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1 hibited a reduced affinity for the substrate ribulose 1,5-bisphosphate.
2 poor ability to recover from incubation with ribulose 1,5-bisphosphate.
3 xidative damage of the CO2 acceptor molecule ribulose 1,5-bisphosphate.
4 le sugar phosphates, including its substrate ribulose 1,5-bisphosphate.
5 nitiated by abstraction of the 3-proton of d-ribulose 1,5-bisphosphate.
6 CO(2), to permit its efficient fixation onto ribulose 1,5-bisphosphate.
7 nylalanine 342 had an increased affinity for ribulose-1,5-bisphosphate.
8 xygenase oxygenates rather than carboxylates ribulose-1,5-bisphosphate.
9 e abstraction of a proton from the substrate ribulose-1,5-bisphosphate.
10 [Formula: see text]), 3-phosphoglycerate, or ribulose-1,5-bisphosphate.
11 s involved in the conversion of glycolate to ribulose-1,5-bisphosphate.
12 acterial Rubisco is not readily inhibited by ribulose 1,5-bisphosphate and fallover is not observed,
13 not only carboxylation and oxygenation of d-ribulose 1,5-bisphosphate but also other promiscuous, pr
15 rains revealed that either form I or form II ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC
16 at there was specific accumulation of form I ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC
17 ymes, including the key Calvin Cycle enzyme, Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco
20 lobal photosynthesis, compartmentalize their Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase (Rubisco
21 laveria bidentis, a dicotyledonous C4 plant, ribulose 1,5-bisphosphate carboxylase (rubisco) accumula
22 ivity of the CO2-fixing Calvin cycle enzyme, ribulose 1,5-bisphosphate carboxylase (RubisCO), prevent
23 g of the presequence of the small subunit of ribulose 1,5-bisphosphate carboxylase fused to the cytoc
27 assembles around many copies of the enzymes ribulose 1,5-bisphosphate carboxylase/ oxygenase and car
28 in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco).
29 n dioxide fixation relies on the function of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
30 sisting of a proteinaceous shell filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO
31 biological selection of randomly mutagenized ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
34 e effects of temperature on gas exchange and ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
35 oxide gas, catalyzed primarily by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
36 that is required for the light activation of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
39 ate, the substrate for the CO2 fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
40 th the genes (rbcL and rbcS) encoding form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
41 d cbbZ were found downstream from the form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
42 in WH7803 chromosomal DNA digests, using the ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
43 s denitrificans, encoding form I and form II ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
44 ep in the carboxylation pathway catalyzed by ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
45 oving the Calvin-Benson-Bassham cycle enzyme Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
48 enhanced by the PRK/Rubisco shunt, in which ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
53 cy of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
54 ation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
56 e multiple copies of the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
59 increased productivity by overexpression of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
62 a proteinaceous outer shell and filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO
64 thotrophic bacteria, the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
65 that form a shell to encapsulate the enzymes ribulose 1,5-bisphosphate carboxylase/oxygenase and carb
66 -balancing systems was further manifested in ribulose 1,5-bisphosphate carboxylase/oxygenase and phos
67 solate contains both the denitrification and ribulose 1,5-bisphosphate carboxylase/oxygenase gene clu
68 nces of the P. vulgaris rbcS2 gene, encoding ribulose 1,5-bisphosphate carboxylase/oxygenase small su
72 ve sites of the CO(2)-fixing enzyme Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) to rele
73 idative decarboxylase, class II aldolase, or ribulose 1,5-bisphosphate carboxylase/oxygenase, large s
74 oding the large and small subunits of form I ribulose 1,5-bisphosphate carboxylase/oxygenase, or Rubi
77 enna proteins (LHCA1, LHCB1, and LHCB4), the ribulose 1.5-bisphosphate carboxylase subunits (rbcL and
78 e abundant cytosolic bicarbonate and provide ribulose 1.5-bisphosphate carboxylase/oxygenase (RubisCO
79 nce of the precursor to the small subunit of ribulose-1, 5-bisphosphate carboxylase (pS) in a precurs
80 tid rbcL gene, encoding the large subunit of ribulose-1, 5-bisphosphate carboxylase, in higher plants
81 in the chloroplast-encoded large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (EC 4.1
82 (L290F) substitution in the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisc
84 bcL gene that codes for the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase, the ke
85 The recovery of nearly 100 genes encoding ribulose-1,5 bisphosphate carboxylase-oxygenase subunit
86 ructures of the plant SET domain enzyme, pea ribulose-1,5 bisphosphate carboxylase/oxygenase large su
87 tion of CAB1, CAB2, and the small subunit of ribulose-1,5-bisphosphate carboxylase (RBCS) promoters i
88 m the genes that encode the small subunit of ribulose-1,5-bisphosphate carboxylase (rbcS), the gene f
89 to glycine reassignment and an archaeal-type ribulose-1,5-bisphosphate carboxylase (RubisCO) involved
90 e enzyme responsible for C3 carbon fixation, ribulose-1,5-bisphosphate carboxylase (Rubisco), however
91 n case of evolutionary adaptation is that of ribulose-1,5-bisphosphate carboxylase (RubisCO), the enz
92 levels relevant to the (1)(3)C flux studies, ribulose-1,5-bisphosphate carboxylase activity is predic
94 /b-binding protein (cab) or small subunit of ribulose-1,5-bisphosphate carboxylase oxygenase (rbcS).
95 ctron transport rate (J), or deactivation of Ribulose-1,5-bisphosphate Carboxylase Oxygenase (Rubisco
96 lleviates the problem of reduced affinity of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO
98 ding those involved in photosynthesis (e.g., ribulose-1,5-bisphosphate carboxylase oxygenase genes rb
99 tid rbcL gene (encoding the large subunit of ribulose-1,5-bisphosphate carboxylase) is regulated post
100 ng mechanism (CCM; concentrates CO(2) around ribulose-1,5-bisphosphate carboxylase, the Calvin-Benson
101 f leaf nitrogen in the photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO
103 carbamylation reaction in the active site of ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO
104 tation with archaeal-like hybrid type II/III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO
105 illales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulf
106 ts to metabolize toxic glycolate formed when ribulose-1,5-bisphosphate carboxylase-oxygenase oxygenat
110 glyceraldehyde-3-phosphate dehydrogenase or ribulose-1,5-bisphosphate carboxylase/oxygenase (compari
111 it (S) increases the catalytic efficiency of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.
112 e (CA), pyruvate, phosphate dikinase (PPDK), ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
113 Archaeoglobus fulgidus RbcL2, a form III ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
114 ription activator gene, cbbR, and the form I ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
116 in of activase is involved in recognition of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
117 nd 6 in the alpha/beta-barrel active site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
120 biological selection of randomly mutagenized ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
121 ensional structure and active-site residues, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
124 ing a product with substantial similarity to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
126 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
131 f nonstructural carbohydrates and changes in ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
132 loroplast gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
133 s been shown previously to express a form II ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
134 3A, encoding a small subunit protein (S) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
135 es not markedly facilitate the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
136 ynthesis and growth to maturity of antisense ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
137 mining the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
138 on of the Arabidopsis thaliana gene encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
140 bacco Rubisco activase in ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
141 n dioxide (CO(2)) assimilation by the enzyme Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco
143 ncy of the environmentally relevant protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
144 embraneless organelles containing the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
145 ophic organisms fix inorganic carbon (Ci) by RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO
149 hate, the carbon-fixing co-substrate used by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
151 ains 74.1% protein and is mainly composed of Ribulose-1,5-BISphosphate Carboxylase/Oxygenase (RuBisCO
152 ytic inefficiencies of the CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
153 y focused on enhancing the CO2 fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
154 ts and concentrates the carbon-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
155 capsulated the two key carboxysomal enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
156 Carboxysomes compartmentalize the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
157 raising the CO2 concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
159 hat enhance carbon fixation by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
164 ivated transition-state analog-bound form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
165 important enzymes, and immunolocalization of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
166 ich algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
167 ining the CO(2) concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
168 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
169 s), which sequester the CO(2)-fixing enzymes ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
170 sensitive green fluorescent protein (GFP) to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
171 ADP sensitivity for both ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
173 ria and some chemoautotrophs by sequestering ribulose-1,5-bisphosphate carboxylase/oxygenase and carb
174 al domains of the TP of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and its
175 ost efficient answer to the dual activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the
176 for interaction with CcmM and, by extension, ribulose-1,5-bisphosphate carboxylase/oxygenase and the
177 s into the conservation of Mg(2+) within the ribulose-1,5-bisphosphate carboxylase/oxygenase family o
180 containing the rbcL gene for cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase produced
182 io calculations of an active-site mimic of D-ribulose-1,5-bisphosphate carboxylase/oxygenase suggest
183 precursors of Toc75 and the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase to intac
184 s condense the primary carboxylase, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) as part
187 ction center protein D1), and "Form I" rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) genes f
188 I-TOF-TOF confirmed the presence of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) in all
189 in which the shell and the internal RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) lattice
190 ubunits of the carbon-fixing enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), a majo
192 l changes, such as the reduced expression of ribulose-1,5-bisphosphate carboxylase/oxygenase, indicat
193 entuates the feedback and down-regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase, resulti
194 rbcS-1A, which encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, was not
195 -light conditions, major contribution of the ribulose-1,5-bisphosphate carboxylase/oxygenase-bypass t
199 resistance of atmospheric CO(2) to sites of ribulose 1,5-bisphosphate carboxylation inside bundle sh
200 An were used to model maximal rates of RuBP (ribulose-1,5-bisphosphate) carboxylation (Vcmax ) and el
201 3-phosphoglyceric acid content and increased ribulose-1, 5-bisphosphate content, which is indicative
204 bisco (Vc,max 117 mumol CO2 m(-2) s(-1)) and ribulose-1:5-bisphosphate limited carboxylation rate (Jm
206 external Ci and their modulation of internal ribulose-1,5-bisphosphate, phosphoglycerate, and Ci pool
207 ers the allocation of photosynthates between ribulose 1,5-bisphosphate regeneration and starch synthe
208 postulate, the turnover of 1-(3)H-labeled D-ribulose 1,5-bisphosphate (RuBP) by impaired position-16
209 uncovered the presence of genes that encode ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (
211 eased NADPH : NADP ratio, as well as malate, ribulose 1,5-bisphosphate (RuBP), fructose 1,6-bisphosph
213 atalyzes the addition of CO(2) onto enolized ribulose 1,5-bisphosphate (RuBP), producing 3-phosphogly
215 ed by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phospha
216 bisco isoform that functions to scavenge the ribulose-1,5-bisphosphate (RuBP) by-product of purine/py
217 is) contains the cbbLS genes encoding form I ribulose-1,5-bisphosphate (RuBP) carboxylase oxygenase (
218 pable of using CO2 as sole source of carbon, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (
220 to reach BS to generate enough ATP to allow ribulose-1,5-bisphosphate (RuBP) regeneration in BS.
223 s in this cycle catalyse the regeneration of ribulose-1-5 bisphosphate (RuBP), the CO(2) acceptor mol
224 y abstraction of the proton from C3 of the d-ribulose 1,5-bisphosphate substrate by a carbamate oxyge
225 conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate, the substrate for the CO2 fix
226 the CBBC, contributes to the regeneration of ribulose-1,5-bisphosphate, the carbon-fixing co-substrat
227 o 3 times more xylulose-1,5-bisphosphate per ribulose-1,5-bisphosphate utilized than wild-type or F92
228 d the lack of fallover and the inhibition by ribulose 1,5-bisphosphate were similar to those of form