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1 kinase 1 (PDK1) on Thr346 to inactivate the pyruvate dehydrogenase complex.
2 of the lipoyl-bearing subunit (E(2)) of the pyruvate dehydrogenase complex.
3 gluconeogenic substrates by inactivating the pyruvate dehydrogenase complex.
4 PDH2, which encodes a subunit of the plastid pyruvate dehydrogenase complex.
5 ld-type kinase toward the protein substrate, pyruvate dehydrogenase complex.
6 lipoamide dehydrogenase associated with the pyruvate dehydrogenase complex.
7 at may catalyze the dephosphorylation of the pyruvate dehydrogenase complex.
8 nt, uncompetitive inhibitor of the bacterial pyruvate dehydrogenase complex.
9 ologic phenotypes, or PDHX, a subunit of the pyruvate dehydrogenase complex.
10 sion of pyruvate to acetyl-coenzyme A by the pyruvate dehydrogenase complex.
11 in kinase that regulates the activity of the pyruvate dehydrogenase complex.
12 edium, likely because of the activity of the pyruvate dehydrogenase complex.
13 the tricarboxylic acid (TCA) cycle enzymes, pyruvate dehydrogenase complex, 2-oxoglutarate dehydroge
14 decreases occurred in the activities of the pyruvate dehydrogenase complex (-41%), isocitrate dehydr
15 ia, in the absence (control) and presence of pyruvate dehydrogenase complex activation by dichloroace
21 et-induced obese mice significantly augments pyruvate dehydrogenase complex activity with reduced pho
24 The assembled core structure of mammalian pyruvate dehydrogenase complex also includes the dihydro
25 es were tested by ELISA for E2 components of pyruvate dehydrogenase complex and 2-oxoglutarate dehydr
26 or entry points to oxidative metabolism (eg, pyruvate dehydrogenase complex and Acyl-CoA dehydrogenas
27 ferase (tE2) of the Saccharomyces cerevisiae pyruvate dehydrogenase complex and complexes of the tE2
29 phosphate (HEThDP) with the Escherichia coli pyruvate dehydrogenase complex and its E1 subunit (PDHc-
31 rifies the essential nature of the plastidic pyruvate dehydrogenase complex and its role in embryo fo
32 utomers coexist on the E1 component of human pyruvate dehydrogenase complex and pyruvate oxidase.
33 ase-specific loss of immune tolerance to the pyruvate dehydrogenase complex and subsequent developmen
34 rotein complexes identified in our analysis, pyruvate dehydrogenase complex and succinate dehydrogena
35 e of oxythiamine, which can inhibit both the pyruvate dehydrogenase complex and transketolase, result
36 was determined by measuring the activity of pyruvate dehydrogenase complex, and cellular metabolic s
37 LUT4, hexokinase II, the E1 component of the pyruvate dehydrogenase complex, and subunits of all four
39 l analysis showing that the lipoyl moiety of pyruvate dehydrogenase complex appears to be involved in
41 and kinetic parameters as determined by the pyruvate dehydrogenase complex assay; (ii) in thermostab
43 of the E1 component of the Escherichia coli pyruvate dehydrogenase complex become organized only on
44 enase kinase (PDK) inhibit the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the
45 enzyme form the structural core of the human pyruvate dehydrogenase complex by providing the binding
46 ively regulate activity of the mitochondrial pyruvate dehydrogenase complex by reversible phosphoryla
47 cetyltransferase (E2) component of mammalian pyruvate dehydrogenase complex can form a 60-mer via ass
49 e that loss of PDHK4, a key regulator of the pyruvate dehydrogenase complex, caused a profound cell g
50 ites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distan
53 s (R1-2) as containing the E2 subunit of the pyruvate dehydrogenase complex, dihydrolipoamide acetylt
54 e two active centers of the Escherichia coli pyruvate dehydrogenase complex E1 component provides a s
55 (ThDP) binding site of the Escherichia coli pyruvate dehydrogenase complex E1 subunit (PDHc-E1), and
56 een in the structure of the Escherichia coli pyruvate dehydrogenase complex E1 subunit (PDHc-E1), mas
57 hondrial matrix-located citrate synthase and pyruvate dehydrogenase complex E1alpha-subunit polypepti
58 y biliary cirrhosis (PBC) is the presence of pyruvate dehydrogenase complex E2 subunit (PDC-E2) antim
59 e S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) was isolated from a
60 lecule in BEC, we examined the expression of pyruvate dehydrogenase complex-E2 (PDC-E2) messenger RNA
61 fferential expression of glycolysis, plastid pyruvate dehydrogenase complex, fatty acid, and lipid sy
62 The PKCdelta/retinol complex signaled the pyruvate dehydrogenase complex for enhanced flux of pyru
64 acetyltransferase (E2) catalytic core of the pyruvate dehydrogenase complex from Bacillus stearotherm
67 nase (PDH), the first component of the human pyruvate dehydrogenase complex, has two isoenzymes, soma
68 s (HiBECs) translocate the E2 subunit of the pyruvate dehydrogenase complex immunologically intact in
69 f pdhD, putatively encoding a subunit of the pyruvate dehydrogenase complex, impairs survival of both
70 ute to the tissue-specific regulation of the pyruvate dehydrogenase complex in normal and pathophysio
72 without increased glucose oxidation through pyruvate dehydrogenase complex in the energy-poor, hyper
73 complex that spontaneously reconstituted the pyruvate dehydrogenase complex in the presence of native
74 hyperphosphorylation and inactivation of the pyruvate dehydrogenase complex in these metabolic condit
75 ly resembles that of the lipoyl domains from pyruvate dehydrogenase complexes, in accord with the exi
76 ainst a complex set of proteins, among which pyruvate dehydrogenase complex is considered the main au
78 component of this entire class of bacterial pyruvate dehydrogenase complexes is responsible for bind
79 rase), the E2 component of the mitochondrial pyruvate dehydrogenase complex, is a novel metabolic lon
80 E1 (pyruvate dehydrogenase) component of the pyruvate dehydrogenase complex, it has not proved possib
81 ensional reconstruction of the bovine kidney pyruvate dehydrogenase complex (M(r) approximately 7.8 x
82 t indicates that inhibition of the bacterial pyruvate dehydrogenase complex may represent a promising
84 f light on the activity of the mitochondrial pyruvate dehydrogenase complex (mt-PDC) by using intact
85 E1 component (pyruvate decarboxylase) of the pyruvate dehydrogenase complex of Bacillus stearothermop
86 poyl acetyltransferase (E2) component of the pyruvate dehydrogenase complex of Bacillus stearothermop
88 ct of its activity, the inactive form of the pyruvate dehydrogenase complex (P-Pdc), both of which ar
89 mportance of muscle pyruvate availability to pyruvate dehydrogenase complex (PDC) activation during i
90 increasing CHO oxidation in vivo, using the pyruvate dehydrogenase complex (PDC) activator, dichloro
91 uscle protein: DNA ratio, a 56% reduction in pyruvate dehydrogenase complex (PDC) activity (P < 0.05)
94 ion status of glycogen phosphorylase and the pyruvate dehydrogenase complex (PDC) and on the accumula
95 or dephosphorylation and reactivation of the pyruvate dehydrogenase complex (PDC) and, by this means,
96 w that all the subunits of the mitochondrial pyruvate dehydrogenase complex (PDC) are also present an
98 and, in particular, the E2 component of the pyruvate dehydrogenase complex (PDC) are the target of a
99 yl-CoA acetyltransferase 1 (ACAT1) regulates pyruvate dehydrogenase complex (PDC) by acetylating pyru
103 cetyltransferase (E2) component of mammalian pyruvate dehydrogenase complex (PDC) consists of 60 COOH
104 oantibodies to the assumed major autoantigen pyruvate dehydrogenase complex (PDC) dihydrolipoamide ac
106 ogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells.
107 structural diversity of the E2 component of pyruvate dehydrogenase complex (PDC) in normal and disea
108 any putative (causative) association between pyruvate dehydrogenase complex (PDC) inhibition and lact
121 cterized by serum autoantibodies against the pyruvate dehydrogenase complex (PDC) located in the inne
122 e carbohydrate reserves, the reaction of the pyruvate dehydrogenase complex (PDC) must be down-regula
123 poyl domain, p45, has been identified in the pyruvate dehydrogenase complex (PDC) of the adult parasi
125 ion in adjusting the activation state of the pyruvate dehydrogenase complex (PDC) through determining
126 ogenase kinase (PDHK) is an integral part of pyruvate dehydrogenase complex (PDC) to which it is anch
127 rase (E2) subunit of the maize mitochondrial pyruvate dehydrogenase complex (PDC) was postulated to c
128 wing 2-oxo acid dehydrogenase complexes: the pyruvate dehydrogenase complex (PDC), the branched chain
129 pyruvate dehydrogenase (E1) in the mammalian pyruvate dehydrogenase complex (PDC), whose activity is
131 ized that PDK4 up-regulation, which inhibits pyruvate dehydrogenase complex (PDC)-dependent carbohydr
132 immunized rabbits develop high-titer Abs to pyruvate dehydrogenase complex (PDC)-E2, the major autoa
144 oligodeoxynucleotides (ODN) on responses to pyruvate dehydrogenase complex (PDC, the autoantigen in
145 49 (92%), with specificity directed against pyruvate dehydrogenase complex (PDC-E2) alone in 22 of 4
146 poylated enzymes such as the E2 component of pyruvate dehydrogenase complex (PDC-E2) are targets for
147 they were specifically directed against the pyruvate dehydrogenase complex (PDC-E2) in 15 of 19 pati
150 hondrial response to the E2 component of the pyruvate dehydrogenase complex (PDC-E2), has unique feat
151 e acetyltransferase, the E2 component of the pyruvate dehydrogenase complex (PDC-E2), is the autoanti
152 cognized by AMA are the E2 components of the pyruvate dehydrogenase complex (PDC-E2), the branched ch
153 oantigens including the E2 components of the pyruvate dehydrogenase complex (PDC-E2), the branched-ch
154 ecular mimicry between the E2 subunit of the pyruvate dehydrogenase complex (PDC-E2), the major mitoc
161 ry biliary cirrhosis (PBC), E2 components of pyruvate dehydrogenase complexes (PDC-E2), has a lipoate
162 , amino acids 159 to 167 on E2 components of pyruvate dehydrogenase complexes (PDC-E2), the major mit
165 nodominant mitochondrial autoantigen of PBC (pyruvate dehydrogenase complex [PDC-E2]) was addressed.
173 cherichia coli and report that disruption of pyruvate dehydrogenase complex (PDHc), which converts py
176 oxylase variant, or to the E1 subunit of the pyruvate dehydrogenase complex (PDHc-E1) from Escherichi
178 fpr promoter region as the E1 subunit of the pyruvate dehydrogenase complex (PDHE1), a central enzyme
179 drogenase kinase 4 (PDK4) is upregulated and pyruvate dehydrogenase complex phosphorylation is increa
180 s to be a common feature in the phylogeny of pyruvate dehydrogenase complexes, protein dynamics is an
182 e acetyltransferase (tE(2)) component of the pyruvate dehydrogenase complex reveal an extraordinary e
183 he E3-binding domain (E3BD) of the mammalian pyruvate dehydrogenase complex show that hSBDb has an ar
184 ese novel genetic interactions involving the pyruvate dehydrogenase complex suggested a new role for
185 mitochondrial antibodies that react with the pyruvate dehydrogenase complex, targeting the inner lipo
186 boxylate pyruvate: the E1 component of human pyruvate dehydrogenase complex, the E1 subunit of Escher
187 e investigated whether the E2 subunit of the pyruvate dehydrogenase complex, the E2 subunit of the br
188 chondrial protein kinase that phosphorylates pyruvate dehydrogenase complex, thereby down-regulating
189 dehydrogenase kinase 2 (PDHK2) inhibits the pyruvate dehydrogenase complex, thereby regulating entry
190 umor activity is its ability to activate the pyruvate dehydrogenase complex through inhibition of pyr
191 ch that down-regulates activity of the human pyruvate dehydrogenase complex through reversible phosph
192 t binding of the lipoyl domain 2 (L2) of the pyruvate dehydrogenase complex to PDK3 induces a "cross-
193 n exposure of LThDP to the E1 subunit of the pyruvate dehydrogenase complex was 0.4 s(-1), still more
195 KGDH enzymatic activity, whereas the related pyruvate dehydrogenase complex was unmodified by TFEC an
196 CCase subunits; (2) four subunits to plastid pyruvate dehydrogenase complex were 25% to 70% down-regu
197 stearothermophilus and Enterococcus faecalis pyruvate dehydrogenase complexes were determined and rev
198 g protein, inactivated kinase-depleted maize pyruvate dehydrogenase complex when incubated with MgATP
199 apicoplast LipDH is an integral part of the pyruvate dehydrogenase complex which occurs only in the
200 ion that was required to elicit a 50% active pyruvate dehydrogenase complex, which indicates a marked
201 complex, the E1 subunit of Escherichia coli pyruvate dehydrogenase complex, yeast pyruvate decarboxy
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