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5 n estimated molecular mass of 77.3 kDa and a pI value of 5.66, characteristics consistent with transf
6 s are used as internal standards to assign a pI value to each individually detected mitochondrial eve
7 nce fully developed, it can potentially be a pI-based sample fractionation tool for proteomic analysi
8 ily oxidized in cultured cells, generating a pI 5.8 isoform, but an artificial C106A mutant was not.
9 dged by native gel electrophoresis and has a pI value of 4.55, as found for most of the fungi of beta
10 ll nucleic acid-interacting proteins, have a pI of 7.94 or higher; virtually all these 12,000 protein
12 ic and spectrophotometric titration showed a pI of 4.22 +/- 0.33 and apparent pK values of 6.74 +/- 0
15 he pI are often observed for proteins with a pI above 7.0 upon phosphorylation, whereas little change
16 ovo set of peptides/proteins, largely with a pI between 5.0 and 8.0 and a molecular mass distribution
19 tion of ErA, resulting in a main peak with a pI of 7.35 and an acidic species minor peak at 7.0, both
23 to polyriboinosinic:polyribocytidylic acid (pI:C), DCs mount a specific integrated stress response d
25 Only the predominant AMACR IA has an acidic pI and contains the previously identified peroxisomal ta
29 (four) were located in two strongly acidic (pI 4 to 4.9) domains in the distal N- and C-terminal reg
30 dominant B-cell epitopes within the acidic (pI 5.35) ankyrin repeat-containing 200-kDa major immunor
32 dies revealed that LAMP2 has a more alkaline pI in Pompe compared with control iPSC-CMs due largely t
33 sociated with dissolved proteins of alkaline pIs in surface seawater, while Zn was mainly associated
34 h a molecular weight of 33.38+/-0.34kDa, and pI of 6.30+/-0.15 was confirmed in samples of SOD extrac
35 eins differ widely in buffering capacity and pI and therefore the same PTMs may give rise to quite di
41 itive rate associated with accurate mass and pI measurements is presented to demonstrate the utility
44 antigen features, such as protein weight and pI, and subcellular localizations of bacterial proteins.
46 used to electrostatically stabilize the AOx (pI 4.3) on the anode operating on direct electrochemistr
47 ynthesized AOx-AuNPs conjugate from the AOx (pI 4.5) protein (zeta, -30mV) implied good stability of
50 s-Arg-(pI)DPhe-Tic-NH2], and 41 [Ac-Arg-Arg-(pI)DPhe-DNal(2')-NH2] were more potent (EC50 < 73 nM) th
51 e most potent MC3R agonists, 18 [Ac-Arg-Arg-(pI)DPhe-Tic-NH2], 1 [Ac-His-Arg-(pI)DPhe-Tic-NH2], and 4
52 he-Tic-(pNO2)DPhe-NH2, Ac-His-(pCl)DPhe-Arg-(pI)Phe-NH2, and Ac-Arg-(pCl)DPhe-Tic-(pNO2)DPhe-NH2, rev
53 Ac-Arg-Arg-(pI)DPhe-Tic-NH2], 1 [Ac-His-Arg-(pI)DPhe-Tic-NH2], and 41 [Ac-Arg-Arg-(pI)DPhe-DNal(2')-N
54 plate contains a sequentially reversed "Arg-(pI)DPhe" motif with respect to the classical "Phe-Arg" m
60 oint (pI) is particularly attractive because pI is a well-defined parameter and it is orthogonal to h
69 nificant relationship between the calculated pI of successfully crystallized proteins and the differe
73 ructed with axes of protein mass and charge (pI) and converted to density estimates comparable across
75 a and C/EBPdelta, and their binding to CIITA pI and pIV, in correlation with inhibition of IFN-gamma-
77 omponent ampholyte buffers with well-defined pI cutoff values, controlled separation of protein mixtu
80 most proteins, the experimentally determined pI is very close to that predicted by the databases.
82 ides of similar molecular mass but different pI, suggesting the possibility of posttranslational modi
84 xoS analyzed from eukaryotic cells displayed pI heterogeneity and prompted an analysis of this hetero
85 mammals, other properties of Spot 14 (i.e., pI, subcellular localization, transcriptional control an
87 roducible fractionation of model fluorescent pI markers and proteins is achieved using single membran
88 isoelectric focusing of several fluorescent pI markers and proteins is demonstrated across pH 3.8-7.
89 strating the applicability of the method for pI determination in micropreparative procedures within a
90 rmodynamics for adding and removing HCN from pI under Titan conditions suggests that such dynamics is
91 ermined as negatively charged glycoproteins (pI < 6) with molecular masses between 100 and 300 kDa.
95 noantennary glycans associated with the high-pI fractions, nor were predominantly tri- and tetra-ante
97 ved interconversion between the dark, higher pI and bright, lower pI GFP populations is tightly contr
98 tylcarboxylic acid, Anc, JRH420-12), Ac-His-(pI)DPhe-Arg-Trp-NH2 (JRH322-18), chimeric AGRP-melanocor
99 unds at all these hMC4R SNPs include Ac-His-(pI)DPhe-Tic-(pNO2)DPhe-NH2, Ac-His-(pCl)DPhe-Tic-(pNO2)D
100 to pt-DNA versus ds-DNA, and a difference in pI for these two complexes, whereas Klentaq does not, su
101 proteins uncovered unexpected differences in pI and/or size of specific proteins thought to be highly
104 yield of protein that has a broader range in pI, and reducing experimental time compared to conventio
106 DJ-1 isoforms, of which the acidic isoforms (pI 5.5 and 5.7) of DJ-1 monomer and the basic isoforms (
107 5.7) of DJ-1 monomer and the basic isoforms (pI 8.0 and 8.4) of SDS-resistant DJ-1 dimer are selectiv
110 creasing pHs, especially at pHs close to its pI (pH 4.0), indicating the occurrence of co-precipitati
113 horter variant form of IIA (IIAs, Mw 28 kDa, pI 9.65), which lacks the 5' half of the alternative fif
116 ly a single 39-kDa band and a single 39-kDa, pI 5.0 spot on one- and two-dimensional immunoblots of B
118 An immunoreactive protein spot (MW: 44 kDa, pI: 4.5) was microsequenced and the related cDNA was clo
119 trol the assembly of cytochrome c (12.5 kDa, pI 10.5) and azurin (13.9 kDa, pI 5.7) proteins into sep
120 , a protein spot of MW approximately 75 kDa, pI 5.5 was cored from a Coomassie-stained two-dimensiona
121 c (12.5 kDa, pI 10.5) and azurin (13.9 kDa, pI 5.7) proteins into separate 3D DNA nanocages, in a pr
123 tly all recombinant basic proteins (at least pI-1 > or = 6.94) may be purified from E. coli in a sing
125 nthesized and used to selectively enrich low pI peptides from complex mixtures for MALDI-MS detection
128 f apoptosis protein-binding protein with low pI (Diablo) protein translocates into the cytosol during
129 ibitor of apoptosis-binding protein with low pI (Smac/DIABLO) into the cytoplasm and substantial incr
131 ibitor of apoptosis-binding protein with low pI may be differentially released from the mitochondria,
132 ibitor of apoptosis-binding protein with low pI were released following the addition of TNF-alpha.
133 caspase/direct IAP-binding protein with low pI) and caspase-9 bind, is a promising strategy for inhi
134 caspases/direct IAP-binding protein with low pI), a factor that neutralizes the protective actions of
136 f apoptosis protein-binding protein with low pI), caspase-3 activity (but not procaspase-3 cleavage),
137 ibitor of apoptosis-binding protein with low pI); anti-apoptotic: XIAP (X-linked inhibitor of apoptos
138 caspases/direct IAP binding protein with low pI, and apoptosis-inducing factor release), caspase acti
141 etween the dark, higher pI and bright, lower pI GFP populations is tightly controlled by differential
143 wnregulated protein in A3HtrAOE with a mass, pI and MALDI-TOF spectrum consistent with outer membrane
145 le distributions of individual mitochondrial pI, accurate determination of the pI of individual mitoc
146 ses of redox proteins with acidic-to-neutral pI values have been obtained on pure alkanethiol as well
149 proteins show a substantial acidification of pI and require high salt concentrations for cooperative
152 We speculate that the directionality of pI's intermolecular and intramolecular =N-H(...)N hydrog
155 onstrated a separation of binary mixtures of pI markers and proteins without applying any external fi
159 n molecular weight that possessed a range of pI values were represented by molecular forms of CgA and
162 l fractionation of peptide mixtures based on pI can be accomplished by varying the pH of the aqueous
166 ic point and (2) the introduction of peptide pI is effective in minimizing both false positive and fa
167 on for measurable adsorption and the peptide pI, and proximity of cationic groups to the surface in t
172 cations (PTMs) on protein isoelectric point (pI) and molecular weight and displays the calculated pat
173 ted by differences in the isoelectric point (pI) and the ion exchange properties of the printed subst
174 accurate mass and peptide isoelectric point (pI) as identification criteria, and represents a change
176 luidic platforms for fast isoelectric point (pI) determinations via free-flow electrophoresis with in
177 fe style and a low median isoelectric point (pI) for all predicted proteins, suggesting a 'salt-in' s
178 ng protein with low pH of isoelectric point (pI) from the mitochondria, and the activation of caspase
179 ractionation based on the isoelectric point (pI) is particularly attractive because pI is a well-defi
180 l protein (ORF3), with an isoelectric point (pI) of 10.0 and a calculated molecular mass of 22.8 kDa.
181 tein Data Bank (PDB), the isoelectric point (pI) of a protein has been explored as a useful indirect
183 ely one pH unit below the isoelectric point (pI) of the recombinant proteins, most of the latter bind
184 uled out by comparing the isoelectric point (pI) values to the adsorption of proteins to lignin surfa
186 such as applied voltage, isoelectric point (pI), bulk pH, and bulk conductivity, on the protein trap
187 A novel continuous-flow isoelectric point (pI)-based sorting technique has been developed for prote
190 containing proteins with isoelectric points (pI values) higher than the pI of albumin, a second fract
192 g compounds with varying isoelectric points (pI) and pK(a) values over a range of aqueous solution pH
193 rved to exhibit distinct isoelectric points (pI) and, thus, distinct formal electrostatic charges.
194 (CIEF-WCID) method, the isoelectric points (pI) of complete intact polioviruses were determined.
196 es (i.e., those with low isoelectric points (pI)) by matrix-assisted laser desorption/ionization-mass
197 that likely have unique isoelectric points (pI), which are related to their surface compositions and
198 eawater exhibit alkaline isoelectric points (pIs of 8.10 and 8.37) and also acid Ips (4.82, 5.13, 5.4
200 tigate the chain conformations of polyimine (pI), a polymer identified as one major component of poly
201 s Senseless not in the primary SO precursor (pI) selection, but in the specification of pI progeny.
202 ed peptides from the theoretically predicted pI values was on average 0.21 pH units, which is more ac
203 k at 7.0, both comparing well with predicted pI values based on the sum of protein residue pKa values
205 copies regarding their selection pressures, pI values and tissue expression patterns, suggesting the
206 is expressed from three distinct promoters (pI, pIII, and pIV) in a developmental and cell type-spec
208 size polyacrylamide gel to determine protein pI followed by immobilization of pI-resolved proteins.
212 liquid separation technique in which protein pI is used as the first-dimension separation parameter.
216 ot analysis revealed that the representative pI of the 32-kDa sCD44 was 6.96 +/- 0.07 in POAG versus
217 an be optimized to generate highly resolved, pI-based fractions in solution which can be used for suc
219 rboxyl to lysine substitutions, 5K RNase Sa (pI=10.2), have been determined by NMR at 20 degrees C in
220 atable groups in ribonuclease Sa (RNase Sa) (pI=3.5), and a charge-reversed variant with five carboxy
222 that the intrinsic positive charges of SEVI (pI = 10.21) facilitate virion attachment to and fusion w
223 d been secreted by P. aeruginosa also showed pI heterogeneity with five charge forms ranging in pI fr
226 other hand, required the addition of a small pI range (4-6.5) of ampholytes to improve resolution and
228 ration and isolated peptides within specific pI ranges from sample mixtures, where the pI range was s
229 equence analysis of a 67.8 kDa protein spot (pI 5.7) on a Coomassie-stained two-dimensional (2D) gel
233 rency in Titan's atmosphere, indicating that pI could be photochemically active and drive chemistry o
238 s developed to calculate more accurately the pI values of peptides identified from experimental data.
239 idatively modified by carbonylation, and the pI 5.0 isoform is selectively accumulated in AD and PD.
240 ), and Lys (11.3 and 10.6) peptides, and the pI of BSA (4.8) and FN (5.7), were consistent with publi
242 eins with pI values in the same range as the pI of albumin, and a third fraction containing proteins
243 soelectric point-commonly referred to as the pI-can be defined as the point of singularity in a titra
246 tigate the disputed relationship between the pI of a protein and the pH at which it crystallizes.
247 the early days of solution biochemistry, the pI has been recorded and reported, and thus literature r
248 inylated oligodeoxynucleotide containing the pI or pIV binding sites, and chromatin immunoprecipitati
249 These devices allow one to determine the pI of a biomolecule from a sample mixture with moderatel
250 the improved device, it was applied for the pI fractionation of yeast proteome digest into 18 fracti
253 acterized by posttranslational change in the pI of sCD44 and hypophosphorylation, which clearly disti
254 These modifications cause changes in the pI of the protein by adding, removing or changing titrat
256 V light was demonstrated by the shift in the pI value of Bax on two-dimensional gels and confirmed by
258 with PNGase F or neuraminidase narrowed the pI range, indicating variable degrees of glycosylation a
259 alitatively with trends in B except near the pI of amylase, where physical stability was minimal.
260 found that a mobile phase pH value near the pI of the zwitterionic adsorbent surface leads to full r
261 ochondrial pI, accurate determination of the pI of individual mitochondria by the use of internal sta
262 d whey was explained by the proximity of the pI of whey protein (4.9-5.2), where proteins were found
263 proteins are mostly acidic, and based on the pI determined theoretically, apparently all recombinant
265 he electrophoretic field required to run the pI-based sorting is generated by the diffusion of buffer
267 tion of cell lysates with Mn(2+) shifted the pI of ExoS(E381D) to a pI identical to secreted ExoS.
268 Using this adjusted CIEF-WCID technique, the pI of biologically hazardous components like toxins or v
269 oelectric points (pI values) higher than the pI of albumin, a second fraction containing proteins wit
275 ic pI ranges from sample mixtures, where the pI range was simply set by the pH values of the buffer s
276 al muscle mitochondria) and to determine the pIs of other biological or nonbiological particles.
277 based program, pIMethylation, to predict the pIs for peptides with and without methyl esterification.
279 This allowed the determination of their pI via multispectral imaging of protein and pH sensor fl
281 bunits traveled primarily according to their pI and apparently were not associated with other protein
282 Peptide fractionation according to their pI is also widely used in current proteomics sample prep
284 peptides left the focusing gel because their pIs are higher than the upper limit of the immobilized p
287 IEF results were consistent with theoretical pIs of methylated peptides calculated by pIMethylation.
288 type cytochrome c oxidase (T. thermophilus) (pI = 6.0) exhibit optimal voltammetric responses on 1:1
290 mutants were also demonstrated to migrate to pI values consistent with predictions (pI 7.0 for one de
291 observed post-translational modifications to pI shifts relative to the unmodified protein of interest
292 More recently, an off-line method that uses pI-based separation on immobilized pH gradients was deve
293 ed VCP expression and an acidic shift in VCP pI, which was inhibited by protein phosphatase 2A treatm
296 longs to the class of neutral proteases with pI value of 6.8, optimal proteolytic activity displayed
298 , a second fraction containing proteins with pI values in the same range as the pI of albumin, and a
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