Hydrogenases are complex metalloproteins that catalyze the reversible reduction o

264 Superoxide dismutases (SODs) are metalloproteins that protect organisms from toxic reacti

265 s even more challenging to rationally design metalloproteins that reproduce both the structure and fu

266 we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains

267 Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenu

268 e range of metal ions, but unlike many other metalloproteins, the structures of apo- and partially me

269 built from interactions observed in simpler metalloproteins, they contain novel features that may be

270 an analytical method capable of finding new metalloproteins, this is the first report of a new diago

271 For metalloproteins to acquire the right metals, metal senso

272 Biology employs three classes of metalloproteins to cover the majority of the 2-V range o

273 re important biological ligands that bind to metalloproteins to function crucially in processes such

274 Selective binding by metalloproteins to their cognate metal ions is essential

275 e structure data from two of the purified Zn metalloproteins to validate predicted metalloprotein bin

276 uctural characterization of de novo designed metalloproteins together with determination of chemical

277 Four iron-containing metalloproteins (transferrin, myoglobin, hemoglobin, and

278 n of cytochrome c (cyt c), a heme containing metalloprotein using its specific monoclonal antibody.

279 shifts in paramagnetic metalloporphyrins and metalloproteins using quantum chemical methods should op

280 uctural and dynamical determination of large metalloproteins using solid-state nuclear magnetic reson

281 A de novo designed coiled-coil metalloprotein was prepared that uses electrostatic inte

282 residues were coordinated with metals and 15 metalloproteins were endogenously modified supporting me

283 not equally active and due to the fact that metalloproteins were rarely used as drug targets.

284 the geometric structure and the dynamics of metalloproteins, when NMR parameters are available of nu

285 An extra layer of complexity is added in metalloproteins, where a metal cofactor participates in

286 es share properties with the active sites of metalloproteins, where function is correlated strongly w

287 Pho8 appears to be a rare example of a metalloprotein whose stability is regulated by its metal

288 PerR is a dimeric, Zn2+-containing metalloprotein with a regulatory metal-binding site that

289 1 periplasmic, catalytic domain to be a zinc metalloprotein with an alkaline phosphatase/sulphatase f

290 characterization revealed a Bpy-Ala-mediated metalloprotein with the ability to bind divalent cations

291 after purification, indicating that Mca is a metalloprotein with zinc as the native metal.

292 cellular damage initiated by the reaction of metalloproteins with H2O2.

293 ethod also facilitates the de novo design of metalloproteins with novel structures and functions, inc

294 ng the rupture mechanism of metal centers in metalloproteins with unprecedented resolution by using s

295 purified STM1808 suggests that it is a zinc metalloprotein, with histidine residues H32 and H82 requ

296 on protein design efforts to create de novo metalloproteins within alpha-helical scaffolds.

297 detoxification, also deliver zinc to certain metalloproteins within intracellular compartments.

298 An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins.

299 essful design of a structural and functional metalloprotein would greatly advance the field of protei

300 nt with the hypothesis that E4 34k is a zinc metalloprotein, zinc binding by baculovirus-expressed E4