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1 ernible singly charged ions detected in a MS peptide map.
2 g 32P-labeled peptides isolated from tryptic peptide maps.
3 difficult to detect them in the conventional peptide maps.
4 extracted ion chromatograms from the tryptic peptide maps.
5 spectrometry, ion mobility, and quantitative peptide mapping.
6 ion by mass spectrometry and two-dimensional peptide mapping.
7 2-amino acid motif in the N-terminal CbpA by peptide mapping.
8 tion signals as determined by phosphotryptic peptide mapping.
9 ool to increase sequence coverage in tryptic peptide mapping.
10 esis-electrospray ionization (CE-ESI)-TOF MS peptide mapping.
11 by peptide sequencing and mass spectrometric peptide mapping.
12 residue reactivity with dithiodipyridine and peptide mapping.
13 ing to the partial amino acid sequences from peptide mapping.
14 n, followed by proteolytic and immunological peptide mapping.
15 and liquid chromatography/mass spectrography peptide mapping.
16 of DNA-dependent protein kinase (DNA-PK) by peptide mapping.
17 ee-disulfide species have been identified by peptide mapping.
18 spectrometry and glycation sites located by peptide mapping.
19 ein variants that are difficult to detect by peptide mapping.
20 ing truncated GBS-PGK molecules, followed by peptide mapping.
21 ation was investigated by mass spectrometric peptide mapping.
22 uid chromatography-mass spectrometry (LC-MS) peptide mapping.
23 residue preceding lysine 222, determined by peptide mapping.
24 n vivo by [(32)P]orthophosphate labeling and peptide mapping.
25 MAP-D002 peptide was higher than that of the peptide MAP-911, whereas the avidity of D002 peptide was
26 e we examined the effect of mouse activating peptide (mAP), a specific activator of PAR-2, on electro
27 y mass (10000.5 Da) and amino acid sequence (peptide mapping after proteolysis) determined by matrix-
29 n sites of carboxylase by mass spectrometric peptide mapping analyses combined with site-directed mut
30 l and complementary technique to RPLC-MS for peptide mapping analyses of antibody-drug conjugates (AD
32 reduced by 60, 7, and 96%, respectively, and peptide mapping analysis of the mutant enzymes confirmed
34 ered as a result of intact mass measurement, peptide mapping analysis, and tandem mass spectroscopy s
36 ization on the isolated glycated material by peptide mapping analysis, using liquid chromatography-ma
38 etween proteolytic peptide masses from an MS peptide map and theoretical proteolytic peptide masses o
39 Bottom-up characterization using RP-HPLC/MS peptide mapping and accurate mass measurements identifie
40 and the antigenic structure of B5R(275t) by peptide mapping and by reciprocal MAb blocking studies u
42 nized with HCV-1 rE1E2 was conducted through peptide mapping and competition studies with a panel of
43 of high mass accuracy in mass spectrometric peptide mapping and database searching, selected protein
47 ed laser desorption-ionization (MALDI) TOFMS peptide mapping and intact MW so that a standard map is
49 -inactivated CYP3A4(His)(6) followed by HPLC-peptide mapping and mass spectrometric (LC/MS/MS) analys
50 tion of various deamidated forms followed by peptide mapping and mass spectrometric analyses revealed
56 using the traditional bottom-up approach of peptide mapping and MS sequencing methodologies, two DMP
58 vitro by ERK1, JNK and p38, and confirmed by peptide mapping and mutagenesis that Thr53 is phosphoryl
60 e element of the GLUT1 ATP binding domain by peptide mapping and N-terminal sequence analysis of prot
74 ction/alkylation of the protein, followed by peptide mapping and tanden mass spectrometry (MS/MS) seq
76 parameter together with the intact MW value, peptide map, and MS/MS results for identification of the
77 Immunoreactive epitopes were searched for by peptide mapping, and 171 cleavable, biotinylated 17-mer
79 complex with trypsin, followed by isolation, peptide mapping, and mass spectrometric and tandem mass
80 ies of VEGF-D using a neutralizing antibody, peptide mapping, and mutagenesis to demonstrate that the
82 Using a combination of receptor mutagenesis, peptide mapping, and N-terminal sequencing, we identifie
84 with monoclonal antibodies, one-dimensional peptide mapping, and partial amino acid sequencing demon
85 were identified by purification, proteolytic peptide mapping, and radiochemical sequencing of labeled
87 tterns, reactivity with various Abs, tryptic peptide maps, and NH2-terminal sequences of their chains
89 nces within EC2 and N terminus identified by peptide mapping are in close proximity in the equilibriu
91 n-labeled RTPR with endoproteinase Glu-C and peptide mapping at pH 5.8 revealed that C419 was predomi
92 inhibitor could no longer be detected after peptide mapping at this site or at the catalytic site.
93 rating peptide (CPP), i.e. Model Amphipathic Peptide (MAP), attached to a pH-sensitive masking peptid
101 gel electrophoresis with in-gel proteolysis, peptide mapping by MS, and sequence database searches fo
103 d by MS are not unique; i.e., each mass in a peptide map can match randomly one or several proteins i
105 e 50-kDa gingipain R2, or multiple antigenic peptide (MAP)-conjugated gingipain R-derived peptides an
106 size and fully characterize multiple antigen peptide (MAP) conjugates containing protective epitopes
107 ve efficacy in rabbits of multiple antigenic peptides (MAPs) consisting of aa 304-319 from the LND of
108 mice with three doses of a multiple antigen peptide (MAP) construct containing four branches of amin
110 oped an approach of lipidating a multiple Ag peptide (MAP) containing part of the V3 loop from HIV-1
113 d fluorescence detection, the sensitivity of peptide mapping could be improved 2000 times compared to
115 d after limited proteolysis was confirmed by peptide mapping coupled with tandem mass spectrometry an
116 intact and reduced mass analysis as well as peptide map data derived from the three major HIC fracti
121 p (Glu(345)), as demonstrated by proteolytic peptide mapping, deglycosylation, micropurification, and
126 he liquid phase and the molecular weight and peptide maps determined by MALDI-TOF MS for identificati
127 with chemically modified, multiple antigenic peptides (MAPs) developed for the detection and discrimi
128 previously showed that a multiple antigenic peptide (MAP) displaying amino acids (aa) 305 to 319 fro
129 ogenicity in rabbits of a multiple antigenic peptide (MAP) displaying copies of amino acids (aa) 305
130 pectrometry (CZE-MS) has great potential for peptide mapping due to high efficiency and outstanding s
131 ressed in COS-1 cells using a combination of peptide mapping, Edman degradation, and mass spectrometr
132 ve approach for protein characterization via peptide mapping employing a data independent LC-MS acqui
137 However, despite this considerable homology, peptide-mapping experiments also revealed that immunodom
138 munodepletion, in vitro phosphorylation, and peptide-mapping experiments indicated that Cdc2 is likel
141 include CE as a complement to reverse-phase peptide mapping for the identification of small peptides
142 tion of the analytical artifact during LC-MS peptide mapping for the measurement of Met sulfoxide.
148 on-exchange chromatography (CEX) and tryptic peptide maps generated with the new digestion method.
150 labeling, trypsin digestion, two-dimensional peptide mapping, high performance liquid chromatography,
152 ct association between the two proteins, and peptide mapping identified an ERK2 binding site within t
156 s the determination of such heterogeneity by peptide mapping in both the heavy chain and the light ch
158 as further complemented experimentally using peptide mapping in tandem with mass spectrometry and sit
159 artic acid and 80% aspartic acid detected by peptide mapping in the degraded sample (8 weeks, 45 degr
160 dified minimally with methylglyoxal, tryptic peptide mapping indicated a hotspot of modification at A
164 omatography with mass spectrometry (RPLC-MS) peptide mapping is routinely used for interrogating mole
166 ng, and reduce cost and preparation time, of peptide mapping LC-MS workflows in protein analytical re
172 ied with fucose and through a combination of peptide mapping, mass spectrometry, and sequence analysi
176 a high-resolution, high-sensitivity LC-UV-MS peptide mapping method for the therapeutic antibody, tra
181 mine, by a sodium borohydride-dependent mass peptide mapping method, the galactation sites in HSA; an
184 e chromophores were further located by a new peptide mapping methodology with a combination of mass s
187 lytic (lysylendopeptidase-C) digestion, HPLC-peptide mapping, microEdman sequencing, and mass spectro
194 hogonal technique with growing attention for peptide mapping of biotherapeutic proteins due to its hi
195 er516 was confirmed by tryptic digestion and peptide mapping of COX-2 labeled with [1-14C-acetyl]sali
203 1) and Cys(32)-Cys(39) by protease-generated peptide mapping of partially reduced and S-alkylated rSM
206 identification of phosphopeptides from HPLC peptide mapping of proteolytic digests of phosphoprotein
208 In vitro PKA phosphorylation and tryptic peptide mapping of SNS and mutant SNS(SA) I-II loops exp
209 proved mixing experiments and by comparative peptide mapping of specific polypeptides recovered from
210 nto two subgroups based on serological data, peptide mapping of the coat protein, nucleic acid hybrid
213 for differences in Km and thermal stability, peptide mapping of the LDH-As of all six species was fir
214 to be proximal to the major groove of DNA by peptide mapping of the region of TBP cross-linked at bp
222 y mutations affecting Ser831 altered the 32P peptide maps of GluR1 from HEK-293 cells co-expressing a
225 from an isolated protein followed by either peptide mapping or tandem MS (MS/MS) to obtain sequence
226 yed included various proteolytic digestions, peptide mapping, partial reduction, and assignment of di
231 d that they were different, with the tryptic peptide maps providing evidence that the beta-subunits l
232 g is monitored using mass spectrometry-based peptide mapping, providing spatially resolved measuremen
236 present results from optimization of CZE-MS peptide mapping separation using mixed aqueous-aprotic d
237 The resulting proteins were characterized by peptide mapping, sequence analysis, and mass spectrometr
240 dimensional gel electrophoresis and tryptic peptide mapping showed that entry into the nucleus resul
241 high performance liquid chromatography, and peptide mapping showed that it was the same in the two e
245 mbination with mass spectrometry and tryptic peptide mapping showed unambiguously that RLF is larger
246 with FPR are consistent with cross-linking, peptide mapping, spectroscopic, and electron transfer da
253 sult, taken together with the results of the peptide mapping studies, establishes that the site of Bp
254 rroborated the chemical modification and the peptide mapping studies, establishing the importance of
259 as a function of the number of masses in the peptide map, the mass accuracy, the degree of incomplete
261 f the three homologs having the most similar peptide maps, those of the north temperate species, S. a
262 This dimerization interface is validated by peptide mapping through hydrogen/deuterium exchange mass
263 used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P.
264 es, we used photo affinity cross-linking and peptide mapping to identify the substrate-binding sites
265 Ultimately, the proteins can be studied by peptide mapping to search for posttranslational modifica
268 performed and demonstrated that 13 different peptides mapped to identical regions of MchA1 and MchA2.
271 sequence coverage by the number of distinct peptides mapping to each protein identification, the CIT
272 ssays was demonstrated against, or shown by, peptides mapping to the third and fourth predicted surfa
273 chsp10 were generated with multiple-antigen peptides (MAPs) to promote recognition of Chlamydia-spec
276 e Ser/Thr kinase domain of PKCdelta based on peptide mapping using liquid chromatography/mass spectro
277 as identified as the phosphorylation site by peptide mapping using mass spectrometry, site-directed m
280 inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed wi
281 accurate molecular weight together with the peptide map was used to obtain protein identification us
286 study, mass spectrometry and two-dimensional peptide mapping were used to determine that tyrosines 22
287 ntages were evaluated through application to peptide mapping, wherein CSH C18 was found to aid the de
288 raction were counted for 3H label within the peptide map which rapidly pinpointed the original four p
289 e alternative to conventional time-intensive peptide mapping which is prone to artificial oxidation d
290 with Girard's Reagent T (GRT) and subsequent peptide mapping with high-resolution mass spectrometry.
293 18O, and time point samples were analyzed by peptide mapping with mass spectrometry to measure the ra
295 pwise reduction and alkylation at acidic pH, peptide mapping with matrix-assisted laser desorption io
298 ing on the beta1 chain was localized by CNBr peptide mapping within residues 130-146, a region that c
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