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1 spectrometry, ion mobility, and quantitative peptide mapping.
2 tion signals as determined by phosphotryptic peptide mapping.
3 ool to increase sequence coverage in tryptic peptide mapping.
4 esis-electrospray ionization (CE-ESI)-TOF MS peptide mapping.
5 by peptide sequencing and mass spectrometric peptide mapping.
6 residue reactivity with dithiodipyridine and peptide mapping.
7 ing to the partial amino acid sequences from peptide mapping.
8 n, followed by proteolytic and immunological peptide mapping.
9 and liquid chromatography/mass spectrography peptide mapping.
10 of DNA-dependent protein kinase (DNA-PK) by peptide mapping.
11 ee-disulfide species have been identified by peptide mapping.
12 gelsolin by amino acid sequencing following peptide mapping.
13 spectrometry and glycation sites located by peptide mapping.
14 ein variants that are difficult to detect by peptide mapping.
15 ing truncated GBS-PGK molecules, followed by peptide mapping.
16 ation was investigated by mass spectrometric peptide mapping.
17 uid chromatography-mass spectrometry (LC-MS) peptide mapping.
18 residue preceding lysine 222, determined by peptide mapping.
19 n vivo by [(32)P]orthophosphate labeling and peptide mapping.
20 ion by mass spectrometry and two-dimensional peptide mapping.
21 2-amino acid motif in the N-terminal CbpA by peptide mapping.
22 ve-like conformation was further verified by peptide mapping after limited trypsin proteolysis, and b
23 y mass (10000.5 Da) and amino acid sequence (peptide mapping after proteolysis) determined by matrix-
24 n sites of carboxylase by mass spectrometric peptide mapping analyses combined with site-directed mut
25 l and complementary technique to RPLC-MS for peptide mapping analyses of antibody-drug conjugates (AD
27 reduced by 60, 7, and 96%, respectively, and peptide mapping analysis of the mutant enzymes confirmed
29 ered as a result of intact mass measurement, peptide mapping analysis, and tandem mass spectroscopy s
31 ization on the isolated glycated material by peptide mapping analysis, using liquid chromatography-ma
33 ns) were phosphorylated in vivo, and tryptic peptide-mapping analysis suggested a single, similar pho
34 Bottom-up characterization using RP-HPLC/MS peptide mapping and accurate mass measurements identifie
36 and the antigenic structure of B5R(275t) by peptide mapping and by reciprocal MAb blocking studies u
38 nized with HCV-1 rE1E2 was conducted through peptide mapping and competition studies with a panel of
39 of high mass accuracy in mass spectrometric peptide mapping and database searching, selected protein
43 ed laser desorption-ionization (MALDI) TOFMS peptide mapping and intact MW so that a standard map is
45 was demonstrated by two-dimensional tryptic peptide mapping and mass analysis to be either threonine
46 -inactivated CYP3A4(His)(6) followed by HPLC-peptide mapping and mass spectrometric (LC/MS/MS) analys
47 tion of various deamidated forms followed by peptide mapping and mass spectrometric analyses revealed
53 using the traditional bottom-up approach of peptide mapping and MS sequencing methodologies, two DMP
55 vitro by ERK1, JNK and p38, and confirmed by peptide mapping and mutagenesis that Thr53 is phosphoryl
58 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
75 Immunoreactive epitopes were searched for by peptide mapping, and 171 cleavable, biotinylated 17-mer
77 complex with trypsin, followed by isolation, peptide mapping, and mass spectrometric and tandem mass
78 mance liquid chromatography, two-dimensional peptide mapping, and matrix-assisted laser desorption/io
79 ies of VEGF-D using a neutralizing antibody, peptide mapping, and mutagenesis to demonstrate that the
81 Using a combination of receptor mutagenesis, peptide mapping, and N-terminal sequencing, we identifie
83 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 nces within EC2 and N terminus identified by peptide mapping are in close proximity in the equilibriu
89 n-labeled RTPR with endoproteinase Glu-C and peptide mapping at pH 5.8 revealed that C419 was predomi
90 inhibitor could no longer be detected after peptide mapping at this site or at the catalytic site.
99 gel electrophoresis with in-gel proteolysis, peptide mapping by MS, and sequence database searches fo
102 d fluorescence detection, the sensitivity of peptide mapping could be improved 2000 times compared to
104 d after limited proteolysis was confirmed by peptide mapping coupled with tandem mass spectrometry an
107 p (Glu(345)), as demonstrated by proteolytic peptide mapping, deglycosylation, micropurification, and
111 pectrometry (CZE-MS) has great potential for peptide mapping due to high efficiency and outstanding s
112 ressed in COS-1 cells using a combination of peptide mapping, Edman degradation, and mass spectrometr
113 lytical methods such as amino acid analysis, peptide mapping, electrospray mass spectrometry, and Edm
114 ve approach for protein characterization via peptide mapping employing a data independent LC-MS acqui
119 However, despite this considerable homology, peptide-mapping experiments also revealed that immunodom
120 munodepletion, in vitro phosphorylation, and peptide-mapping experiments indicated that Cdc2 is likel
123 include CE as a complement to reverse-phase peptide mapping for the identification of small peptides
124 tion of the analytical artifact during LC-MS peptide mapping for the measurement of Met sulfoxide.
127 labeling, trypsin digestion, two-dimensional peptide mapping, high performance liquid chromatography,
128 ct association between the two proteins, and peptide mapping identified an ERK2 binding site within t
132 s the determination of such heterogeneity by peptide mapping in both the heavy chain and the light ch
134 as further complemented experimentally using peptide mapping in tandem with mass spectrometry and sit
135 structure of the receptor was determined by peptide mapping in the absence and presence of reducing
136 artic acid and 80% aspartic acid detected by peptide mapping in the degraded sample (8 weeks, 45 degr
137 dified minimally with methylglyoxal, tryptic peptide mapping indicated a hotspot of modification at A
141 omatography with mass spectrometry (RPLC-MS) peptide mapping is routinely used for interrogating mole
143 ng, and reduce cost and preparation time, of peptide mapping LC-MS workflows in protein analytical re
147 ied with fucose and through a combination of peptide mapping, mass spectrometry, and sequence analysi
150 a high-resolution, high-sensitivity LC-UV-MS peptide mapping method for the therapeutic antibody, tra
155 mine, by a sodium borohydride-dependent mass peptide mapping method, the galactation sites in HSA; an
158 e chromophores were further located by a new peptide mapping methodology with a combination of mass s
161 ific modification with 4-vinylpyridine, HPLC peptide mapping methods, and mass spectrometry to analyz
162 lytic (lysylendopeptidase-C) digestion, HPLC-peptide mapping, microEdman sequencing, and mass spectro
168 s regions to the immune system was tested by peptide mapping of antiserum specificities against sets
169 hogonal technique with growing attention for peptide mapping of biotherapeutic proteins due to its hi
170 er516 was confirmed by tryptic digestion and peptide mapping of COX-2 labeled with [1-14C-acetyl]sali
178 1) and Cys(32)-Cys(39) by protease-generated peptide mapping of partially reduced and S-alkylated rSM
181 identification of phosphopeptides from HPLC peptide mapping of proteolytic digests of phosphoprotein
183 In vitro PKA phosphorylation and tryptic peptide mapping of SNS and mutant SNS(SA) I-II loops exp
184 proved mixing experiments and by comparative peptide mapping of specific polypeptides recovered from
185 nto two subgroups based on serological data, peptide mapping of the coat protein, nucleic acid hybrid
188 for differences in Km and thermal stability, peptide mapping of the LDH-As of all six species was fir
189 to be proximal to the major groove of DNA by peptide mapping of the region of TBP cross-linked at bp
198 from an isolated protein followed by either peptide mapping or tandem MS (MS/MS) to obtain sequence
199 yed included various proteolytic digestions, peptide mapping, partial reduction, and assignment of di
204 g is monitored using mass spectrometry-based peptide mapping, providing spatially resolved measuremen
205 pha 2(I) chains as determined by V8 protease peptide mapping, reached the highest intracellular level
210 present results from optimization of CZE-MS peptide mapping separation using mixed aqueous-aprotic d
211 The resulting proteins were characterized by peptide mapping, sequence analysis, and mass spectrometr
215 dimensional gel electrophoresis and tryptic peptide mapping showed that entry into the nucleus resul
216 high performance liquid chromatography, and peptide mapping showed that it was the same in the two e
220 mbination with mass spectrometry and tryptic peptide mapping showed unambiguously that RLF is larger
221 with FPR are consistent with cross-linking, peptide mapping, spectroscopic, and electron transfer da
228 sult, taken together with the results of the peptide mapping studies, establishes that the site of Bp
229 rroborated the chemical modification and the peptide mapping studies, establishing the importance of
233 This dimerization interface is validated by peptide mapping through hydrogen/deuterium exchange mass
234 psilon to the gamma subunit was localized by peptide mapping to a region of the gamma subunit between
235 used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P.
236 es, we used photo affinity cross-linking and peptide mapping to identify the substrate-binding sites
237 Ultimately, the proteins can be studied by peptide mapping to search for posttranslational modifica
240 sequence coverage by the number of distinct peptides mapping to each protein identification, the CIT
241 ssays was demonstrated against, or shown by, peptides mapping to the third and fourth predicted surfa
243 e Ser/Thr kinase domain of PKCdelta based on peptide mapping using liquid chromatography/mass spectro
244 as identified as the phosphorylation site by peptide mapping using mass spectrometry, site-directed m
252 study, mass spectrometry and two-dimensional peptide mapping were used to determine that tyrosines 22
253 ntages were evaluated through application to peptide mapping, wherein CSH C18 was found to aid the de
254 e alternative to conventional time-intensive peptide mapping which is prone to artificial oxidation d
255 with Girard's Reagent T (GRT) and subsequent peptide mapping with high-resolution mass spectrometry.
258 18O, and time point samples were analyzed by peptide mapping with mass spectrometry to measure the ra
260 pwise reduction and alkylation at acidic pH, peptide mapping with matrix-assisted laser desorption io
263 ing on the beta1 chain was localized by CNBr peptide mapping within residues 130-146, a region that c
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