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1 with its nucleotide exchange factor eIF2B by electron cryomicroscopy.
2 membrane and analyze its oligomeric state by electron cryomicroscopy.
3 n15 (epsilon15) particle, by single-particle electron cryomicroscopy.
4 hree-dimensional reconstructions obtained by electron cryomicroscopy.
5 acillus stearothermophilus taken by low-dose electron cryomicroscopy.
6 d empty CPV determined at 13-A resolution by electron cryomicroscopy.
7 virus type 1 (HSV-1) B capsid, determined by electron cryomicroscopy.
8 een determined at 8.5 angstrom resolution by electron cryomicroscopy.
9 were analyzed using biochemical methods and electron cryomicroscopy.
10 the scaffolding protein have been studied by electron cryomicroscopy.
11 ist-bound GluN1-2D NMDARs by single-particle electron cryomicroscopy.
12 S)-stabilized PfAct1 filaments determined by electron cryomicroscopy.
13 es of interest, and imaged the vesicles with electron cryomicroscopy.
14 .1 angstrom-resolution using single particle electron cryomicroscopy.
15 um thermophilum, obtained by single-particle electron cryomicroscopy.
16 ermined its structure to 3.6-A resolution by electron cryomicroscopy.
17 c using single-particle electron cryomicroscopy.
18 of SERCA in the presence of wild-type SLN by electron cryomicroscopy.
19 esolutions between 2.5 and 5.0 A by means of electron cryomicroscopy.
20 ubiquitylated nucleosome, and validate it by electron cryomicroscopy.
21 of EBOV, both determined by single-particle electron cryomicroscopy.
22 tion of 3.8 A, determined by single-particle electron cryomicroscopy.
23 nward-facing conformation by single-particle electron cryomicroscopy.
24 osin at a resolution of 6.5 A, determined by electron cryomicroscopy.
25 s confidence in a structure determined using electron cryomicroscopy.
28 implex virus type 1 virions were examined by electron cryomicroscopy, allowing the three-dimensional
36 orbol-13-acetate to obtain HHV-8 capsids for electron cryomicroscopy and computer reconstruction.
38 plied X-ray crystallography, single-particle electron cryomicroscopy and electrophysiology to rat NMD
50 id isolated from VEEV has been determined by electron cryomicroscopy and image reconstruction and rep
52 e was determined to 12-A resolution by using electron cryomicroscopy and image reconstruction techniq
54 erminus of VP2 within the core, we have used electron cryomicroscopy and image reconstruction to dete
57 d barrel clathrin coat at 21 A resolution by electron cryomicroscopy and of the clathrin terminal dom
58 atelet integrin alpha(IIb)beta(3) derived by electron cryomicroscopy and single particle image recons
59 annel (also known as RyR1) was determined by electron cryomicroscopy and single particle reconstructi
60 ith an ATP-ADP mixture at 11 A resolution by electron cryomicroscopy and single-particle averaging of
61 ion of human fatty acid synthase obtained by electron cryomicroscopy and single-particle image proces
62 -density lipoprotein (LDL) was obtained from electron cryomicroscopy and single-particle image recons
64 te receptor (InsP3R1) has been determined by electron cryomicroscopy and single-particle reconstructi
67 o directly locate the KSHV SCP, we have used electron cryomicroscopy and three-dimensional reconstruc
68 ime allowing direct structure comparisons by electron cryomicroscopy and three-dimensional reconstruc
70 protein (FKBP12), have been characterized by electron cryomicroscopy and three-dimensional reconstruc
74 ng time-resolved phosphorescence anisotropy, electron cryomicroscopy, and all-atom molecular dynamics
75 We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to i
76 Here we demonstrate using genomic analysis, electron cryomicroscopy, and image reconstruction that t
78 ysis, x-ray crystallography, single-particle electron cryomicroscopy, and molecular dynamics simulati
80 mensional crystals of CydDC were analyzed by electron cryomicroscopy, and the protein was shown to be
81 these structures, X-ray crystallography and electron cryomicroscopy are capable of determining struc
82 we are now firmly within the "atomic age" of electron cryomicroscopy, as these studies can reveal ato
84 ex from Neurospora crassa by single-particle electron cryomicroscopy at 3.3 angstrom resolution, show
85 type 1 RyR (RyR1), solved by single-particle electron cryomicroscopy at an overall resolution of 4.8
86 formed by Abeta(1-40) peptide, determined by electron cryomicroscopy at approximately 8-A resolution.
87 ) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre
88 m falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (R
89 the structure of a K. lactis CBF3 complex by electron cryomicroscopy at ~4 angstrom resolution and co
90 n of the Pr-minus and wild-type B capsids by electron cryomicroscopy, at an unprecedented 12.5-angstr
93 res of many proteins cannot be determined by electron cryomicroscopy because the individual proteins
96 biochemical reconstitutions, single-particle electron cryomicroscopy, cross-linking mass spectrometry
100 A protease with its transmembrane domains by electron cryomicroscopy (cryo-EM) and atomic structure f
104 large high-symmetry viruses, single-particle electron cryomicroscopy (cryo-EM) has achieved the deter
112 Here we present 3 to 3.5 angstrom resolution electron cryomicroscopy (cryo-EM) structures comprising
118 Here, we have used single-particle analysis electron cryomicroscopy (cryo-EM) to determine structure
120 ity called the "stutter." Here, we have used electron cryomicroscopy (cryo-EM) to determine the struc
121 tate optimization of lead compounds, we used electron cryomicroscopy (cryo-EM) to determine the struc
123 captured images of this transient process by electron cryomicroscopy (cryo-EM) to reveal the structur
125 ormed mass-per-length (MPL) measurements and electron cryomicroscopy (cryo-EM) with 3D reconstruction
129 nt an integrated approach of single-particle electron cryomicroscopy (cryo-EM), computational modelin
139 infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle ana
140 FcRY's pH-dependent binding mechanism using electron cryomicroscopy (cryoEM) and small-angle X-ray s
141 r Epinephelus malabaricus, was determined by electron cryomicroscopy (cryoEM) and three-dimensional r
142 f antigen-antibody complexes.Single-particle electron cryomicroscopy (cryoEM) can circumvent some of
143 possible to thin and vitrify a specimen for electron cryomicroscopy (cryoEM) faster than proteins di
146 We have combined image reconstructions from electron cryomicroscopy (cryoEM) of bovine papillomaviru
148 a template:primer RNA duplex, determined by electron cryomicroscopy (cryoEM) to a resolution of 2.5
153 sion electron microscopy (TEM), transmission electron cryomicroscopy (cryoTEM), and thermogravimetric
154 ific structural information that complements electron cryomicroscopy data and defines targets and str
157 Fitting of the modeled PapA subunit into the electron cryomicroscopy data provides a detailed view of
158 procapsid and infectious virion derived from electron cryomicroscopy density maps determined at 3.8-
159 to the previously determined 25-A-resolution electron cryomicroscopy density maps of HAstV allowed us
162 s complex I, determined to 5-A resolution by electron cryomicroscopy, described the structure of the
164 study, we analyzed E1HT by a combination of electron cryomicroscopy, electron crystallography of neg
165 of TRPV1 determined by using single-particle electron cryomicroscopy exhibits fourfold symmetry and c
166 rus structure and reflect the growing use of electron cryomicroscopy for atomic modeling of protein f
167 nd to F-actin, highlighting the potential of electron cryomicroscopy for structure-based drug design.
170 Despite a molecular weight of only 24 kDa, electron cryomicroscopy illustrated a remarkable level o
172 ted mutagenesis, ultrastructural analysis by electron cryomicroscopy, immunocytochemistry, and molecu
173 To this end we have used single-particle electron cryomicroscopy in combination with cross-linkin
176 e of the alpha(V)beta(3) ectodomain into the electron cryomicroscopy map of alpha(IIb)beta(3) require
179 e, allowing us to obtain a ~3.9-A resolution electron cryomicroscopy map of the VO complex and build
185 ion images of assembled coats, determined by electron cryomicroscopy, now provide the information nec
186 cherichia coli multidrug transporter EmrE by electron cryomicroscopy of 2D crystals, including data t
187 ce at subnanometre resolution, obtained from electron cryomicroscopy of coats assembled in vitro.
191 luenza neuraminidase, has been determined by electron cryomicroscopy of single particles and image an
192 synthase at approximately 18 A resolution by electron cryomicroscopy of single particles in amorphous
195 ly 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows
196 ed in icosahedral image reconstructions from electron cryomicroscopy of trypsinized rotavirus virions
197 eromyosin suitable for structural studies by electron cryomicroscopy of unstained, frozen-hydrated sp
198 e here a structure at 3.9 A resolution, from electron cryomicroscopy, of Pepino mosaic virus (PepMV),
200 sualized the double-layered COPII coat using electron cryomicroscopy, providing insight into how coat
204 , determined by fitting the subunit into the electron cryomicroscopy reconstruction of the virus, ide
205 e cleavage site, did not mature at pH 5, and electron cryomicroscopy reconstruction showed that it wa
208 were clearly visible and well ordered in the electron cryomicroscopy reconstructions of TR TLPs, they
210 cofilactin filament structures determined by electron cryomicroscopy reveal how cofilin enhances the
211 FTCD structure by X-ray crystallography and electron cryomicroscopy revealed that the eight subunits
215 ensional structures of full and empty CPV by electron cryomicroscopy show identical outer shells but
218 Three-dimensional structural studies using electron cryomicroscopy showed that the binding of one F
221 rientation distribution of a single-particle electron cryomicroscopy specimen limits the resolution o
222 s has been determined to 3.4 A, using a 22-A electron cryomicroscopy structure as a phasing model.
223 describe a 4.2-A resolution single-particle electron cryomicroscopy structure of complex I from Bos
224 re, we report a 3.6-A helical reconstruction electron cryomicroscopy structure of four-stranded mini
226 uman aminopeptidase N (hAPN), as well as the electron cryomicroscopy structure of the 229E S-protein.
230 ur knowledge, near-atomic (4.7 A) resolution electron cryomicroscopy structure of the tetrameric mamm
231 nal and visualization analysis from the 8.5A electron cryomicroscopy structure of the whole capsid.
232 binding S-layer array with a single-particle electron cryomicroscopy structure, revealing detailed fe
233 , we present high-resolution single-particle electron cryomicroscopy structures of an ABC transporter
236 e aminoglycosides, determine high-resolution electron cryomicroscopy structures of m(1)A1408-modified
238 virions, the available crystallographic and electron cryomicroscopy structures of NV have not reveal
239 P22 coat protein lattice, we have determined electron cryomicroscopy structures of scaffolding-contai
242 as advanced techniques, such as transmission electron cryomicroscopy, synchrotron-based X-ray absorpt
243 scattering (SEC-MALS) and images obtained by electron cryomicroscopy that McrB exists as a hexamer in
247 tif with nanogold and used three-dimensional electron cryomicroscopy to compare images of microtubule
252 hannel called "portal protein." We have used electron cryomicroscopy to determine the structure of ba
255 emerging technique of Zernike phase-contrast electron cryomicroscopy to enhance the image contrast of
257 tional constraints from linear dichroism and electron cryomicroscopy to obtain the allowed orientatio
263 A three-dimensional reconstruction from electron cryomicroscopy was used as a molecular replacem
271 By using recent advances in single-particle electron cryomicroscopy, we have solved the structure of
273 to a reconstruction of the whole virion from electron cryomicroscopy, we propose that each sigma3 sub
275 d fully defined chromatin arrays obtained by electron cryomicroscopy, we report a linker histone-depe
277 ined under various chemical conditions using electron cryomicroscopy, we show here that the viral gen
278 report the structures of PaaZ determined by electron cryomicroscopy with and without bound ligands.