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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 ally by harnessing its binding energy to the metalloprotein.
8  there has been no suggestion that TAG was a metalloprotein.
9  experiments show that Nkd is a zinc-binding metalloprotein.
10 ially incorporated into the active site of a metalloprotein.
11 viously shown that the E. coli TGT is a zinc metalloprotein.
12 e electronic structure and the function of a metalloprotein.
13 pplementation suggested the involvement of a metalloprotein.
14 various biological functions of O2-utilizing metalloproteins.
15 ovide metals for the periplasmic assembly of metalloproteins.
16  transition metals, typically in the form of metalloproteins.
17 ir occurrence as alpha-chiral amino acids in metalloproteins.
18  solvent-less (molten) liquids of functional metalloproteins.
19 ondria as a cofactor for several matrix zinc metalloproteins.
20 n to allow correct biochemical maturation of metalloproteins.
21 latter mechanism is especially possible with metalloproteins.
22 of how metalloproteins work is to design new metalloproteins.
23 ed investigations of paramagnetic centers of metalloproteins.
24 gated in a family of copper-containing redox metalloproteins.
25  conditions is performed for the suite of Fe-metalloproteins.
26 uantitative determination of iron-containing metalloproteins.
27 ation range of 0.1-100 microg/mL iron in the metalloproteins.
28 e(II)-, Co(II)-, and Ni(II)-binding sites of metalloproteins.
29 for studies of diamagnetic vanadium sites in metalloproteins.
30 d to determine the binding site of copper in metalloproteins.
31 ly one-third of all proteins estimated to be metalloproteins.
32 aryotic members of the PPP family, which are metalloproteins.
33 rameters that are applicable to redox-active metalloproteins.
34 r NO-induced release of Zn(2+) from cellular metalloproteins.
35 g the amino acid residues bound to copper in metalloproteins.
36 s an approach for simulating active sites of metalloproteins.
37 an be used to determine Fe-N-O geometries in metalloproteins.
38 S) to identify the binding site of copper in metalloproteins.
39 to mediate the transfer of hydrogen atoms in metalloproteins.
40 steine plays a key role as a metal ligand in metalloproteins.
41 ine-control of the structure and function of metalloproteins.
42 rtant properties of these prototypical redox metalloproteins.
43  reactions of NO with both model systems and metalloproteins.
44 on of possible evolutionary relationships of metalloproteins.
45 tal and has been widely used to characterize metalloproteins.
46 of these non-native peptides in the study of metalloproteins.
47 xperimentally accessing both redox states of metalloproteins.
48 he isozymes were shown to be zinc-containing metalloproteins.
49 g in many heme proteins, models, and related metalloproteins.
50 sical properties of the resulting artificial metalloproteins.
51 d highly structured ligands found in natural metalloproteins.
52 etry (MS) to identify Zn-bound histidines in metalloproteins.
53 f DNP in paramagnetically doped materials or metalloproteins.
54 f inhibitors that target clinically relevant metalloproteins.
55 ethod for identifying Zn-bound histidines in metalloproteins.
56 the Mn(II) ion in coordination complexes and metalloproteins.
57 centrations or in the maturation of secreted metalloproteins.
58 d that allows for robust characterization of metalloproteins.
59 is, metal tolerance, and the biosynthesis of metalloproteins.
60 l chelation, protein folding and function in metalloproteins, a family of de novo-designed peptides w
61 the vast majority, and the view is that most metalloproteins acquire their metals directly from cellu
62               Structure determination of the metalloprotein active site is obtained through a self-co
63 ic structure and coordination environment of metalloprotein active sites.
64 ifferent aspects of metal homeostasis and/or metalloprotein activity elicits distinct protective mech
65 nd Fe-S proteins, two other classes of redox metalloproteins, also possess ESE rate constants of appr
66                                         Both metalloprotein and flavin-linked sulfhydryl oxidases cat
67 e (NMR) spectroscopic shifts in paramagnetic metalloprotein and metalloporphyrin systems.
68 , these results indicate that NS5A is a zinc metalloprotein and that zinc coordination is likely requ
69             The discovery that Fur is a zinc metalloprotein and the use of surrogate metals for Fe(2+
70                   All three enzymes are Zn2+ metalloproteins and also require Mg2+ for activity.
71   These highly covalent ligands are found in metalloproteins and are also used as models for Fe-O2 sy
72 ructures of transition-metal active sites in metalloproteins and chemical catalysts.
73 iniscent of the strategy followed by several metalloproteins and highlight the possible implication o
74  functional and bibliographic information on metalloproteins and other complex proteins, with an emph
75 e based on the radical processes mediated by metalloproteins and their synthetic analogs.
76 s that may be missing from studies of native metalloproteins and their variants, but also can result
77 n S = 0, (1)/(2), 1, (3)/(2), 2, and (5)/(2) metalloproteins and/or model systems.
78 her studies, it had been shown that PP1 is a metalloprotein, and in this study, we have largely focus
79 Our results indicate that Abeta in vivo is a metalloprotein, and the loosening of the structure follo
80 idea that the intracellular form of the PerR metalloprotein, and therefore its hydrogen peroxide sens
81         Eukaryotic cells contain hundreds of metalloproteins, and ensuring that each protein receives
82 the glass pores, react with the encapsulated metalloproteins, and establish the interprotein electron
83  complex, iron-containing redox cofactors of metalloproteins, and manage a myriad of biochemical tran
84 scent cluster, traffic the cluster to target metalloproteins, and regulate the assembly machinery in
85                 To leverage the experimental metalloprotein annotations, we used a sequence-based de
86          The implication is that mononuclear metalloproteins are common targets of H(2)O(2) and that
87 ility has remained an enigma, because copper metalloproteins are prevalent and essential throughout a
88                                          The metalloproteins are reduced both chemically and electroc
89 active site analysis on the genome scale for metalloproteins as a class, revealing new insights into
90 c mobilization, implicating DNA-binding zinc metalloproteins as critical targets of NO-related antimi
91          The interstitial collagenase matrix metalloprotein-ase-1 (MMP-1) is up-regulated in the lung
92                                     How each metalloprotein assembles the correct metal at the proper
93 , in principle, be used to nucleate specific metalloprotein assemblies if introduced into proteins su
94 trix proteoglycans/glycoproteins is a Zn(2+) metalloprotein at physiological Zn(2+) concentrations.
95                   Interactions of a model Cu-metalloprotein, azurin, with 10-100 nm silver nanopartic
96 le chemical transformations accessible using metalloprotein-based catalysts.
97 stead by cyanide ion until its toxicity with metalloproteins became a problem and primitive enzymes w
98 ve the reversible unfolding and refolding of metalloproteins because of a loss or decomposition of th
99               The DAHP synthase isozymes are metalloproteins, being activated in vitro by a variety o
100 ied Zn metalloproteins to validate predicted metalloprotein binding site structures.
101  is one of the most complicated processes in metalloprotein biochemistry.
102 rguably one of the most complex processes in metalloprotein biochemistry.
103 for enzyme-based bioelectrochemical sensors, metalloprotein bioelectronics, and energy research.
104 epresents a novel organism in which to study metalloprotein biology in that this spirochete has uniqu
105 pillary electrophoresis to follow a globular metalloprotein--bovine carbonic anhydrase II (BCA, EC 4.
106              This binding mode is rare among metalloproteins but well suited for an ultrasensitive ge
107  S-nitrosylation of Cu(II)-bound cysteine in metalloproteins, but also shed light on the reaction mec
108 ns that could be used for the measurement of metalloproteins by on-line IDMS analysis.
109            Azurin is a member of a family of metalloproteins called cupredoxins.
110 s, misallocation of the wrong metal ion to a metalloprotein can have resounding and often detrimental
111                                 Paramagnetic metalloproteins can be effective MRI sensors due to the
112 od before structure-function correlations of metalloproteins can be made on the basis of high-resolut
113  results show that structural and functional metalloproteins can be rationally designed in silico.
114 ause of their high affinity and selectivity, metalloproteins can be used as transducers in novel sens
115               The release of metal ions from metalloproteins can have significant biological conseque
116 prion protein (PrP) has been identified as a metalloprotein capable of binding multiple copper ions a
117                                              Metalloproteins catalyse some of the most complex and im
118 bene-mediated transformations accessible via metalloprotein catalysts and introduces a potentially ge
119 Ss, including resolved (1)H PCSs, in a large metalloprotein, Co(2+)-substituted superoxide dismutase
120 istent with annealing of an initially formed metalloprotein complex (k anneal = 0.4 min(-1)).
121                 The kinetic stability of the metalloprotein complex can be traced to stabilization by
122 ion of modes, (2) optimization of the ligand-metalloprotein complex geometry by combined quantum mech
123 00 nm in diameter and is the largest natural metalloprotein complex known.
124 nding the assembly of this integral membrane metalloprotein complex.
125                                  A series of metalloprotein complexes embedded in a mitochondrial or
126 roperties, and interactions of the resulting metalloprotein complexes with azide, hydrogen peroxide,
127 2+) binding site within two de novo designed metalloprotein constructs using (111m)Cd perturbed angul
128 ts indicating that EutT was an oxygen-labile metalloprotein containing a redox-active metal.
129         Our structure reveals a new class of metalloprotein containing multinuclear iron clusters.
130 cate that (i) the Gram-positive pol III is a metalloprotein containing tightly bound zinc in a stoich
131                  We also show that RsrA is a metalloprotein, containing near-stoichiometric amounts o
132 e was used as the plasmonic donor, while the metalloprotein cytochrome c was used as the acceptor mol
133 oteins have probed lambda and HAB in several metalloproteins (cytochrome c, myoglobin, azurin).
134                                          The Metalloprotein Database and Browser at The Scripps Resea
135 ut may have a catalytic mechanism similar to metalloprotein de-N-acetylases such as LpxC.
136 HDLP), using a modified scoring function for metalloproteins, demonstrate excellent agreement (R = 0.
137 atography separations of the iron-containing metalloproteins demonstrates the feasibility of the PB/H
138 he protein matrix upon the metal center make metalloprotein design a very fruitful area for the explo
139                                              Metalloprotein design and semiconductor nanoparticles ha
140                                        While metalloprotein design has now yielded a number of succes
141                              A major goal in metalloprotein design is to build protein scaffolds from
142      This experiment is the first successful metalloprotein design that has a high coordination numbe
143                                              Metalloprotein design was used to generate a Pb(2+) ion
144 ed with regard to metalloprotein folding and metalloprotein design.
145        The metal binding preferences of most metalloproteins do not match their metal requirements.
146 n parallel with known metal substitutions of metalloproteins, driven by the Great Oxidation Event.
147 sibility of applications of this approach to metalloprotein drug targets, such as matrix metalloprote
148 in the four-helix bundle of de novo designed metalloprotein Duo Ferro 1.
149  is a good model for redox reactions between metalloproteins (electron carriers) and specific organic
150 ydrolase (PR-AMP cyclohydrolase) is a Zn(2+) metalloprotein encoded by the hisI gene.
151 ive metal required as a cofactor in multiple metalloproteins essential for a host of life processes.
152 Direct metal ligands to transition metals in metalloproteins exert a profound effect on protein-metal
153                                      Work on metalloprotein export in bacteria, and protein import in
154 er DNA with an affinity equal to that of the metalloprotein (Fe-SoxR), but lacks significant ability
155 ns and the redox activities of the resulting metalloprotein films.
156 itric oxide synthases (NOSs) are multidomain metalloproteins first identified in mammals as being res
157    The mechanism is discussed with regard to metalloprotein folding and metalloprotein design.
158                                          The metalloprotein follows the halogenation cycle, whereby c
159 environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection
160 g a vector, we introduced an MRI reporter, a metalloprotein from the ferritin family, into specific h
161 rometry (ICP-MS) to characterize cytoplasmic metalloproteins from an exemplary microorganism (Pyrococ
162      To overcome this limitation, artificial metalloproteins have been created by incorporating compl
163 Detailed pathways for metal ion release from metalloproteins have been difficult to elucidate by clas
164 uring thermodynamic metal ion selectivity of metalloproteins have been performed, and the major deter
165                                Consequently, metalloproteins have key roles in most biological proces
166                                         Many metalloproteins have the capacity to bind diverse metals
167 elationship between the activity of the zinc metalloprotein IDE and glucose homeostasis remains uncle
168 at protein phosphatase 1 may be an iron/zinc metalloprotein in vivo.
169 gate the structure-function relationships of metalloproteins in a minimal, well-defined and controlle
170  sensitive visualization and quantitation of metalloproteins in biological samples.
171 these biological assemblies by encapsulating metalloproteins in sol-gel silica glass and letting mobi
172 ssion protocols, sensitivity-enhanced NMR of metalloproteins in solution, the investigation of solven
173 owever, this technique cannot be extended to metalloproteins in solution.
174 actors represent the largest single class of metalloproteins in the human genome.
175                    Little is known about how metalloproteins in the secretory pathway obtain their me
176 sfer Fe-S clusters to the appropriate target metalloproteins in vivo.
177 llowed to determine epsilon values for other metalloproteins in which metal binding contributes to th
178 ded the Rosetta design methodology to design metalloproteins in which the amino acid (2,2'-bipyridin-
179                   The transferase is a Zn/Fe metalloprotein, in which the metal ions stabilize the st
180 ginosa azurin is a 128-residue beta-sandwich metalloprotein; in vitro kinetic experiments have shown
181                                     For some metalloproteins (including all transferrin family member
182 ty during cofactor assembly for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-de
183 e of the reduction potential E degrees for a metalloprotein indicates that the protonation state of a
184 tegy for the discovery of lead fragments for metalloprotein inhibition.
185 at despite their ability to bind metal ions, metalloprotein inhibitors are not prone to widespread of
186 e selected as well as several other reported metalloprotein inhibitors in order to represent a broad
187                        Representative ligand-metalloprotein interaction energies are obtained by subs
188                             Metal centers in metalloproteins involve multiple metal-ligand bonds.
189 tantial variations in concentrations of iron metalloproteins involved in nitrogen fixation and photos
190 y definition, the release of metal ions from metalloproteins involves the disruption of multiple meta
191         An important feature of the designed metalloprotein is its two cationic redox centers embedde
192                     Cyt c, a heme containing metalloprotein is located in the intermembrane space of
193         Quality computational description of metalloproteins is a great challenge due to the vast spa
194  of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bi
195 nition of biologically active amino acids of metalloproteins is elicited by the presence of specific
196  analyze accurately and precisely individual metalloproteins is of increasing importance.
197 ting that species-specific ID-MS analysis of metalloproteins is possible.
198 nalysis of unpaired electron spin density in metalloproteins is presented, which allows a fast and ro
199  structural determination of active sites of metalloproteins is presented.
200 , a product of catabolism of heme-containing metalloproteins, is a key inducer of ROS.
201 parison to recent successes in designing non-metalloproteins, it is even more challenging to rational
202 the problems in the receptor-based design of metalloprotein ligands due to inadequacies in the force-
203 ctive intermediates and transition states in metalloproteins may be widespread in nature.
204                                        Other metalloproteins may have similarly adapted to using mang
205                                           In metalloproteins, metal centers serve as active sites for
206  series of 24 inorganic, organometallic, and metalloprotein/metalloporphyrin model systems in S = 0,
207  across a 16-mer helical bundle (three-helix metalloprotein) modified with a capping CoIII(bipyridine
208                                              Metalloproteins (MPs) comprise one-third of all known pr
209 allenging to design metalloproteins than non-metalloproteins, much progress has been made in this are
210 gn of a structural and functional model of a metalloprotein, nitric oxide reductase (NOR), by introdu
211                            The two-component metalloprotein nitrogenase catalyzes the reductive fixat
212           We conclude that this bifunctional metalloprotein of the osteoclast is required for normal
213 als an organism assimilates and identify its metalloproteins on a genome-wide scale.
214 owever, existing MRI reporter genes based on metalloproteins or chemical exchange probes are limited
215 e show that the technique can be extended to metalloproteins or complex:protein interactions.
216  roles of Zn2+ donation to, or removal from, metalloproteins, or Zn2+ storage in vegetative plant tis
217 13C strongly hyperfine-shifted resonances in metalloprotein paramagnetic centers.
218 n microcrystalline powders of a paramagnetic metalloprotein permit NMR crystallography.
219                  ESI-TOF mass spectra of the metalloproteins present in nondenaturing solutions exhib
220 f CusF (log K = 14.3 +/- 0.1), a periplasmic metalloprotein required for the detoxification of elevat
221 h Institute is a web-accessible resource for metalloprotein research.
222 ting from in situ chemical manipulation of a metalloprotein sample.
223 ectron paramagnetic resonance spectra of the metalloproteins show that encapsulation in sol-gel glass
224 -nitrosylation and denitrosylation involving metalloproteins, SNO lyase(s) and GSNO reductase.
225 nhance the understanding of similar sites in metalloproteins, specifically cobalt-substituted zinc en
226 butions of metal-protein interactions toward metalloprotein stability is largely due to an inability
227 ontribution of a Zn(II)-(S.Cys)4 site toward metalloprotein stability relevant to classic structural
228  Here we show that a de novo designed Zn(II) metalloprotein stabilizes a chemically reactive organic
229 n and evaluation of an isotopically enriched metalloprotein standard for use as a calibrant in specie
230 eins as a class, revealing new insights into metalloprotein structure and function.
231 etail is critical to a full understanding of metalloprotein structure--function relationships.
232 n provide a reliable balanced description of metalloproteins' structure, dynamics, and electronic str
233 binding site that appears to be unique among metalloproteins studied to date.
234                   Among them, there are four metalloprotein subunits, including a 113 kDa iron-sulfur
235 ins two histidine motifs resembling those of metalloproteins such as fatty acid desaturases.
236 ficking required for the assembly of complex metalloproteins such as nitrogenase.
237 te (67)Zn NMR spectra of model compounds for metalloproteins, such as [H(2)B(3,5-Me(2)pz)(2)](2)Zn (p
238 em that affected to the levels of metals and metalloproteins, such as MT, Cu/Zn-SOD, or Mn-CA, the br
239 for understanding the mechanism of important metalloproteins, such as photosystem II.
240 lar procedures should be generally useful in metalloprotein systems.
241 though it is much more challenging to design metalloproteins than non-metalloproteins, much progress
242 oxygen ((1)O(2)) is mediated by ChrR, a zinc metalloprotein that binds to and inhibits the activity o
243             Transferrin (Tf) is an enigmatic metalloprotein that exhibits a profound conformational c
244 for the assembly of periplasmic and secreted metalloproteins that are essential for survival in extre
245  metal ions, with emphasis on copper(II), to metalloproteins that are hallmarks of these diseases - a
246           Transferrins constitute a class of metalloproteins that are involved in circulatory iron tr
247         Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular syst
248 es to date are the AHL lactonases, which are metalloproteins that belong to the metallo-beta-lactamas
249              [FeFe]-Hydrogenases are complex metalloproteins that catalyze the reversible reduction o
250             Superoxide dismutases (SODs) are metalloproteins that protect organisms from toxic reacti
251 s even more challenging to rationally design metalloproteins that reproduce both the structure and fu
252  we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains
253        Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenu
254  built from interactions observed in simpler metalloproteins, they contain novel features that may be
255                                          For metalloproteins to acquire the right metals, metal senso
256             Biology employs three classes of metalloproteins to cover the majority of the 2-V range o
257 re important biological ligands that bind to metalloproteins to function crucially in processes such
258                         Selective binding by metalloproteins to their cognate metal ions is essential
259 e structure data from two of the purified Zn metalloproteins to validate predicted metalloprotein bin
260 uctural characterization of de novo designed metalloproteins together with determination of chemical
261                         Four iron-containing metalloproteins (transferrin, myoglobin, hemoglobin, and
262 n of cytochrome c (cyt c), a heme containing metalloprotein using its specific monoclonal antibody.
263 shifts in paramagnetic metalloporphyrins and metalloproteins using quantum chemical methods should op
264 uctural and dynamical determination of large metalloproteins using solid-state nuclear magnetic reson
265                       That human BVR is a Zn metalloprotein was further substantiated by 65Zn exchang
266               A de novo designed coiled-coil metalloprotein was prepared that uses electrostatic inte
267 residues were coordinated with metals and 15 metalloproteins were endogenously modified supporting me
268  not equally active and due to the fact that metalloproteins were rarely used as drug targets.
269  the geometric structure and the dynamics of metalloproteins, when NMR parameters are available of nu
270     An extra layer of complexity is added in metalloproteins, where a metal cofactor participates in
271 es share properties with the active sites of metalloproteins, where function is correlated strongly w
272    Phage T4 gene 32 protein (gp32) is a zinc metalloprotein which binds cooperatively and preferentia
273 redoxins, rusticyanin is a copper-containing metalloprotein, which is composed of a core beta-sandwic
274       Pho8 appears to be a rare example of a metalloprotein whose stability is regulated by its metal
275           PerR is a dimeric, Zn2+-containing metalloprotein with a regulatory metal-binding site that
276 1 periplasmic, catalytic domain to be a zinc metalloprotein with an alkaline phosphatase/sulphatase f
277 characterization revealed a Bpy-Ala-mediated metalloprotein with the ability to bind divalent cations
278 after purification, indicating that Mca is a metalloprotein with zinc as the native metal.
279 cellular damage initiated by the reaction of metalloproteins with H2O2.
280 ethod also facilitates the de novo design of metalloproteins with novel structures and functions, inc
281 ng the rupture mechanism of metal centers in metalloproteins with unprecedented resolution by using s
282  purified STM1808 suggests that it is a zinc metalloprotein, with histidine residues H32 and H82 requ
283 detoxification, also deliver zinc to certain metalloproteins within intracellular compartments.
284     An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins.
285 essful design of a structural and functional metalloprotein would greatly advance the field of protei
286 nt with the hypothesis that E4 34k is a zinc metalloprotein, zinc binding by baculovirus-expressed E4

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