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1 ucture less than 5 A (fraction of completely folded structures).
2 e known to confer structural rigidity to the folded structure.
3 ropagating local chirality via a dynamically folded structure.
4 dicating that it results from a higher order folded structure.
5 d three single T loops also adopt a parallel folded structure.
6 eriments demonstrated that p58C forms a well folded structure.
7 ugh it is well protected from solvent in the folded structure.
8 otein binding was affected by sR6's distinct folded structure.
9 structured in the transition state as in the folded structure.
10 l causes Hmg2p to undergo a change to a less folded structure.
11  denaturation, to probe the stability of the folded structure.
12 pentapeptide derived from Hsp90 stabilises a folded structure.
13 tially different under conditions that favor folded structure.
14 ior of the barrel, thereby destabilizing its folded structure.
15 associated with the C-terminal domain in the folded structure.
16 in the unfolded state, as well as the native folded structure.
17 milar to the native fold than any individual folded structure.
18 beta-amino acids that adopts a cooperatively folded structure.
19  d(GGTTGGTGTGGTTGG), inducing a unimolecular folded structure.
20 s can be functional even in the absence of a folded structure.
21 olecules likely adopt a co-transcriptionally folded structure.
22 rmation of the third disulfide and the final folded structure.
23 ranched aliphatic side chain contacts in the folded structure.
24 extensive network of interactions across the folded structure.
25 hancement in the formation of the N-terminal folded structure.
26 rther increased selection for the N-terminal folded structure.
27 ce atomically characterized to retain a well-folded structure.
28 the fluorescence properties of the resulting folded structure.
29 he forces that maintain the integrity of the folded structure.
30 ide is random coil-like and lacks a dominant folded structure.
31 onformational change from a random coil to a folded structure.
32 to determine dynamic features related to the folded structure.
33 y of each other (d approximately 3 A) in the folded structure.
34 amics of hydrated tRNA while stabilizing its folded structure.
35 nfolding of an i-motif through the partially folded structure.
36 from H/D exchange, implying an intrinsically folded structure.
37 hroism spectra and 1D-NMR spectra typical of folded structures.
38 ange, consistent with the NTDs having formed folded structures.
39 called LoopA, LoopB, and LoopC, adopt stable folded structures.
40 mino acids and their microenvironment in the folded structures.
41  of sequence space most likely to yield well folded structures.
42 only the desired fold but also alternatively folded structures.
43 he presence of a heterogeneous population of folded structures.
44 llow native proteins to acquire their unique folded structures.
45 generate de novo proteins with cooperatively folded structures.
46 odel (GNM) recently introduced for analyzing folded structures.
47 ificant differences were detectable in their folded structures.
48 ficulty associated with obtaining pure, well-folded structures.
49  their columnar phases are more ordered than folded structures.
50 lex structures, and two form macrocyclic 1,3-folded structures.
51 radiation followed by aging to restore fully folded structures.
52 thrusting GLUT3's microstate sampling toward folded structures.
53 n the solid state, revealing compact, highly folded structures.
54 he S-S bridge as a natural building block in folded structures.
55 ying membrane proteins and determining their folded structures.
56 rmal and chemical stability of the resultant folded structures.
57 tion results in the formation of a partially folded structure, a stable core comprising the C-termina
58 rally occurring proteins sample the space of folded structures accessible to the polypeptide chain.
59 e PUA domain bind RNA molecules with complex folded structures, adding to the growing collection of n
60                                          The folded structure agrees excellently with the NMR NOE dat
61 tch: loss of the bound zinc ion disrupts the folded structure, allowing the ligand cysteine residues
62 ide oligomers have been shown to form stable folded structures analogous to those encountered in natu
63 amolecular interactions that favor the final folded structure and a less specific set of intermolecul
64 m half-life in vivo without compromising its folded structure and activity.
65 erefore, protein models that encode only the folded structure and are energetically unfrustrated (Go-
66           We have experimentally deduced the folded structure and characterized the ssDNA promoter pr
67 ally disordered proteins lack a well-defined folded structure and contain a high degree of structural
68 , qualitatively indicating disruption of the folded structure and development of static conformationa
69               Adenine binding stabilizes the folded structure and significantly decreases the unfoldi
70 ingers are required for processing only as a folded structure and that the location but not the ident
71 helicase activity with substrates containing folded structures and 5' single-stranded tails, suggesti
72  show how primordial functions are linked to folded structures and how their interaction with cofacto
73 e of the protein is a triple funnel with two folded structures and one misfolded structure that are s
74 pro alpha 1 and C-pro alpha 2 have different folded structures and stability.
75 , leading to the formation of only partially folded structures and the disappearance of TADs from con
76  of proteins (for example, three-dimensional folded structure) and other natural materials.
77 IDPs/IDRs) that do not adopt a dominant well-folded structure, and therefore remain "unseen" by tradi
78 e the residues that interact the most in the folded structure, and they are often residues that displ
79         However, functional RNAs have stable folded structures, and such structures are much more dif
80 any different protein sequences have similar folded structures, and that there is a relatively high p
81  stacking, and/or binding of Mg2+ within the folded structure are responsible for stabilizing the P4-
82 wo residues, both parallel- and antiparallel-folded structures are able to form.
83 sis reveals that marginally stable partially folded structures are also present in the nominally unfo
84 NMR studies provide strong evidence that the folded structures are conserved in solution.
85 ymers like RNA interconvert between multiple folded structures are critical for their cellular functi
86 en cyanide chains is observed, even when the folded structures are energetically favored.
87                                The partially folded structures are formed predominantly by coiled coi
88 ability of SCHEMA to identify chimeras whose folded structures are likely not to be disrupted by reco
89        Overall, our results imply that the 2 folded structures are preencoded by the alpha-synuclein
90 led an increased order and stability of sRNA folded structure as a result of L7 binding.
91  the F helix is important in stabilizing the folded structure, as shown by the instability of the 1-1
92 thalpy, Deltanion, and DeltanW, the dominant folded structure at high salt is most likely the antipar
93 st to the significant destabilization of the folded structure at high temperatures, Trp-cage cold den
94             DNA containing d(ATTCT)9 forms a folded structure at relatively low temperatures, whereas
95 ition is observed with a folded or partially folded structure at very low (<10 wt % H(2)O) and high (
96 y of nucleosomal arrays to form higher-order folded structures at all ionic conditions tested.
97 e is greatly influenced by the GC content of folded structures at the mRNA entry site.
98 ty through specific amino acid sequences and folded structures at their active sites.
99                                       Stably folded structures based on the design principle describe
100                                         This folded structure becomes destabilized and loses the U*U
101                                   When their folded structure breaks down, protein chains do not beco
102   Thermodynamics not only dictates the final folded structure but also is the driving force for the e
103 des, thus enabling not only access to stable folded structures but also the incorporation of exocycli
104 ant amount of alpha-helix, indicating that a folded structure can be maintained despite the loss of i
105                                 Furthermore, folded structures can be transferred between aqueous sol
106           On the other hand, the fraction of folded structures changes more slowly with time and fits
107 veal that the PEMV-1 pseudoknot is a compact-folded structure composed almost entirely of RNA triple
108 ncy virus type 1 (HIV-1) genome has a highly folded structure, comprising at least two RNA stem-loops
109  be maximized when a well defined pathway of folded structure connects the two sites.
110                                         This folded structure consists of three short helical segment
111 l, making possible the formation of a stable folded structure containing a single A:T base pair.
112 idence that tertiary interactions within the folded structure contribute to product binding energy.
113 dration in the skin it is plausible that the folded structures contribute to both the elasticity and
114       OPUS-Dom generates a large ensemble of folded structure decoys by VECFOLD and labels the domain
115  helices that are prominently exposed in the folded structure decreases the ATPase stimulation by the
116 , the decreased free energy in the partially folded structure (DeltaG(unfold) 10.4 +/- 0.7 kcal/mol)
117 hypothesize the SUMO1 E2 enzyme recognizes a folded structure-dependent motif that includes residues
118 human MTAP require the inhibitors to adopt a folded structure, displacing the phosphate nucleophile f
119 the formation of a compact, intramolecularly folded structure dominated by two stacked guanine quarte
120 zed, indicating that the protein retains its folded structure during the labeling process.
121 ynucleotide tails was studied at pH 5.0, the folded structure entered the nanocavity of alpha-HL from
122 table hairpin with no evidence for any other folded structure even at low pH.
123 ts, favorable conditions for the creation of folded structures exist.
124  data provided evidence that elements of the folded structure form at temperatures well below the Tm,
125 s of 1, 3, 4, 6, and 7 indicate that similar folded structures form in chloroform.
126         The peptide segments in the residual folded structures form the "building block" for aggregat
127 iments reveal NOE contacts typically seen in folded structures formed by guanine quartets, such as th
128         The explanation proposed is that the folded structure found at the telomere helps appose the
129  convergence and identification of correctly folded structures from a large number of simulations.
130 y and physical properties is readily seen in folded structures from intestinal villi and pollen grain
131  clear energetic separation of the correctly folded structures from misfolded structures for the two
132         Origami describes rules for creating folded structures from patterns on a flat sheet, but doe
133 ucleotides that could not form the compactly folded structure had markedly reduced half-lives (t1/2 f
134 , turn, and beta-strand motifs of biopolymer folded structures have been found to prevail also in non
135 r removal produces apo-azurin which adopts a folded structure identical to that of the holo-form.
136 nternal ribosome entry site (CrPV-IRES) is a folded structure in a viral mRNA that allows initiation
137 egments associate noncoaxially in the active folded structure in a way that brings catalytically impo
138 does not prevent the adoption of the natural folded structure in any of the circular proteins.
139 for the intermediate nature of the partially folded structure in comparison to the i-motif.
140 ed that the TDP-43 N terminus encodes a well-folded structure in concentration-dependent equilibrium
141                Here, we show that the stable folded structure in headpiece is localized to a subdomai
142  switch, resulting in destabilization of the folded structure in solution and thereby promoting the i
143 nsfer demonstrated enhanced stability of the folded structure in the context of a four-way helical ju
144 f the aptamer domain, adopts a predominantly folded structure in the presence of Mg(2+) alone.
145 at the engineered zinc finger motif adopts a folded structure in which the native beta-sheet arrangem
146  non-modular loop prototypes combine to form folded structures in protein domain evolution.
147 peratures, it appears that the mutants adopt folded structures in solution that are virtually identic
148 R chemical shifts supports the assignment of folded structures in solution.
149 herichia coli, and to adopt stable monomeric folded structures in solution.
150 l six consensus proteins adopt cooperatively folded structures in solution.
151  little sequence homology and generally lack folded structures in the absence of their targets, aspec
152                                              Folded structures in the coding region of an mRNA repres
153                                              Folded structures in the DNA template, such as hairpins
154 ane-reconstituted GLIC and ELIC both exhibit folded structures in the minimal PC membranes that stabi
155                             All mutants have folded structures in their lipid-free state, however the
156 ediate conformation as a collection of fully folded structures in which each of them contains a set o
157 one of the two strands to form a more stable folded structure, in our case the CAGG strand, explains
158                     These ions stabilize the folded structures, in part, by accumulating in regions o
159                         The stability of the folded structure increases with the charge of the polyam
160 rnative guide regions demonstrated that sRNA folded structure induced by specific guide sequences imp
161  the photoinduced unfolding of the helically folded structures initiates from relatively flexible par
162 assembled aggregates, this work introduces a folded structure into soft matters formed by amphiphiles
163                                    A beta 42 folded structure is characterized by a turn in the C-ter
164                             This ideal chain-folded structure is corroborated by annealing studies on
165              This implies therefore that its folded structure is important for its biological activit
166 onformational alterations, while the overall folded structure is maintained.
167 anced stability of a pseudorotaxane inside a folded structure is measured to be DeltaG = ca. 0.5 kcal
168 obtained by simulation, we see that the mean folded structure is more similar to the native fold than
169         We find that at room temperature the folded structure is more stable, whereas at higher tempe
170 her that the ability to adopt an intrastrand folded structure is not sufficient for expansion, or tha
171 steric covalent linkages indicates that this folded structure is stable against displacement by the p
172 dicator of the residues not belonging to the folded structure is suggested.
173                         This class of chiral folded structures is achieved by controlling the reactiv
174  two positive charges closer together in the folded structures is compensated for by the additional h
175 or OFF-state with their catalytic heads in a folded structure known as the interacting-heads motif (I
176         An exposed hydrophobic pocket in the folded structure may be sufficient to confer the observe
177 ximity in either the primary sequence or the folded structure may differ considerably.
178 n in photolyase and cryptochrome, and such a folded structure may have a functional role in initial p
179 roduced in Escherichia coli had little or no folded structure, measured by NMR and CD.
180 arrays can neither condense into extensively folded structures nor cooperatively oligomerize in MgCl(
181 ations impart thermodynamic stability to the folded structure not achievable with unmodified DNA.
182 BM antiserum indicated that acquisition of a folded structure occurred with a similar time course in
183 ically possible to inhibit by disrupting the folded structure of a protein or, in the limit, to bind
184 in emerges from the ribosome can specify the folded structure of a protein.
185                            The amyloidogenic folded structure of Abeta is important for the formation
186 r this cotranslational folding can alter the folded structure of an encoded protein in vivo, versus t
187           Previously we found that the whole folded structure of both polypeptides as well as specifi
188 ical for specifying the unique cooperatively folded structure of KIX.
189                                 The residual folded structure of locally unfolded apoSOD1 corresponds
190 ally employed to assess the stability of the folded structure of mouse mammary tumor virus pseudoknot
191 atures of this algorithm, we incorporate the folded structure of mRNA.
192 ane, an inhaled anesthetic, destabilizes the folded structure of myoglobin.
193  of the PxxP motif within the context of the folded structure of Nef.
194 so that the mechanical stress imposed by the folded structure of one subunit causes the other subunit
195 tin, such that the free energy stored in the folded structure of one subunit is used to drive unfoldi
196 o contribute to the overall stability of the folded structure of peptides and proteins.
197  most anti-PrP antibodies were hidden in the folded structure of PrP(RES), even though these epitopes
198 asis of thermal denaturation, we show that a folded structure of T30177 is much more stable than that
199                 Consequently, the N-terminal folded structure of the Arctic mutants closely resembles
200                                          The folded structure of the bound IDP appears to be defined
201                       However, the secondary folded structure of the DNA binding domain of RAR and RX
202            Thus, our study suggests that the folded structure of the H4 basic patch in the nucleosome
203 ses this results in severe distortion of the folded structure of the junction.
204 essibility to proteases, which indicated the folded structure of the loops or their shielding by the
205                                    Using the folded structure of the monounsaturated fatty acid obser
206 nterior surface of the binding cavity in the folded structure of the oligomer.
207 P4, P6, and P6a, indicating that a partially folded structure of the P4-P6 domain is required.
208 roduce larger particles in which neither the folded structure of the polymer nor the fusogenic proper
209                         Stabilization of the folded structure of the protein by residue substitution
210             Ribosomal proteins stabilize the folded structure of the ribosomal RNA and enable the rec
211 t the ligand-free state is often a partially folded structure of the RNA, with conformational heterog
212     Human GAPDH was found to destabilize the folded structure of the stem-loop IIIa RNA based upon ob
213 .1a (P13) and P2 and P5c (P14) stabilize the folded structure of the Tetrahymena group I intron.
214 trongly support the importance of the stable folded structure of this family of peptides for binding
215  presented in this work show that the unique folded structure of TolC reflects a unique assembly path
216 gnesium ions are crucial for stabilizing the folded structure of tRNA.
217                           In contrast to arm-folded structures of cohesin and condensin, Smc5 and Smc
218 h show more hydrogen bonds in representative folded structures of hydrated 1,7-diammoniumheptane vers
219 in packing in specifying and stabilizing the folded structures of proteins.
220 essential for specifying and stabilizing the folded structures of proteins.
221 The computed lowest-energy manifolds for the folded structures of the two beta-hairpins agree closely
222                           Predictions of the folded structures of these box C/D snoRNA-like miRNA pre
223  energy and examine the stability of various folded structures of these molecules along a well-define
224                        This tandem "flexible-folded" structure of the polypeptide chain derived for t
225 pha7) is disordered in solution and adopts a folded structure on MTs, indicating that TPX2(alpha5-alp
226 rase that are also nearly identical in their folded structures, only the mitochondrial form (mAAT) is
227 inding: whether the free TAZ1 domain forms a folded structure or behaves as a molten globule will hav
228 der conditions that promote formation of the folded structure or complex, as well as 'control' condit
229 F-box proteins (for example, substrates with folded structures or limited length) that are incompatib
230 to overcome for the construction of discrete folded structures, particularly for the development of a
231 e unfolded state and flexible linkers in the folded structure play essential roles in protein stabili
232 hat interresidue contacts not present in the folded structure play little or no role in the self-asse
233 onation of the heterocycle leads to a rigid, folded structure presenting a network of hydrogen bonds.
234                           It forms a compact folded structure, presenting a loop between Cys8 and Cys
235                    Lack of requirement for a folded structure prompted us to investigate antitumor pr
236                                  The initial folded structure rearranges to form a beta-sheet like st
237 tation, L92V, near the PR active site in the folded structure recently emerged during TL-3 selection.
238 h an additional emission, but also induces a folded structure, reducing molecular stacking and facili
239 Although the peptide does not adopt a stable folded structure, regions of unstable structure exist ov
240 i-donor-acceptor subunits provides access to folded structures reminiscent of the tertiary structure
241 d equimolar amounts of the N- and C-terminal folded structures, respectively.
242            Heating native p53 to destroy the folded structure restores DNA-independent acetylation si
243 odel three-helix-bundle protein with a known folded structure, reveal that 13C-labeled residues in th
244 lding, and variants adopt distinct partially folded structures seen along the OLF(WT) urea-unfolding
245                The i-motif and the partially folded structure share similar rupture forces of 22-26 p
246 or-acceptor interactions responsible for the folded structure shows a high constant rupture force ove
247             Brain HA forms three dimensional folded structures similar to the macroscopic appearance
248 ackbone modifications but nevertheless adopt folded structures similar to those of natural polypeptid
249 d RNA structures, although distinct from the folded structure stabilized by multivalent cations.
250  a replica exchange algorithm that samples a folded structure starting from a completely unfolded sta
251 cid sequences can give rise to more than one folded structure, such as for proteins that undergo larg
252 ype of photoproduct might also form in other folded structures, such as G-quadruplexes and i-motif st
253 riety of sequences prone to the formation of folded structures, such as long hairpins and quadruplexe
254 lphFold2 uncovered rapid convergence towards folded structure, suggesting that a folding vocabulary e
255 sed tendency to form alternate, incompletely folded structures, suggesting a more complex picture of
256  events within domains, which might preserve folded structure, target functional residues more freque
257      Despite having a considerably different folded structure than conventional dsRNA, the cytotoxici
258 than the wild-type protein, it adopts a well-folded structure that can be chemically denatured in a c
259 ults suggest that domain III adopts a stably folded structure that can mediate binding of tick-borne
260 h telomeres beyond a threshold length form a folded structure that links the chromosome terminus to t
261 ree-dimensional structure: a single-stranded folded structure that makes multiple contacts with the a
262  this family of pseudoknots adopts a tightly folded structure that maximizes the cooperativity and co
263                           RNAs adopt diverse folded structures that are essential for function and th
264 l protein design to investigate the space of folded structures that can be generated by tandem repeat
265 olecules can form complex, three-dimensional folded structures that have surprisingly sophisticated f
266                     Both RRM3 and RRM4 adopt folded structures that NMR data show to be similar to th
267 acent CCG trinucleotides, trapping partially folded structures that readily base pair with another RN
268     Riboswitches are RNAs that form complex, folded structures that selectively bind small molecules
269  reduced rate of motion backward depended on folded structures that were only present with longer lin
270  protein and its conformation in the overall folded structure, the amino acid sequence corresponding
271 and F488L C-termini mutants retained stable, folded structures, the secondary structures of both muta
272                                          The folded structure then is derived via a direct molecular
273  results can be rationalized in terms of the folded structure, there are a number of surprises.
274 f deltaX(++), which is the distance from the folded structure to the unfolding transition state.
275  mutations were required to restore a stably folded structure to this RNA.
276          These results suggest that a stable folded structure together with three or more basic amino
277  stable molten globules but lacks a uniquely folded structure-translocase mutants that rescued export
278                             In the correctly folded structure, two of the three tyrosines putatively
279                In contrast r(AUUCU)9 forms a folded structure under physiologically reasonable condit
280 that the precursor protein achieves a stable folded structure upon dilution from urea, suggesting tha
281 mbrane transport machineries can translocate folded structures, we overexpressed the 17-kDa subunit o
282 the 2-10 mum range and the retention of some folded structure were associated with an increased respo
283                         First, potential VPg folded structures were identified, yielding a suite of p
284 and molecular modeling studies, two types of folded structures were proposed and several conformation
285  show that: (i) 16S rRNA remains in a highly folded structure when it is bound to S15; (ii) in the ab
286                    Other motifs form complex folded structures when transcribed as RNA molecules and
287 ffold via overcrowded alkenes, adopt an anti-folded structure, which upon oxidation convert to singly
288 n extended state, we obtained an ensemble of folded structures, which is on average 1.7A and 1.9A awa
289       However, unique to the NMR, are highly folded structures, whose characteristic morphology is de
290 cs calculations yielded an unusually stable, folded structure with a double "S"-like bend incorporati
291 oglobin molten globule has a complex, partly folded structure with a folded A[B]GH subdomain; the fac
292 nd adult epithelium develops to form a multi-folded structure with elaborate connective tissue and mu
293 bilization of FAS1-4 and induces a partially folded structure with increased surface exposure of hydr
294  The retained fragments acquired a partially folded structure with intra-chain disulfide bonds and co
295 de oligomers can assemble into cooperatively folded structures with potential application in enzyme d
296 number may result from the formation of more folded structures with similar stability rather than few
297 showed that at pH 5.0, all five circles form folded structures with similar stability, while at pH 7.
298 nian walk in the conformational space to the folded structure, with each step controlled by k(alpha).
299 t are capable of acquiring unique and stably folded structures would be valuable in the examination o
300 -residue description of the evolution of the folded structure, yet contains many fewer adjustable par

 
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