Catalogo dei prodotti della ricerca

SALVI, Giovanni
 Distribuzione geografica
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Continente #
NA - Nord America 2.111
EU - Europa 722
AS - Asia 338
SA - Sud America 34
AF - Africa 3
Continente sconosciuto - Info sul continente non disponibili 1
Totale 3.209
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Nazione #
US - Stati Uniti d'America 2.082
DE - Germania 165
IN - India 143
SE - Svezia 124
CN - Cina 123
IT - Italia 115
UA - Ucraina 101
FI - Finlandia 92
SG - Singapore 65
BG - Bulgaria 36
IE - Irlanda 32
AR - Argentina 31
GB - Regno Unito 27
CA - Canada 26
FR - Francia 8
BE - Belgio 7
RO - Romania 7
TR - Turchia 4
MX - Messico 3
NL - Olanda 3
CL - Cile 2
KR - Corea 2
ZA - Sudafrica 2
BR - Brasile 1
CH - Svizzera 1
DK - Danimarca 1
EG - Egitto 1
ES - Italia 1
EU - Europa 1
LU - Lussemburgo 1
PL - Polonia 1
SA - Arabia Saudita 1
Totale 3.209
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Città #
Fairfield 294
Chandler 231
Ashburn 154
Woodbridge 130
Ann Arbor 119
Houston 109
Cambridge 103
Beijing 94
Wilmington 92
Seattle 83
Plano 77
Princeton 77
Grafing 61
Boston 51
Bremen 50
Rome 40
Jacksonville 38
Dearborn 37
Sofia 36
Dublin 32
Boardman 31
Federal 31
San Diego 30
Millbury 25
Lawrence 20
San Paolo di Civitate 16
Helsinki 15
Ottawa 15
Norwalk 14
Andover 13
Singapore 12
Bühl 11
Toronto 10
Fremont 9
New York 8
Brussels 7
Falls Church 7
Hefei 6
Moncalieri 6
Auburn Hills 5
Mazzano Romano 5
Des Moines 4
Guangzhou 4
London 4
Nanjing 4
Pune 4
San Mateo 4
Horia 3
Istanbul 3
Los Angeles 3
Mexico City 3
Milan 3
San Francisco 3
Washington 3
Albano Laziale 2
Buffalo 2
Cassino 2
Fabriano 2
Kunming 2
Laurel 2
Provo 2
Redmond 2
Redwood City 2
Seoul 2
Silverton 2
Torino 2
Turin 2
Bagno di Romagna 1
Baotou 1
Bern 1
Bonn 1
Cairo 1
Chengdu 1
Chiswick 1
Chongqing 1
Copenhagen 1
Frankfurt am Main 1
Fuzhou 1
Giugliano in Campania 1
Hauteville-lompnes 1
Hebei 1
Hounslow 1
Indiana 1
Luxembourg 1
Madrid 1
Mcallen 1
Montréal 1
Naaldwijk 1
Omegna 1
Pasian Di Prato 1
Phoenix 1
Portland 1
Preturo 1
Quzhou 1
Shenyang 1
University Center 1
Vanves 1
Warsaw 1
Xian 1
Zhengzhou 1
Totale 2.308
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Nome #
Controlled expression of pectic enzymes in Arabidopsis thaliana enhances biomass conversion without adverse effects on growth 84
Polygalacturonase-inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection. 81
Studi strutturali e molecolari dell'interazione fra poligalatturonasi fungine e PGIP.11° Incontro su "Aspetti Molecolari e fisiologici delle interazioni pianta-patogeno" 77
Pectin Methylesterase Is Induced in Arabidopsis upon Infection and Is Necessary for a Successful Colonization by Necrotrophic Pathogens 76
Extracellular H2O2 induced by oligogalacturonides is not involved in the inhibition of the auxin-regulated rolB gene expression in tobacco leaf explants 76
EFFECTS OF OLIGOGALACTURONIDES ON TOBACCO LEAF EXPLANTS CULTURED ON ROOT-INDUCING MEDIUM 72
Analysis of the interaction between PGIP from Phaseolus vulgaris L. and fungal endopolygalacturonases using biosensor technology 70
Molecular signalling and recognition in plant defense mechanisms 68
Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase-inhibiting proteins. 68
Cloning and characterization of the gene encoding the endopolygalacturonase of Fusarium moniliforme 67
Accumulation of PGIP, a leucine-rich receptor-like protein, correlates with the hypersensitive response in race-cultivar interactions 67
Sensitive detection and measurement of oligogalacturonides in Arabidopsis 66
A polygalacturonase-inhibiting protein in the flowers of Phaseolus vulgaris L. 64
Oligogalacturonides inhibit the formation of roots on tobacco explants 63
Oligogalacturonides stimulate pericycle cell wall thickening and cell divisions leading to stoma formation in tobacco leaf explants 62
Oligogalacturonides prevent rhizogenesis in rolB-transformed tobacco explants by inhibiting auxin-induced expression of the rolB gene 62
The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense 61
A polygalacturonase-inhibiting protein from alfalfa callus cultures 60
Expression of endopolygalacturonase and other fungal genes induced by pectin 58
Fusarium moniliforme secretes four endopolygalacturonases derived from a single gene product 58
Polygalacturonase, PGIP and oligogalacturonides in cell-cell communication 57
The interaction between fungal endopolygalacturonase and plant cell wall PGIP (Polygalacturonase-Inhibiting Protein) 57
Comparison of immunological reactivity of polygalacturonases from different fungi 56
Release of phytoalexin elicitor-active oligogalacturonides by microbial pectic enzymes 54
The role of polygalacturonase, PGIP and pectin oligomers in fungal infection 54
Un gene per difendere le piante dai funghi fitopatogeni 51
Molecular evolution of fungal polygalacturonase 51
Induction of extracellular polygalacturonase and its mRNA in the phytopathogenic fungus Fusarium moniliforme 51
PGIPs: LRR cell wall proteins involved in defense and development 50
Site-directed mutagenesis of endopolygalacturonase from Fusarium moniliforme: hystidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP) 49
Three aspartic acid residues of polygalacturonase inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG 49
Elicitation of necrosis in Vigna unguiculata Walp. by homogeneous Aspergillus niger endo-polygalacturonase and by α-D-galacturonate oligomers 46
Cloning and characterization of the gene encoding the endopolygalacturonase-inhibiting protein (PGIP) of Phaseolus vulgaris L. 45
Interaction of fungal polygalacturonase with plant proteins in relation to specificity and regulation of plant defense response 44
Dissection of oligogalaturonide-mediated signalling: role in defence and development 44
Elicitation of phenylalanine ammonia lyase in Daucus carota L. by oligogalacturonides released from sodium polipectate by homogeneous polygalacturonase 41
Structure-function and molecular studies on fungal polygalacturonases and their inhibitors PGIPs 40
Uso di piante con un ridotti livelli di omogalatturonano de-esterificato nella parete cellulare o parti di esse per migliorare la saccarificazione di biomasse vegetali 38
The non-traditional growth regulator pectimorf is an elicitor of defense responses and protects Arabidopsis against Botrytis cinerea 38
Polygalacturonase-inhibiting protein accumulates in Phaseolus vulgaris L. in response to wounding, elicitors and fungal infection 35
Use of plants with reduced levels of de-esterified homogalacturonan in the cell wall or portions thereof for improving the saccharification of plant biomasses 34
Structural requirements for the interaction between fungal endoPG and their plant inhibitors (PGIPs) 33
ARTIFICIAL EVOLUTION CORRECTS A REPULSIVE AMINO ACID IN POLYGALACTURONASE INHIBITING PROTEINS (PGIPs) 33
Cytological localization of the pgip genes in the embryo suspensor cells of Phaseolus vulgaris L. 32
PGIPs: LRR cell wall proteins involved in defence and development". 32
The expression of a Phaseolus vulgaris PGIP in tobacco plants limits Botrytis cinerea colonization 32
CONTROL OF POLYGALACTURONASE ACTIVITY BY PGIP RESTRICTS FUNGAL INVASION 31
Use of plants with reduced levels of de-esterified homogalacturonan in the cell wall or portions thereof for improving the saccharification of plant biomasses 31
Studies on plant inhibitors of pectin modifying enzymes: Polygalacturonase -inhibiting protein (PGIP) and Pectin methylesterase inhibitor (PMEI). 31
Molecular analysis of the polygalacturonase inhibiting protein (PGIP) gene family in Phaseolus vulgaris 31
Control of polygalacturonase activity by PGIP restricts fungal invasion. 31
Analysis of the structural requirements for the interaction between fungal endoPGs and their plant inhibitors (PGIPs) to design novel recognition specifity 30
structural requirements for the interaction between fungal endoPGs and their plant inhibitors (PGIPs) to design novel recognition specifity 30
IN VITRO EVOLUTION HIGHLIGHTS THE RESIDUE 224 OF PGIPs AS A PRIMARY SPOT OF VARIABILITY FOR IMPROVEMENT OF INHIBITION CAPABILITY” 30
Control of polygalacturonase activity by PGIP restricts fungal invasion. 30
Expression of PGIP and Polygalacturonase in plants influences growth and development 30
Structural and molecular studies on the cell wall protein PGIPs. 30
Purification and characterization of a polygalaturonase-inhibiting protein from phaseolus vulgaris L. 29
Un’ ipotesi di sistema immunitario nelle piante 29
Phytoalexin elicitor-active alpha-1,4-D-oligogalacturonides reduce auxin perception by plant cells and tissues 28
Extracellular accumulation of an auxin-regulated protein in Phaseolus vulgaris L. cell is inhibited by oligogalacturonides 26
Molecular signalling in plant defense mechanisms 26
The PGIP (Polygalacturonase-inhibiting protein) family: extracellular proteins specialized for recognition 26
Use of plants with reduced levels of de-esterified homogalacturonan in the cell wall or portion thereof for improving the saccharification of plant biomasses 25
Modification of plant extracellular matrix by targeting pectins 25
Structure-function studies on the leucine-rich repeat polygalacturonase-inhibiting protein (PGIP). 24
Polygalacturonase-inhibiting proteins with different specificities are expressed in Phaseolus vulgaris 24
THE EXPRESSION OF A PHASEOLUS VULGARIS PGIP IN TOBACCO PLANTS LIMITS BOTRYTIS CINEREA COLONIZATION 24
The expression of bean PGIP in tobacco limits fungal colonization 23
Structure -function and molecular studies on fungal polygalacturonase and their inhibitors. 23
Plant LRR proteins: Role in development and defense 23
Mutagenesis of endopolygalacturonase from Fusarium moniliforme: histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP). 20
Transgenic tabacco plants expressing P. vulgaris PGIP are less susceptible to Botrytis cinerea colonization. 17
Molecular analysis of PGIP gene family in Phaseolus vulgaris 17
Transgenic plants expressing P.vulgaris PGIP are less susceptible to Botrytis cinerea colonization 17
The interaction of Botrytis cinerea polygalcturonase (PG1) with PGIPs from different plants 16
Polygalacturonase-Inhibiting Proteins (PGIPs) with different specificities are expressed in Phaseolus vulgaris L. 13
Totale 3.296
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Categoria #
all - tutte 8.315
article - articoli 0
book - libri 0
conference - conferenze 0
curatela - curatele 0
other - altro 0
patent - brevetti 326
selected - selezionate 0
volume - volumi 0
Totale 8.641
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Totale Lug Ago Sett Ott Nov Dic Gen Feb Mar Apr Mag Giu
2018/2019210 0 0 0 0 0 0 0 0 0 0 128 82
2019/2020664 109 18 4 27 58 81 87 75 61 78 55 11
2020/2021263 39 20 6 15 7 19 9 16 76 37 16 3
2021/2022746 7 47 83 15 94 7 15 71 61 66 123 157
2022/2023735 131 72 26 141 101 92 2 60 50 22 30 8
2023/2024300 18 55 11 21 49 62 4 26 0 42 12 0
Totale 3.296