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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 n vivo by [(32)P]orthophosphate labeling and 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 spectrometry, ion mobility, and quantitative peptide mapping.
12 by peptide sequencing and mass spectrometric peptide mapping.
13 residue reactivity with dithiodipyridine and peptide mapping.
14 ing to the partial amino acid sequences from peptide mapping.
15 n, followed by proteolytic and immunological peptide mapping.
16 and liquid chromatography/mass spectrography peptide mapping.
17 of DNA-dependent protein kinase (DNA-PK) by peptide mapping.
18 ee-disulfide species have been identified by peptide mapping.
19 graphy, and PTM levels were calculated using peptide mapping.
20 spectrometry and glycation sites located by peptide mapping.
21 ein variants that are difficult to detect by peptide mapping.
22 ing truncated GBS-PGK molecules, followed by peptide mapping.
23 ation was investigated by mass spectrometric peptide mapping.
24 uid chromatography-mass spectrometry (LC-MS) peptide mapping.
25 residue preceding lysine 222, determined by peptide mapping.
26 MAP-D002 peptide was higher than that of the peptide MAP-911, whereas the avidity of D002 peptide was
27 e we examined the effect of mouse activating peptide (mAP), a specific activator of PAR-2, on electro
28 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 to demonstrate the utility in improving both peptide mapping analysis and intact mass analysis, the t
34 reduced by 60, 7, and 96%, respectively, and peptide mapping analysis of the mutant enzymes confirmed
36 ered as a result of intact mass measurement, peptide mapping analysis, and tandem mass spectroscopy s
38 ization on the isolated glycated material by peptide mapping analysis, using liquid chromatography-ma
41 etween proteolytic peptide masses from an MS peptide map and theoretical proteolytic peptide masses o
42 Bottom-up characterization using RP-HPLC/MS peptide mapping and accurate mass measurements identifie
43 and the antigenic structure of B5R(275t) by peptide mapping and by reciprocal MAb blocking studies u
45 nized with HCV-1 rE1E2 was conducted through peptide mapping and competition studies with a panel of
46 of high mass accuracy in mass spectrometric peptide mapping and database searching, selected protein
50 ed laser desorption-ionization (MALDI) TOFMS peptide mapping and intact MW so that a standard map is
52 -inactivated CYP3A4(His)(6) followed by HPLC-peptide mapping and mass spectrometric (LC/MS/MS) analys
53 tion of various deamidated forms followed by peptide mapping and mass spectrometric analyses revealed
59 using the traditional bottom-up approach of peptide mapping and MS sequencing methodologies, two DMP
61 vitro by ERK1, JNK and p38, and confirmed by peptide mapping and mutagenesis that Thr53 is phosphoryl
63 e element of the GLUT1 ATP binding domain by peptide mapping and N-terminal sequence analysis of prot
77 ction/alkylation of the protein, followed by peptide mapping and tanden mass spectrometry (MS/MS) seq
78 ved and homogeneous, which was determined by peptide mapping and top-down analysis of PE, PilA, and P
80 parameter together with the intact MW value, peptide map, and MS/MS results for identification of the
81 Immunoreactive epitopes were searched for by peptide mapping, and 171 cleavable, biotinylated 17-mer
83 complex with trypsin, followed by isolation, peptide mapping, and mass spectrometric and tandem mass
84 ies of VEGF-D using a neutralizing antibody, peptide mapping, and mutagenesis to demonstrate that the
86 Using a combination of receptor mutagenesis, peptide mapping, and N-terminal sequencing, we identifie
88 with monoclonal antibodies, one-dimensional peptide mapping, and partial amino acid sequencing demon
89 were identified by purification, proteolytic peptide mapping, and radiochemical sequencing of labeled
92 nces within EC2 and N terminus identified by peptide mapping are in close proximity in the equilibriu
94 n-labeled RTPR with endoproteinase Glu-C and peptide mapping at pH 5.8 revealed that C419 was predomi
95 inhibitor could no longer be detected after peptide mapping at this site or at the catalytic site.
96 rating peptide (CPP), i.e. Model Amphipathic Peptide (MAP), attached to a pH-sensitive masking peptid
104 gel electrophoresis with in-gel proteolysis, peptide mapping by MS, and sequence database searches fo
106 d by MS are not unique; i.e., each mass in a peptide map can match randomly one or several proteins i
107 data obtained demonstrate that MAM by LC-MS peptide mapping can, in principle, adequately replace se
109 e 50-kDa gingipain R2, or multiple antigenic peptide (MAP)-conjugated gingipain R-derived peptides an
110 size and fully characterize multiple antigen peptide (MAP) conjugates containing protective epitopes
111 ve efficacy in rabbits of multiple antigenic peptides (MAPs) consisting of aa 304-319 from the LND of
112 mice with three doses of a multiple antigen peptide (MAP) construct containing four branches of amin
114 oped an approach of lipidating a multiple Ag peptide (MAP) containing part of the V3 loop from HIV-1
116 d fluorescence detection, the sensitivity of peptide mapping could be improved 2000 times compared to
119 d after limited proteolysis was confirmed by peptide mapping coupled with tandem mass spectrometry an
120 intact and reduced mass analysis as well as peptide map data derived from the three major HIC fracti
124 p (Glu(345)), as demonstrated by proteolytic peptide mapping, deglycosylation, micropurification, and
128 he liquid phase and the molecular weight and peptide maps determined by MALDI-TOF MS for identificati
129 with chemically modified, multiple antigenic peptides (MAPs) developed for the detection and discrimi
130 previously showed that a multiple antigenic peptide (MAP) displaying amino acids (aa) 305 to 319 fro
131 ogenicity in rabbits of a multiple antigenic peptide (MAP) displaying copies of amino acids (aa) 305
132 pectrometry (CZE-MS) has great potential for peptide mapping due to high efficiency and outstanding s
133 ressed in COS-1 cells using a combination of peptide mapping, Edman degradation, and mass spectrometr
134 ve approach for protein characterization via peptide mapping employing a data independent LC-MS acqui
139 However, despite this considerable homology, peptide-mapping experiments also revealed that immunodom
140 munodepletion, in vitro phosphorylation, and peptide-mapping experiments indicated that Cdc2 is likel
143 include CE as a complement to reverse-phase peptide mapping for the identification of small peptides
144 tion of the analytical artifact during LC-MS peptide mapping for the measurement of Met sulfoxide.
150 on-exchange chromatography (CEX) and tryptic peptide maps generated with the new digestion method.
152 labeling, trypsin digestion, two-dimensional peptide mapping, high performance liquid chromatography,
154 ct association between the two proteins, and peptide mapping identified an ERK2 binding site within t
158 s the determination of such heterogeneity by peptide mapping in both the heavy chain and the light ch
160 as further complemented experimentally using peptide mapping in tandem with mass spectrometry and sit
161 artic acid and 80% aspartic acid detected by peptide mapping in the degraded sample (8 weeks, 45 degr
162 dified minimally with methylglyoxal, tryptic peptide mapping indicated a hotspot of modification at A
166 omatography with mass spectrometry (RPLC-MS) peptide mapping is routinely used for interrogating mole
168 ng, and reduce cost and preparation time, of peptide mapping LC-MS workflows in protein analytical re
170 ional and chemical modifications in a single peptide mapping liquid chromatography-mass spectrometry
175 ied with fucose and through a combination of peptide mapping, mass spectrometry, and sequence analysi
178 rt the development of an improved nonreduced peptide map method coupled with machine learning to enab
180 from trifluoroacetic acid (TFA) in a typical peptide mapping method can be effectively mitigated, thu
181 a high-resolution, high-sensitivity LC-UV-MS peptide mapping method for the therapeutic antibody, tra
186 mine, by a sodium borohydride-dependent mass peptide mapping method, the galactation sites in HSA; an
189 e chromophores were further located by a new peptide mapping methodology with a combination of mass s
192 lytic (lysylendopeptidase-C) digestion, HPLC-peptide mapping, microEdman sequencing, and mass spectro
199 hogonal technique with growing attention for peptide mapping of biotherapeutic proteins due to its hi
200 er516 was confirmed by tryptic digestion and peptide mapping of COX-2 labeled with [1-14C-acetyl]sali
207 1) and Cys(32)-Cys(39) by protease-generated peptide mapping of partially reduced and S-alkylated rSM
210 identification of phosphopeptides from HPLC peptide mapping of proteolytic digests of phosphoprotein
212 In vitro PKA phosphorylation and tryptic peptide mapping of SNS and mutant SNS(SA) I-II loops exp
213 proved mixing experiments and by comparative peptide mapping of specific polypeptides recovered from
214 nto two subgroups based on serological data, peptide mapping of the coat protein, nucleic acid hybrid
217 to be proximal to the major groove of DNA by peptide mapping of the region of TBP cross-linked at bp
225 y mutations affecting Ser831 altered the 32P peptide maps of GluR1 from HEK-293 cells co-expressing a
227 from an isolated protein followed by either peptide mapping or tandem MS (MS/MS) to obtain sequence
231 haracterization of PTMs using a conventional peptide mapping procedure requires time-consuming and la
236 d that they were different, with the tryptic peptide maps providing evidence that the beta-subunits l
237 g is monitored using mass spectrometry-based peptide mapping, providing spatially resolved measuremen
241 present results from optimization of CZE-MS peptide mapping separation using mixed aqueous-aprotic d
242 The resulting proteins were characterized by peptide mapping, sequence analysis, and mass spectrometr
245 high performance liquid chromatography, and peptide mapping showed that it was the same in the two e
249 mbination with mass spectrometry and tryptic peptide mapping showed unambiguously that RLF is larger
250 with FPR are consistent with cross-linking, peptide mapping, spectroscopic, and electron transfer da
251 This approach also includes a differential peptide mapping step for identification of pyroglutamate
257 sult, taken together with the results of the peptide mapping studies, establishes that the site of Bp
258 rroborated the chemical modification and the peptide mapping studies, establishing the importance of
261 as a function of the number of masses in the peptide map, the mass accuracy, the degree of incomplete
263 This dimerization interface is validated by peptide mapping through hydrogen/deuterium exchange mass
264 used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P.
265 es, we used photo affinity cross-linking and peptide mapping to identify the substrate-binding sites
266 Ultimately, the proteins can be studied by peptide mapping to search for posttranslational modifica
269 performed and demonstrated that 13 different peptides mapped to identical regions of MchA1 and MchA2.
272 sequence coverage by the number of distinct peptides mapping to each protein identification, the CIT
273 ssays was demonstrated against, or shown by, peptides mapping to the third and fourth predicted surfa
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 accurate molecular weight together with the peptide map was used to obtain protein identification us
284 study, mass spectrometry and two-dimensional peptide mapping were used to determine that tyrosines 22
285 sted samples, which limits the efficiency of peptide mapping when there is an increasing demand for p
286 ntages were evaluated through application to peptide mapping, wherein CSH C18 was found to aid the de
287 raction were counted for 3H label within the peptide map which rapidly pinpointed the original four p
288 e alternative to conventional time-intensive peptide mapping which is prone to artificial oxidation d
289 with Girard's Reagent T (GRT) and subsequent peptide mapping with high-resolution mass spectrometry.
292 18O, and time point samples were analyzed by peptide mapping with mass spectrometry to measure the ra
294 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