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1  of a series of proline variants of [28-111] alpha-lactalbumin.
2 osecond dynamics of native and the denatured alpha-lactalbumin.
3 he complex of alphaB-crystallin and unfolded alpha-lactalbumin.
4 ne resonances of the molten globule state of alpha-lactalbumin.
5 by Dobson and Kim for the homologous protein alpha-lactalbumin.
6 ptide containing only residues 101 to 111 of alpha-lactalbumin.
7 nd to the reduced, carboxymethylated form of alpha-lactalbumin.
8 he permeability of endothelial monolayers to alpha-lactalbumin.
9 larly evident for 125I-alpha-globin and 125I-alpha-lactalbumin.
10  of the native main chain fold of apo bovine alpha-lactalbumin.
11 peptides derived from beta-lactoglobulin and alpha-lactalbumin.
12 s approximately 1.3 times as high as that of alpha-Lactalbumin.
13  denaturation of the globular protein, human alpha-lactalbumin.
14 mplex of bovine Gal-T1-Mn(2+)-UDP-GalNAc-Glc-alpha-lactalbumin.
15 tates of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants
16 ion of four proteins, bovine S-carboxymethyl-alpha-lactalbumin (a disordered form of the protein with
17                            S-(Carboxymethyl)-alpha-lactalbumin, a disordered form of the protein with
18 e immunized SWXJ mice with recombinant mouse alpha-lactalbumin, a lactation-dependent, breast-specifi
19                                       Bovine alpha-lactalbumin, a small acidic Ca(2+)-binding milk pr
20                                              alpha-Lactalbumin, a small calcium-binding protein, form
21  to determine whether the disulfide bonds of alpha-lactalbumin account for the lack of cooperative fo
22 as decreased from pH 7 toward pH 2, at which alpha-lactalbumin adopts a molten globule state, a small
23 creasing degree of suppression of insulin or alpha-lactalbumin aggregation correlated with a decreasi
24  cheese whey (CW), beta-lactoglobulin (BLG), alpha-lactalbumin (ALA) and bovine serum albumin (BSA).
25 , ALA-1) and type-3 (without calcium, ALA-3) alpha-lactalbumin (ALA) were examined.
26 ting known bovine milk IgE-binding epitopes [alpha-lactalbumin (ALA), beta- and kappa-casein] and the
27 , namely cationic lysozyme (Lys) and anionic alpha-lactalbumin (aLac), both of which can be found in
28                                     By using alpha-lactalbumin, alcohol dehydrogenase, and insulin as
29          The pathway of oxidative folding of alpha-lactalbumin (alpha LA) (four disulfide bonds) has
30                                              alpha-Lactalbumin (alpha LA) forms a well-populated equi
31  heating cow milk at 80 degrees C for 60min, alpha-lactalbumin (alpha-la) and beta-lactoglobulin (bet
32                                       Bovine alpha-lactalbumin (alpha-La) and kappa-casein (CN) displ
33   The reversible thermal denaturation of apo alpha-lactalbumin (alpha-LA) and lysozyme was measured i
34  camel milk at 80 degrees C for 60min, camel alpha-lactalbumin (alpha-la) and peptidoglycan recogniti
35 he free energy of unfolding (DeltaG(D-N)) of alpha-lactalbumin (alpha-LA) as a function of net charge
36 fluorescence properties of three variants of alpha-lactalbumin (alpha-LA) containing a single tryptop
37                   The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized usin
38                  The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a proto
39                                       Bovine alpha-lactalbumin (alpha-LA) has been shown by intrinsic
40              Recently, the molten globule of alpha-lactalbumin (alpha-LA) has been shown to adopt a n
41                                              alpha-Lactalbumin (alpha-LA) is a two-domain calcium-bin
42                                              Alpha-lactalbumin (alpha-LA) is one of the whey proteins
43    The 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and
44 his variant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number
45 to study the adsorption of Alexa 555 labeled alpha-lactalbumin (alpha-LA) on two chemically identical
46 LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globul
47 ously identified calcium binding residues in alpha-lactalbumin (alpha-LA) was investigated by site-di
48    Results showed that increased contents of alpha-lactalbumin (alpha-La) were associated with increa
49 n heated whey protein isolate (WPI) and pure alpha-lactalbumin (alpha-La) were investigated.
50  side-chain packing in the molten globule of alpha-lactalbumin (alpha-LA), a highly fluctuating, non-
51                                    For human alpha-lactalbumin (alpha-LA), the equilibrium molten glo
52 on level of beta-lactoglobulin (beta-LG) and alpha-lactalbumin (alpha-LA).
53 e binds to a mammary gland-specific protein, alpha-lactalbumin (alpha-LA).
54 reviously for the archetypal molten globule, alpha-lactalbumin (alpha-LA); this difference may be due
55           Electrostatic interactions between alpha-lactalbumin (alpha-lac) and carboxymethyldextran (
56 structures of complexes made of the proteins alpha-Lactalbumin (alphaLA) and myoglobin (Mb) with the
57 e) and in the presence of a thiol initiator, alpha-lactalbumin (alphaLA) denatures by shuffling its f
58                          Four proteins, BSA, alpha-lactalbumin (alphaLA), lysozyme, and beta-lactoglo
59                                              Alpha-lactalbumin (alphaLA)-IIIA is a major kinetic inte
60  models of the molten globule state of human alpha-lactalbumin (alphaLA).
61 ve unfolding and oxidative folding of bovine alpha-lactalbumin (alphaLA).
62 LA-IIA is a partially folded intermediate of alpha-lactalbumin (alphaLA).
63 I-alpha-globin to approximately 85% for 125I-alpha-lactalbumin and 125I-albumin.
64 mmunoglobulin, lactoperoxidase, lactoferrin, alpha-lactalbumin and beta-lactoglobulin from sheep chee
65 hange the bioactivities of proteins, such as alpha-lactalbumin and beta-lactoglobulin in vitro.
66                              Immune-reactive alpha-lactalbumin and beta-lactoglobulin were found in t
67 ll as immunocytochemistry for milk proteins: alpha-lactalbumin and beta-lactoglobulin.
68 whey protein isolates with varying ratios of alpha-lactalbumin and beta-lactoglobulin.
69                              Proteins in the alpha-lactalbumin and c-type lysozyme family have been s
70 the alpha-helical domain is observed in both alpha-lactalbumin and c-type lysozyme; however, the deta
71 rsistent expression of the milk protein gene alpha-lactalbumin and delayed expression of genes associ
72 guously identify the peak as a fragment from alpha-lactalbumin and eliminate a large number of spurio
73  consists of residues 20 through 36 of human alpha-lactalbumin and includes the entire B-helix.
74 fference in kinetic folding pathways between alpha-lactalbumin and lysozyme can be explained by the d
75  a tumoricidal complex of partially unfolded alpha-lactalbumin and oleic acid (OA).
76 r in preventing the amorphous aggregation of alpha-lactalbumin and the amyloid fibril formation of al
77 B-crystallin became entangled with unfolding alpha-lactalbumin and was a major portion of the resulti
78     RNA levels of endogenous MMTV as well as alpha-lactalbumin and whey acidic protein (WAP) were ele
79                                          The alpha-lactalbumins and c-type lysozymes have virtually i
80  beta-lactoglobulin A, beta-lactoglobulin B, alpha-lactalbumin, and albumin).
81 atalase, pyruvate kinase, albumin, lysozyme, alpha-lactalbumin, and beta-lactoglobulin.
82  For gammaII-crystallin, myoglobin, barnase, alpha-lactalbumin, and cytochrome c the foldons and some
83 that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants o
84 lies of c-type lysozyme and one subfamily of alpha-lactalbumin are defined from 78 sequences, and the
85                            Using insulin and alpha-lactalbumin as model target proteins, we also show
86                                  We selected alpha-lactalbumin as our target vaccine autoantigen beca
87 ed that the levels of beta-lactoglobulin and alpha-lactalbumin associated with the casein micelles in
88 he molten globule state from measurements on alpha-lactalbumin at pH 2.0 over the temperature range 2
89  were discovered for chordin-like protein 2, alpha-lactalbumin, beta-1,4-galactosyl transferase, and
90 ower limits of detection for model proteins, alpha-lactalbumin, beta-lactoglobulin A, and beta-lactog
91 uccessful OIT outcome, as high IgE levels to alpha-lactalbumin, beta-lactoglobulin and casein are ass
92 Humanising' the model formulas by increasing alpha-lactalbumin:beta-lactoglobulin enhanced heat stabi
93                                       In low alpha-lactalbumin:beta-lactoglobulin formulas, protein-p
94 ctions between proteins were minimal in high alpha-lactalbumin:beta-lactoglobulin formulas.
95 protein-protein interactions with increasing alpha-lactalbumin:beta-lactoglobulin has important impli
96 ms (5.5% protein) were formulated to contain alpha-lactalbumin:beta-lactoglobulin ratios of 0.1, 0.5,
97 icated that increased heat stability in high alpha-lactalbumin:beta-lactoglobulin samples was due to
98              The internal dynamics of bovine alpha-lactalbumin (BLA) and its molten globules (MBLA) h
99             Prolonged heating of holo bovine alpha-lactalbumin (BLA) at 80 degrees C in pH 7 phosphat
100                      The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured st
101 olding of the molten globule state of bovine alpha-lactalbumin (BLA) has been obtained using NMR spec
102 e Ca(2+)-free apo form of recombinant bovine alpha-lactalbumin (BLA) is sufficiently stabilised in it
103 s of 125I-labeled human alpha-globin, bovine alpha-lactalbumin, bovine serum albumin, or chicken lyso
104 w-A, consists of residues 72-100 from bovine alpha-lactalbumin, but with Cys 73, Cys 77, and Cys 91 r
105 values lower than the limit of detection and alpha-lactalbumin by approximately 34%, and was reduced
106      Thus, molten globule formation in human alpha-lactalbumin can be driven by the isolated alpha-su
107 main of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7 (IM7),
108                                              alpha-Lactalbumin consists of two subdomains, and the al
109 ill less structured and less stable than the alpha-lactalbumin construct.
110 ts derived from the alpha-subdomain of human alpha-lactalbumin containing the A, B, D, and 3(10) heli
111 havior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has b
112  whereas its complex with the substrates and alpha-lactalbumin, crystallizes in a conformation (2.3A
113 wn non-two-state folding proteins, including alpha-lactalbumin, cytochrome c, intestinal fatty acid b
114 similar to the molten globule state of human alpha-lactalbumin, demonstrates a marginal increase in t
115 ta shows that the heat capacity increment of alpha-lactalbumin denaturation highly correlates with th
116 ed dissociation of an unassigned peak in the alpha-lactalbumin digest provided sufficient data to una
117 tion of R120G alphaB-crystallin to unfolding alpha-lactalbumin enhanced the kinetics and extent of it
118 rying conditions than beta-lactoglobulin and alpha-lactalbumin, especially at longer drying times.
119 rent from one another; the stronger one, apo-alpha-lactalbumin, exhibited a Kd of 35 microM.
120 tiary structure, whereas the intermediate of alpha-lactalbumin exhibits the characteristics of a molt
121 specific for non-native domains since native alpha-lactalbumin fails to interact with Hip.
122 ructural features characteristic of a native alpha-lactalbumin fold.
123                  The calcium binding protein alpha-lactalbumin folds via a molten globule intermediat
124 edure was used to study the refolding of apo alpha-lactalbumin following dilution from guanidinium ch
125 ages displayed a strong immunoreactivity for alpha-lactalbumin for 2-96 h.
126                                          All alpha-lactalbumins form a well populated molten globule
127 s a result, the denaturational transition of alpha-lactalbumin from the native to a highly ordered co
128                                Two different alpha-lactalbumin genetic constructs are studied: [28-11
129                   Although immunization with alpha-lactalbumin had no effect on fertility and birth n
130 actions in stabilizing the molten globule of alpha-lactalbumin has been prepared.
131 dynamics of the molten globule (MG) state of alpha-lactalbumin have been characterized using (15)N tr
132                          Structures of human alpha-lactalbumin have been generated with significantly
133 ted versus flat) of fibrils of lysozyme, apo-alpha-lactalbumin, HET-s (218-289) prion, and a short po
134  In agreement with previous studies on human alpha-lactalbumin (HLA) the unfolding process for BLA ha
135 s of both cytochrome c and disulfide-reduced alpha-lactalbumin homodimers dissociate by a symmetrical
136             Similar results are observed for alpha-lactalbumin homodimers.
137 iting E3alpha-catalyzed conjugation to human alpha-lactalbumin, HsUbc2b-ubiquitin thiolester exhibits
138 es of non-native states of the protein human alpha-lactalbumin (human alpha-LA) with a detailed atomi
139 ar, CI2, spectrin R16 domain, Arc repressor, alpha-lactalbumin, IM7, IM9, and spectrin R17 domain.
140  fertility and birth numbers, pups nursed by alpha-lactalbumin-immunized mice showed significantly di
141            The change in structure of bovine alpha-lactalbumin in environments of decreasing pH from
142 a protein mixture consisting of transferrin, alpha-lactalbumin, insulin, and alpha-2-macroglobulin.
143                                      Because alpha-lactalbumin is conditionally expressed only during
144 f the nonnative structure for the folding of alpha-lactalbumin is discussed.
145 esponding to residues 101-111 of the protein alpha-lactalbumin is remarkably structured in isolation
146 ds (human carbonic anhydrase I, enolase, and alpha-lactalbumin) is achieved at 50- to 100-fold excess
147 ression of a fusion protein comprising human alpha lactalbumin joined by an enterokinase cleavable li
148 gated using six proline variants of [28-111] alpha-lactalbumin, L11P, L12P, M30P, I95P, K108P and Q11
149                                 In addition, alpha-lactalbumin (LA) enhances this Glc-T activity more
150              Under reducing conditions where alpha-lactalbumin (LA) unfolds and aggregates, XaHspA 36
151 se (beta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA), a mammary gland-specific protein
152                        Aromatic cluster 1 of alpha-lactalbumin (LA), a substructure adjacent to the c
153 g to substrates and to the modifier protein, alpha-lactalbumin (LA), by over 99%.
154                           In the presence of alpha-lactalbumin (LA), it transfers Gal to Glc, which i
155                           In the presence of alpha-lactalbumin (LA), the Gal acceptor specificity is
156 le describes some of these proteins, such as alpha-lactalbumin, lactoferrin, osteopontin, and milk fa
157 transcripts, encoding beta-casein (CSN2) and alpha-lactalbumin (LALBA), make up 45% of the total pool
158 rast to the isolated alpha-helical domain of alpha-lactalbumin, Lyso-alpha with two native disulfide
159 region of hen lysozyme and a set of chimeric alpha-lactalbumin--lysozyme constructs.
160                                HAMLET (human alpha-lactalbumin made lethal to tumor cells) is a tumor
161  extraordinary manner in which HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) kills a wi
162 rsity in determining the overall fold of the alpha-lactalbumin molten globule.
163                      However, in the case of alpha-lactalbumin more mass values were needed, and low
164 r, whey acidic protein mRNA was reduced, and alpha-lactalbumin mRNA was undetectable.
165 n E3alpha-catalyzed conjugation of the human alpha-lactalbumin N-end rule substrate shows Ubc2bS120D
166                                          The alpha-lactalbumins of members of the Camelidae family ar
167 f lactoferrin (P < 0.01) and reduced that of alpha-lactalbumin (only at 90 min) (P < 0.05).
168 n 125I-lysozyme turnover, and decreased 125I-alpha-lactalbumin or 125I-albumin degradation by approxi
169 vents: The ATP-dependent degradation of 125I-alpha-lactalbumin or 125I-albumin is probably mediated a
170 ltured in an 18-h ELISpot assay with casein, alpha-lactalbumin, or beta-lactoglobulin.
171 tion had a larger increase in IgG4 levels to alpha-lactalbumin (P = 0.034), beta-lactoglobulin (P = 0
172 ecific IgE levels towards the milk allergens alpha-lactalbumin (P = 0.048), beta-lactoglobulin (P = 0
173 lso less structured and less stable than the alpha-lactalbumin peptide.
174 less structured than the corresponding human alpha-lactalbumin peptide.
175 , did not fibrillate, although Zn(2+)-loaded alpha-lactalbumin precipitated out of solution as amorph
176 of the whey proteins, beta-lactoglobulin and alpha-lactalbumin, promoted colour change from blue to r
177 ddition, the immobilized derivate hydrolyzed alpha-lactalbumin protein with a higher affinity than be
178 om human milk but did affect lactoferrin and alpha-lactalbumin proteolysis and emulsion disintegratio
179       We found that immunoreactivity against alpha-lactalbumin provides substantial protection and th
180  both CKbeta4GT-I and CKbeta4GT-II encode an alpha-lactalbumin-responsive, UDP-galactose:N-acetylgluc
181 reased levels of MMTV, beta-casein, WAP, and alpha-lactalbumin RNA in virgin mammary glands compared
182                          Mice immunized with alpha-lactalbumin showed extensive T-cell-mediated infla
183      A mixture of bovine carbonic anhydrase, alpha-lactalbumin, soybean trypsin inhibitor, and ovalbu
184 e Camelidae family are the only of described alpha-lactalbumins that carry two AsnGly sequences.
185  enthalpy and entropy of the denaturation of alpha-lactalbumin to compact denatured state are always
186                                        Thus, alpha-lactalbumin vaccination may provide safe and effec
187 ration, the percentage of positive cells for alpha-lactalbumin was significantly higher when compared
188 on, the most active chaperone of insulin and alpha-lactalbumin was the Hsp27 (elongated) dimer, the s
189        A specific substrate of this pathway, alpha-lactalbumin, was ubiquitinated faster in the diabe
190 epithelial marker CK14, and lactocyte marker alpha-lactalbumin were amongst the genes most highly exp
191                The trypsin-digested spots of alpha-lactalbumin were analysed by MALDI-TOF mass spectr
192 00 degrees C, whereas 218+/-43 mg/L residual alpha-lactalbumin were found at 130 degrees C.
193  emulsions with the highest concentration of alpha-lactalbumin were most stable to oxidation during s
194 es binding sites for the oligosaccharide and alpha-lactalbumin, when compared to the ligand-free stru
195     The calcium-depleted form of the protein alpha-lactalbumin, which displays a cluster of acidic am
196                      The denatured states of alpha-lactalbumin, which have features of a molten globu
197 nd gave very few spurious masses, and bovine alpha-lactalbumin, which under the conditions used, gave
198 ty with norbixin than beta-lactoglobulin and alpha-lactalbumin, while kappa-casein bound with norbixi
199 red by the aggregation of reduced insulin or alpha-lactalbumin, with Hsp27 self-association as monito

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