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1 as localized to the amino-terminal domain by proteolytic digestion.
2 omplished simply by washing the gel prior to proteolytic digestion.
3  an altered conformation detectable by Glu-C proteolytic digestion.
4 DS-PAGE, Ni(2+) affinity chromatography, and proteolytic digestion.
5 tein aggregates resistant to degradation and proteolytic digestion.
6  near the zinc ligands becomes accessible to proteolytic digestion.
7 sed resistance of the full-length protein to proteolytic digestion.
8 idues, the modified protein was subjected to proteolytic digestion.
9 e fluorescent probe 1,8-ANS, and (3) limited proteolytic digestion.
10 as previously shown, but also the pattern of proteolytic digestion.
11 lex into three protein components by limited proteolytic digestion.
12 y are unstable and undergo hydrolysis during proteolytic digestion.
13 lots and thrombi are stable structures until proteolytic digestion.
14 ficulty in achieving complete and consistent proteolytic digestion.
15 tochondrial DNA helicase more susceptible to proteolytic digestion.
16  complete, including the incubation time for proteolytic digestion.
17 rmediates at <0.007 Da mass accuracy without proteolytic digestion.
18 ither partial unfolding of the enzyme or its proteolytic digestion.
19 xhibit improved regularity and resistance to proteolytic digestion.
20 lization of structural modifications without proteolytic digestion.
21 e of S. mutans alters P1's susceptibility to proteolytic digestion.
22 ition and confers the ECM with resistance to proteolytic digestion.
23 second alkylation was carried out during the proteolytic digestion.
24 idue Rel(Seq) protein are defined by limited proteolytic digestion.
25 fragments resulting from partial or complete proteolytic digestion.
26  greater protein instability in chymotrypsin proteolytic digestions.
27 n (HSA) by online EC reduction of nonreduced proteolytic digestions.
28 form infrared and NMR spectroscopies, and by proteolytic digestions.
29 the total CE protein could be solubilized by proteolytic digestion after saponification, of which inv
30                                              Proteolytic digestion analysis demonstrates A domain mov
31                             A combination of proteolytic digestion and affinity-directed mass spectro
32  sensitive protein identification by on-line proteolytic digestion and analysis of protein digests us
33 ation sites in human NF-H were identified by proteolytic digestion and analysis of the resulting dige
34                   EM analysis, combined with proteolytic digestion and deletion mapping, revealed the
35  demonstrated by increased susceptibility to proteolytic digestion and enhanced susceptibility to unf
36 turized trypsin-membrane reactor for on-line proteolytic digestion and ESI-MS analysis for protein/pe
37                     A simultaneous on-tissue proteolytic digestion and extraction method is described
38             Conformational changes probed by proteolytic digestion and fluorescence signal reported b
39 omponents that restricted AdV access because proteolytic digestion and inhibitors of O-linked glycosy
40 terized by mass spectrometric analysis after proteolytic digestion and isolation of fluorescent photo
41                                       In-gel proteolytic digestion and LC-MS/MS analysis were conduct
42 c analysis of complex protein mixtures using proteolytic digestion and liquid chromatography in combi
43 l acetyl phosphate (MAP) in combination with proteolytic digestion and mass spectral analysis show th
44  as well as proteins in gel slices, prior to proteolytic digestion and mass spectral analysis.
45                                              Proteolytic digestion and mass spectrometric analysis in
46         Chemical cross-linking combined with proteolytic digestion and mass spectrometry (MS) is a pr
47                                    Utilizing proteolytic digestion and nano-LC-MS/MS analysis, we con
48 Mn2+ increased the resistance of HIV-1 IN to proteolytic digestion and produced a digestion pattern t
49                                              Proteolytic digestion and protein kinase protection expe
50 units, p42 and p22, was determined following proteolytic digestion and sequence analysis of the resul
51 ch Edman sequencing, amino acid analysis, or proteolytic digestion and sequencing by tandem mass spec
52 e presence of [32P]ATP, prior to solid-phase proteolytic digestion and two-dimensional phosphopeptide
53 onformational stability, high sensitivity to proteolytic digestion, and a replication rate of 10(6)-f
54 le quantum coherence (HSQC) spectra, limited proteolytic digestion, and fluorescence data suggest tha
55  the elongating new peptide, protect it from proteolytic digestion, and guide its emergence.
56  the Fl(N5[O]) species via isotope labeling, proteolytic digestion, and high-resolution tandem mass s
57 sed a combination of chemical cross-linking, proteolytic digestion, and mass spectrometry (MALDI-TOF
58  combination of hydrogen/deuterium exchange, proteolytic digestion, and mass spectrometry.
59                                   In limited proteolytic digestion assays, SR11335 induced resistance
60 on approach achieved the same results as the proteolytic-digestion-based methodology in a much shorte
61   The coat protein monomer is susceptible to proteolytic digestion, but limited proteolysis by small
62  analogue Cibacron Blue and was sensitive to proteolytic digestion by chymotrypsin.
63 ty, we observed that Sec61p is shielded from proteolytic digestion by native, bound ribosomes.
64 a 2.9 S particle, and is highly sensitive to proteolytic digestion by proteinase K; these characteris
65 ts the enzyme and enhances susceptibility to proteolytic digestion by the isolated 20 S proteasome.
66                   Pet111p was protected from proteolytic digestion by the mitochondrial inner membran
67 denaturing PAGE and increased sensitivity to proteolytic digestion compared with wild type SOD1.
68 we created a set of Sup35NM mutants and used proteolytic digestion coupled with mass spectroscopy to
69 for marked resistance of trefoil peptides to proteolytic digestion, enabling them to function in the
70                                              Proteolytic digestion established the presence of both d
71          In addition, circular dichroism and proteolytic digestion experiments revealed structural di
72 alyses using the yeast two-hybrid system and proteolytic digestion experiments suggest that mu1 and m
73 sine cross-link (as determined by exhaustive proteolytic digestion followed by cation exchange chroma
74  formation of nitrotyrosine was confirmed by proteolytic digestion followed by high performance liqui
75 xidized proteins were collected off-line for proteolytic digestion followed by LC-MS/MS analysis.
76 g Q7-bound products are completely stable to proteolytic digestion for at least 24 h.
77 ied directly by MALDI-TOFMS, or subjected to proteolytic digestion for protein identification.
78 f electronic protein transfer with nanoscale proteolytic digestion in a capillary platform, enabling
79 uclein filaments, because it is resistant to proteolytic digestion in alpha-synuclein filaments; and
80 a subset of lysosomal membrane proteins from proteolytic digestion in intact cells.
81 This nanoscale reaction system enables rapid proteolytic digestion in seconds instead of hours for a
82 embrane extracts, 1a is fully susceptible to proteolytic digestion in the absence of detergent and th
83 29 was also found to be fully susceptible to proteolytic digestion in the absence of detergent and, t
84 of the LukS polypeptide becomes resistant to proteolytic digestion in the fully assembled Luk pore wh
85 their role in protecting the neurotoxin from proteolytic digestion in the GI tract as well as from ad
86  Complexed Chtr is much less reactive toward proteolytic digestion in the presence of high salt than
87          Fibrils showed varied resistance to proteolytic digestion in vitro by either Proteinase K, p
88                                              Proteolytic digestion indicated that in G43:Ras61L both
89             The susceptibility of PrP(Sc) to proteolytic digestion induced by branched polyamines in
90 al-time fluorescent microscopy revealed that proteolytic digestion induces either aggregation of the
91 lysis of polypeptide mixtures resulting from proteolytic digestion is described.
92                                        Their proteolytic digestion leads to a large number of peptide
93                                              Proteolytic digestion mapping showed that the 54-kDa TEF
94 rtial reduction and alkylation, chemical and proteolytic digestion, mass spectrometry, and amino acid
95  region was investigated by fluorescence and proteolytic digestion methods.
96                       In contrast, following proteolytic digestion, MsrA is able to fully reduce one-
97  stable, and neither abnormally sensitive to proteolytic digestion nor prone to aggregation.
98 ructure and dynamics were characterized with proteolytic digestion, nucleotide analogue trapping kine
99 les such as phosphopeptides generated by the proteolytic digestion of a large protein, eNOS, phosphor
100 Subsequent peptide-centric analysis, through proteolytic digestion of C9 and liquid chromatography (L
101 ative regulated heavy meromyosin prepared by proteolytic digestion of chicken gizzard myosin with bet
102 ormation on cross-linked peptides derived by proteolytic digestion of cross-linked proteins has been
103 hromatography tandem mass spectrometry after proteolytic digestion of extracted proteins, solid-phase
104 are important in the entry process, and that proteolytic digestion of glycoprotein 1 by endosomal pro
105                                              Proteolytic digestion of inactivated enzyme, followed by
106 yl-terminal tagged G6PT, we demonstrate that proteolytic digestion of intact microsomes resulted in t
107                                              Proteolytic digestion of milk proteins had no influence
108                                        Rapid proteolytic digestion of monomeric, non-DNA-bound ER-DBD
109                                      Limited proteolytic digestion of mutant G2049E and R2063W protei
110                                              Proteolytic digestion of MutY using thermolysin was foun
111                 However, MAb 7.5G slowed the proteolytic digestion of PA by furin in vitro, suggestin
112                                        After proteolytic digestion of photolabeled DT-A, derivatized
113  detect protease activity (trypsin) based on proteolytic digestion of protamine, and polyanions (pent
114                    The approach involves the proteolytic digestion of proteins prior to the isolation
115 tilizes mass spectral data produced from the proteolytic digestion of proteins, rather than partial o
116 f peptides and peptide mixtures generated by proteolytic digestion of proteins.
117 P scaffolds at early time points, indicating proteolytic digestion of scaffolds.
118 ethod of on-probe solubilization and in situ proteolytic digestion of small, acid-soluble spore prote
119 stigated using immunoelectron microscopy and proteolytic digestion of streptolysin O-permeabilized pa
120                 Here we describe a method of proteolytic digestion of surface-exposed proteins to ide
121            A comparison of the migration and proteolytic digestion of the 54-kDa TEF-1-related polype
122                        It is shown here that proteolytic digestion of the C-loop in beta-cardiac myos
123                                              Proteolytic digestion of the Co3+-PEPCK complex and isol
124 tein complexes often involves solution-phase proteolytic digestion of the complex.
125 after reduction of the putative Schiff base, proteolytic digestion of the enzyme, and isolation of th
126                                      Limited proteolytic digestion of the full-length protein reveale
127 ification by IP-dUMP, which was confirmed by proteolytic digestion of the modified protein followed b
128                                        After proteolytic digestion of the platelet proteins, and isol
129 ter removal of the noncovalent cofactors and proteolytic digestion of the protein moiety.
130                                              Proteolytic digestion of the rafts does not disrupt the
131                                    Following proteolytic digestion of the resulting covalent complex,
132 res of a set of glycopeptides resulting from proteolytic digestion of the well-characterized glycopro
133                                              Proteolytic digestion of tissues has been utilized to re
134 rhea in humans are due, at least in part, to proteolytic digestion of toxin A and B molecules by a se
135  multiplexed inhibitor beads with subsequent proteolytic digestion of unbound proteins and peptide-ba
136 racterization and conformational analysis by proteolytic digestion of WT and mutated (NMBD deletion o
137                             Limited in vitro proteolytic digestions of a biologically active His-MBP
138                                              Proteolytic digestions of F-actin with subtilisin and tr
139                                              Proteolytic digestions of purified forms of clavulanate
140                                  A series of proteolytic digestions of the 1331A/HIV-gp120 complex al
141                                              Proteolytic digestions of the labeled enzyme and analysi
142 l ribosome has been achieved by carrying out proteolytic digestions of whole 28 S subunits followed b
143 l ribosome has been achieved by carrying out proteolytic digestions of whole 39 S subunits followed b
144 en subjected to electronic lysis followed by proteolytic digestion on a single microfabricated bioele
145  fusion of cells expressing only gB, and the proteolytic digestion pattern of gB in virions changes i
146 te fusion, result in the same changes in the proteolytic digestion pattern of gB, possibly representi
147 by changes in intrinsic Trp fluorescence and proteolytic digestion pattern.
148 ne) triphosphate (AMPPCP), Ca2+, and Mg2+ on proteolytic digestion patterns, interpreted in the light
149 stern method for examining Galphat-GTPgammaS proteolytic digestion patterns.
150        The methods employed included various proteolytic digestions, peptide mapping, partial reducti
151                     The use of complementary proteolytic digestion/peptide fragmentation processes al
152 ence analysis in insoluble elastin following proteolytic digestion reveal the P'1 residues in the car
153 id sequences of four peptides isolated after proteolytic digestion revealed that the enzyme is highly
154                                      Limited proteolytic digestion showed labeling sites on nonoverla
155                                      In vivo proteolytic digestion shows that the C-terminus is expos
156                                          The proteolytic digestion step converts a purified recombina
157 esis products, without heavy reliance on the proteolytic digestion step.
158 ts on conformation-dependent protection from proteolytic digestion suggest that, in the presence of B
159 vering and capping and its susceptibility to proteolytic digestion, suggesting a conformational chang
160  spectrometry, tandem mass spectrometry, and proteolytic digestion, that recombinant HOS3 has a disti
161                  As judged by sensitivity to proteolytic digestion, the disease-causing prion protein
162 as labeled using the PhIAT method, and after proteolytic digestion, the labeled peptides were isolate
163 er the intact protein mass or, after on-chip proteolytic digestion, the peptide mass fingerprint and/
164                                        After proteolytic digestion, the PhIAT-labeled peptides were a
165                                    Following proteolytic digestion, the plant UMP/CMP kinase was puri
166  PrPSc proteins showed similar resistance to proteolytic digestion, they differed in their glycoform
167  N-terminal domain of SecA is protected from proteolytic digestion through insertion into the membran
168                                        After proteolytic digestion, TNM-labeled residues were identif
169 tein conjugates are potentially repaired via proteolytic digestion to DNA-peptide conjugates.
170 hylated, and then subjected to a combination proteolytic digestion to obtain a complex peptide mixtur
171 dynamin I that had been subjected to limited proteolytic digestion to remove the PRD.
172                This study presents on-tissue proteolytic digestion using a microwave irradiation and
173           The amount of CHAs released during proteolytic digestion was in the range 0.33-2.67g/100g.
174 gested proteins for reprocessing/consecutive proteolytic digestion, we applied chymotrypsin to redige
175 d-phase HPLC and FAB mass spectrometry after proteolytic digestion, we have identified the sites of m
176  presence of redox reagents used in standard proteolytic digestions; when these are accounted for, a
177                                 By combining proteolytic digestion with peptide mapping and tandem ma
178 P/polypeptide adduct was greatly narrowed by proteolytic digestion with Pronase, confirming that the
179 tly attached to the polynucleotide following proteolytic digestion with trypsin correspond to amino a

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