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1  isoelectric point of PrP quasispecies under two-dimensional electrophoresis.
2 ns from rat liver homogenate and resolved by two-dimensional electrophoresis.
3 rom 14-week cultures, was examined by use of two-dimensional electrophoresis.
4 ristics from wild type AR as determined with two-dimensional electrophoresis.
5 rms are active in glial tumors by performing two-dimensional electrophoresis.
6 PK2 was followed by protein separation using two-dimensional electrophoresis.
7 s NZ131 rgg and NZ131 speB were separated by two-dimensional electrophoresis.
8 f alpha-migrating particles as determined by two-dimensional electrophoresis.
9 arative electrophoresis, electroelution, and two-dimensional electrophoresis.
10  grown in 5% CO2 and in air were examined by two-dimensional electrophoresis.
11 cross the growth range were examined through two-dimensional electrophoresis (2-D gels) of the proteo
12                                              Two-dimensional electrophoresis (2-DE) and matrix-assist
13 Cabernet) in order to obtain a separation by two-dimensional electrophoresis (2-DE) compatible with m
14                   Proteins were separated by two-dimensional electrophoresis (2-DE), visualized by fl
15                                     Although two-dimensional electrophoresis (2D-GE) remains the basi
16                                              Two-dimensional electrophoresis (2D-PAGE) for protein fr
17 g (IEF) with subsequent gel electrophoresis, two-dimensional electrophoresis (2DE) affords more speci
18      Solubilization of membrane proteins for two-dimensional electrophoresis (2DE) is very difficult.
19      Immunoblotting of proteins separated by two-dimensional electrophoresis (2DE) with sera from mic
20 mination of normal H-Ras, K-Ras and N-Ras by two-dimensional electrophoresis after exposure to bacter
21 aration of thousands of cellular proteins by two-dimensional electrophoresis allows the detailed comp
22 tivariate analysis, a total of 63 spots from two-dimensional electrophoresis analysis and 135 protein
23                                              Two-dimensional electrophoresis analysis of B. burgdorfe
24  linked to Hap1 repression and activation by two-dimensional electrophoresis analysis.
25 acted from seeds and pulp juice, resolved by two dimensional electrophoresis and major spots subjecte
26 y 150 soluble root proteins were resolved by two-dimensional electrophoresis and analyzed by MALDI-To
27 dipocyte proteins were separated by one- and two-dimensional electrophoresis and approximately 60 2SC
28  We have resolved the labeled proteins using two-dimensional electrophoresis and autofluorography.
29 ualized using metabolic labeling followed by two-dimensional electrophoresis and fluorography.
30 Soluble thylakoid proteins were separated by two-dimensional electrophoresis and identified by mass s
31 xtreme proteolysis indices were separated by two-dimensional electrophoresis and identified by tandem
32                                              Two-dimensional electrophoresis and immunoblot of adhesi
33                    These include as follows: two-dimensional electrophoresis and immunoblotting; liqu
34                                        Using two-dimensional electrophoresis and liquid chromatograph
35                                              Two-dimensional electrophoresis and MALDI-TOF mass spect
36                                     By using two-dimensional electrophoresis and mass spectrometry (m
37    The protein was identified as HSP60 using two-dimensional electrophoresis and mass spectrometry an
38 ells, we used a proteomic approach involving two-dimensional electrophoresis and mass spectrometry to
39                                              Two-dimensional electrophoresis and mass spectrometry we
40 s of innovations in the core technologies of two-dimensional electrophoresis and mass spectrometry, a
41  in E. coli minicells using a combination of two-dimensional electrophoresis and mass spectrometry.
42  melanocyte versus melanoma cell lines using two-dimensional electrophoresis and mass spectrometry.
43                                              Two-dimensional electrophoresis and matrix-assisted lase
44 y ELISA to those independently determined by two-dimensional electrophoresis and showed that the two
45 om hearts subjected to coronary occlusion by two-dimensional electrophoresis and subsequent matrix-as
46 ith CRHSP-28 in rat acini following one- and two-dimensional electrophoresis and underwent a marked a
47 oduce a large number of species separable by two-dimensional electrophoresis and which we have propos
48         The 6C5-H4CA antigen was resolved by two-dimensional electrophoresis, and a partial protein s
49 sing high performance liquid chromatography, two-dimensional electrophoresis, and immunoblotting with
50 arget of EGCG using affinity chromatography, two-dimensional electrophoresis, and mass spectrometry f
51        We used immunoprecipitation, one- and two-dimensional electrophoresis, and mass spectrometry t
52    Outer membrane proteins were separated by two-dimensional electrophoresis, and proteins recognized
53 ce liquid chromatography (HPLC) and one- and two-dimensional electrophoresis, and the 3H label was de
54 re, performing further protein separation by two-dimensional electrophoresis, and utilizing mass spec
55                       Using highly sensitive two-dimensional electrophoresis-based proteomics, we ide
56  the protein, as determined by a pI shift on two-dimensional electrophoresis, but 14-3-3zeta dimeriza
57  free glutathione and identified by one- and two-dimensional electrophoresis coupled with mass spectr
58 ved by the cumulative time-resolved emission two-dimensional electrophoresis (CuTEDGE) technology fac
59                                              Two-dimensional electrophoresis demonstrated that Kelch
60                                              Two-dimensional electrophoresis demonstrated that produc
61         Consistent with these modifications, two-dimensional electrophoresis demonstrated that SWP3 h
62                          Further analysis by two-dimensional electrophoresis demonstrated three const
63  50 S subunit via a proteomic approach using two-dimensional electrophoresis, electroblotting/protein
64 andmark genomic scanning (RLGS) is a type of two-dimensional electrophoresis employed in the genome-w
65                                              Two-dimensional electrophoresis followed by immunoblotti
66 y SDS-polyacrylamide gel electrophoresis and two-dimensional electrophoresis followed by Western immu
67                                  Analysis by two-dimensional electrophoresis following in vivo phosph
68 lation by wild-type and E381A mutant ExoS by two-dimensional electrophoresis found the former to ADP-
69 tes of viral DNA replication, as revealed by two-dimensional electrophoresis, from transfections of h
70 ystematic comparison of 634 protein spots in two-dimensional electrophoresis gels across five experim
71 ation steps (reverse-phase HPLC and one- and two-dimensional electrophoresis gels), different enzymat
72 rved to migrate to multiple protein spots on two-dimensional electrophoresis gels.
73 abeled proteins are isolated by conventional two-dimensional electrophoresis: (i) nonreducing/reducin
74 rometric analysis of the changes observed in two-dimensional electrophoresis identified a number of p
75             Urine proteins were separated by two-dimensional electrophoresis in 32 patients with FSGS
76                              High-resolution two-dimensional electrophoresis in combination with the
77 in conjugates (50 to >200 kDa; pI 5.3-6.8 by two-dimensional electrophoresis) in bovine rod outer seg
78 aphic purification of greater than 400-fold, two-dimensional electrophoresis indicated that the strom
79                                              Two-dimensional electrophoresis is a critical technique
80 n recognition and quantification in one- and two-dimensional electrophoresis is demonstrated for bioa
81         To resolve the cartilage proteins by two-dimensional electrophoresis, it was necessary to rem
82                                        Using two-dimensional electrophoresis, mass spectrometry, immu
83 ns by using two complementary methodologies, two-dimensional electrophoresis/mass spectrometry and li
84                                      We used two-dimensional electrophoresis (nonequilibrium pH gradi
85                                              Two-dimensional electrophoresis of bovine lens zeta-crys
86  data obtained from combinations of one- and two-dimensional electrophoresis of completely or partial
87  by trypsin and by immunoblot analysis after two-dimensional electrophoresis of isolated lysosomes an
88                                              Two-dimensional electrophoresis of rat heart alphaB-crys
89 fects on DNA replication were analyzed using two-dimensional electrophoresis of replication intermedi
90 dently mutated to an alanine and analyzed by two-dimensional electrophoresis; only serine 4 was phosp
91 ; and Rubia Gallega, RG) were estimated from two-dimensional electrophoresis profiles of meat samples
92                                              Two-dimensional electrophoresis provided evidence that t
93 lization of Toxoplasma secretory products by two-dimensional electrophoresis revealed approximately 1
94                                              Two-dimensional electrophoresis revealed that PMA treatm
95 on in complex samples are also applicable to two-dimensional electrophoresis separations.
96 s, we constructed a high-voltage, automatic, two-dimensional electrophoresis system and used this in
97                                      A novel two-dimensional electrophoresis system to be carried out
98                                        Using two-dimensional electrophoresis, the extracellular prote
99 s in combination with thinner gels to reduce two-dimensional electrophoresis time about 80%.
100                                          The two-dimensional electrophoresis was used for analysis of
101                       Western analysis after two-dimensional electrophoresis was used to measure the
102 g by (35)S and by (14)C combined with native/two-dimensional electrophoresis, we assessed the synthes
103                                        Using two-dimensional electrophoresis, we demonstrate a struct
104                Subcellular fractionation and two-dimensional electrophoresis were used in conjunction
105 ned medium released by PMNs were resolved by two-dimensional electrophoresis with immobilized pH grad
106                                      We used two-dimensional electrophoresis with mass spectrometry t

 
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