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1 ntaining arabinofuranosidase, cellulase, and polygalacturonase.
2 otyls, which overexpresses a gene encoding a polygalacturonase.
3 se beetles whose symbionts solely supplement polygalacturonase.
4 izing the activity of pathogen secreted endo-polygalacturonases.
5 ere produced by fungal pectin lyases, not by polygalacturonases.
6 ylem of the gene ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 1 (ADPG1), which is normally expressed
7                                          The polygalacturonase 11 promoters (GmPG11a/b) include the S
8                       We found that LAX3 and polygalacturonase, a LAX3-induced cell wall-modifying en
9 on, highlighted by the universal presence of polygalacturonase, a primary pectinase targeting nature'
10 putative target RNAs of AtC3H14, including a polygalacturonase, a well-known cell wall modifying gene
11 enzymes at the onset of symbiosis, including polygalacturonase-a pectinase that is universally shared
12 hted unigenes involved in oxidoreductase and polygalacturonase activities.
13  wall, and PGX2(AT) plants show higher total polygalacturonase activity and smaller pectin molecular
14 sed, truncated version of PGX2 also displays polygalacturonase activity in vitro.
15                                              Polygalacturonase activity was quantified indirectly by
16 or lacking PGX1 display alterations in total polygalacturonase activity, pectin molecular mass, and w
17 erologously expressed PGX1 displays in vitro polygalacturonase activity, supporting a function for th
18 ccharomyces cerevisiae) and found to exhibit polygalacturonase activity.
19 ion allele showed a significant reduction in polygalacturonase activity.
20 r, the extent to which pectin degradation by polygalacturonases affects stem development and secondar
21            In addition, the peak activity of polygalacturonase and antioxidant activity was observed
22 n, and activities of pectin methyl esterase, polygalacturonase and cellulase enzymes.
23 oftening enzymes like pectin methylesterase, polygalacturonase and cellulase.
24             This is the first structure of a polygalacturonase and comprises a 10 turn right-handed p
25 roperties of the substrate-binding clefts of polygalacturonase and pectate lyase, which bind and clea
26 's degradation by the combined activities of polygalacturonase and pectate lyase.
27 ta-galactosidase, alpha-arabinofuranosidase, polygalacturonase and pectin methylesterase, were measur
28 nolytic enzymes pectate lyase, pectin lyase, polygalacturonase and rhamnogalacturonase, and unlike th
29 ronide fragments produced by wound-inducible polygalacturonase and that the resulting H(2)O(2) acts a
30  by specific biochemical function, with endo-polygalacturonases and endo-rhamnogalacturonases forming
31 ed genes induced by B. cinerea are LePG (for polygalacturonase) and LeExp1 (for expansin), which enco
32                   Group 11 pollen allergens, polygalacturonase, and actin depolymerizing factor were
33 basal levels of extracellular pectate lyase, polygalacturonase, and cellulase as well as those of tra
34  polymer was resistant to proteinase K, endo-polygalacturonase, and endo-xylanase III (GH11 family) b
35 he effect of pulsed light on the activity of polygalacturonase, and on the structure of the enzyme by
36 ce factors such as zinc metalloproteases and polygalacturonase are known to be secreted by the T2SS.
37 stinct, apparently ancient clades, while exo-polygalacturonases are more widely distributed.
38                      Using the promoter of a polygalacturonase (At2g41850), active primarily in cells
39          RNA gel blot analysis of cellulase, polygalacturonase beta-subunit, 1,3-beta-glucanase, and
40 s defense proteins by inhibiting fungal endo-polygalacturonases, but enzyme assays with extracts of A
41     It is suggested that the inactivation of polygalacturonase by pulsed light is an all-or-none proc
42 t produces very low levels of pectate lyase, polygalacturonase, cellulase, protease, and E. carotovor
43 tomatal movement and greatly altered PME and polygalacturonase (EC 3.2.1.15) activity, resulting in a
44 ith two forms of pectin lyase (EC 4.2.2.10), polygalacturonase (EC 3.2.1.15), or all combinations.
45     Although non-symbiotic cassidines encode polygalacturonase endogenously, their repertoire of plan
46  of the citrus pectin (CP) materials by endo-polygalacturonase (EPG) yielded pectins with average M(w
47 degradation by endogenous pectinases such as polygalacturonases, few of which have been functionally
48 nzymatic degradation by amyloglucosidase and polygalacturonase, followed by fractionation on DEAE-cel
49  and AtPGIP2 encode functional inhibitors of polygalacturonase from Botrytis, and their overexpressio
50     The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovor
51 nd glyoxyl groups and evaluated to stabilize polygalacturonase from Streptomyces halstedii ATCC 10897
52 where the promoter of an abscission-specific polygalacturonase gene (At2g41850/ARABIDOPSIS DEHISCENCE
53 , we describe mutations in the predicted exo-polygalacturonase gene NIMNA (NMA) that lead to cell elo
54 ato (Lycopersicon esculentum cv Ailsa Craig) polygalacturonase genes TAPG1 (LYCes;Pga1;2) and TAPG4 (
55 ther the expression of the Aspergillus niger polygalacturonase II (AnPGII; 35S:AnPGII plants) or a mu
56 owed that pulsed light is able to inactivate polygalacturonase in buffer, with >90% reduction of enzy
57           These results reveal new roles for polygalacturonases in plant development.
58 cyanins and flavanols in Nebbiolo, for which polygalacturonase, individually or in multi-enzyme blend
59  interacting with host PGIPs to negate their polygalacturonase-inhibiting function via enhanced disso
60 al PG was fused with a gene encoding a plant polygalacturonase-inhibiting protein (PGIP) and expresse
61                              A cDNA encoding polygalacturonase-inhibiting protein (PGIP) from mature
62                                              Polygalacturonase-inhibiting proteins (PGIPs) are plant
63                   Plant cell wall-associated polygalacturonase-inhibiting proteins (PGIPs) are widely
64  to study the interactions of EPG-II and the polygalacturonase inhibitor protein (PGIP).
65 teins that are composed of LRRs, such as the polygalacturonase inhibitor proteins (PGIP) of plants.
66 rot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucin
67  defense genes, lipoxygenase, catalase 3 and polygalacturonase-inhibitor protein.
68                           We named this gene POLYGALACTURONASE INVOLVED IN EXPANSION1 (PGX1).
69                   We designated this gene as POLYGALACTURONASE INVOLVED IN EXPANSION2 (PGX2), and the
70                             We characterized POLYGALACTURONASE INVOLVED IN EXPANSION3 (PGX3), which i
71 nservation indicates that the active site of polygalacturonase is between these two loop regions, and
72 al structures of 2 Arabidopsis thaliana PGs, POLYGALACTURONASE LATERAL ROOT (PGLR), and ARABIDOPSIS D
73 assessed in transgenic fruit with suppressed polygalacturonase (LePG) and expansin (LeExp1) expressio
74  there was at least a 1000-fold reduction in polygalacturonase levels in those plants bearing Ds inse
75 om strawberry fruits were digested with endo-polygalacturonase M2 from Aspergillus aculeatus and visu
76 uded HecA hemagglutinin family adhesion, Peh polygalacturonase, new effector HopPtoC(EA), and membran
77 creased synthesis and export of enzymes like polygalacturonase, pectin esterase, and other enzymes im
78 by their degradability by the pectic enzymes polygalacturonase, pectinmethylesterase and rhamnogalact
79 tate lyase isozymes (Pels), cellulase (Cel), polygalacturonase (Peh) and protease (Prt).
80  produces extracellular pectate lyase (Pel), polygalacturonase (Peh), cellulase (Cel), and protease (
81  extracellular enzymes (pectate lyase [Pel], polygalacturonase [Peh], cellulase [Cel], and protease [
82              Pectin methylesterase (PME) and polygalacturonase (PG) activities were higher in A-treat
83 en-derived pectin-degrading enzymes, because polygalacturonase (PG) activity has not been reported in
84             Transgenic experiments show that polygalacturonase (PG) activity is largely responsible f
85                                   In tomato, polygalacturonase (PG) and expansin (Exp) are among the
86 ansformed with a tomato leaf wound-inducible polygalacturonase (PG) beta-subunit gene in the antisens
87 loning of a tomato (Lycopersicon esculentum) polygalacturonase (PG) cDNA, TAPG1, expressed during lea
88  Moreover, IDL6 promotes the expression of a polygalacturonase (PG) gene, ADPG2, and increases PG act
89 ying enzymes pectin-methylesterase (PME) and polygalacturonase (PG) in tomato fruit was tailored by p
90  pectins by tomato (Lycopersicon esculentum) polygalacturonase (PG) in vitro is more extensive than t
91                                              Polygalacturonase (PG) is the major enzyme responsible f
92 responds with an increase in wound-inducible polygalacturonase (PG) mRNA and enzyme activity previous
93 -transcriptional silencing of the endogenous polygalacturonase (PG) sense gene and a truncated homolo
94                                              Polygalacturonase (PG) showed better association with ce
95  transformants harboring a stably integrated polygalacturonase (PG) transgene driven by a constitutiv
96  pectate lyase (PL), pectinesterase (PE) and polygalacturonase (PG)), enzymes involved in fruit color
97 al knockout mutations in the gene for tomato polygalacturonase (PG), a critical enzyme in fruit ripen
98  The PSL1 gene encodes a cell wall-localised polygalacturonase (PG), a pectin-degrading enzyme.
99 Here, cypress pollen allergens, especially a polygalacturonase (PG), were further characterized using
100  the key candidate gene AG1IA_04727 encoding polygalacturonase (PG), which was observed to be signifi
101 ruit have been attributed to the activity of polygalacturonase (PG).
102                                              Polygalacturonases (PGs) are a major group of pectin-hyd
103 pathogens degrade cell wall through secreted polygalacturonases (PGs) during infection.
104                                              Polygalacturonases (PGs) fine-tune pectins to modulate c
105 r cell wall disassembly processes in plants, polygalacturonases (PGs) may be involved.
106 ce of horizontally acquired pectin-digesting polygalacturonases (PGs) of the leaf beetle Phaedon coch
107 ainst phytopathogens by inhibiting microbial polygalacturonases (PGs).
108 ta by partial inhibition of pathogen-encoded polygalacturonases (PGs).
109                                              Polygalacturonase products did not accumulate as larger
110 r the control of the fruit ripening-specific polygalacturonase promoter to divert the metabolic flux
111 ol3 transposon is also present in the tomato polygalacturonase promoter to which it conferred regulat
112 anded RNA, the polymer xanthan, and enzymes (polygalacturonase, protease, cellulase).
113 1g33430, 4-coumarate-coenzyme A ligase 4CL3, polygalacturonase QUARTET3, novel gene At5g58100, and nu
114 oduce ethylene, and have increased levels of polygalacturonase RNA.
115 s involved in pectin metabolism, including a polygalacturonase (SgPG1).
116 on, we identified a gene encoding a putative polygalacturonase that, when overexpressed, resulted in
117                                              Polygalacturonase was activated at 130 MPa, inactivated
118 alysis showed that the tertiary structure of polygalacturonase was changed.
119 -glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions
120 s) are plant proteins that counteract fungal polygalacturonases, which are important virulence factor
121  regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A fro
122   Enzymatic digestion of PD with 1,4-alpha-d-polygalacturonase yielded the fraction PD-E.

 
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