User:Beatrice Cobucci-Ponzano - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:34:07Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: added Contributor tag

2013-05-10T16:06:49Z

added Contributor tag

Beatrice Cobucci-Ponzano at 13:38, 18 June 2010

2010-06-18T13:38:19Z

Beatrice Cobucci-Ponzano at 14:42, 14 June 2010

2010-06-14T14:42:10Z

Beatrice Cobucci-Ponzano at 14:38, 14 June 2010

2010-06-14T14:38:35Z

Beatrice Cobucci-Ponzano at 14:19, 14 June 2010

2010-06-14T14:19:02Z

Beatrice Cobucci-Ponzano at 14:16, 14 June 2010

2010-06-14T14:16:39Z

Beatrice Cobucci-Ponzano at 14:14, 14 June 2010

2010-06-14T14:14:33Z

Beatrice Cobucci-Ponzano at 14:13, 14 June 2010

2010-06-14T14:13:59Z

Harry Brumer at 05:18, 10 June 2010

2010-06-10T05:18:28Z

@@ Line 5: / Line 5: @@
 She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of Marco Moracci at IBP.
-From 2001 she is staff scientist at IBP in the group of ^^^Marco Moracci^^^. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
+From 2001 she is staff scientist at IBP in the group of [[User:Marco Moracci|Marco Moracci]]. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
 She determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.

← Older revision		Revision as of 16:06, 10 May 2013
Line 21:		Line 21:
	#PMID20427274 pmid=20427274		#PMID20427274 pmid=20427274
	</biblio>		</biblio>
		+
		+	[[Category:Contributors\|Cobucci-Ponzano,Beatrice]]

@@ Line 7: / Line 7: @@
 From 2001 she is staff scientist at IBP in the group of ^^^Marco Moracci^^^. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
-She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.
+She determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.
 Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family [[GH116]] <cite>PMID20427274</cite>.

← Older revision		Revision as of 14:42, 14 June 2010
Line 1:		Line 1:
−		+	[[File:Cobuccifoto.jpg\|right]]
−	[[File:Cobuccifoto.jpg]]

	Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).		Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).

← Older revision		Revision as of 14:38, 14 June 2010
Line 1:		Line 1:
		+
		+	[[File:Cobuccifoto.jpg]]
		+
	Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).		Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).

← Older revision		Revision as of 14:16, 14 June 2010
Line 7:		Line 7:
	She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.		She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.

−	Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the ~~new~~ CAZy family [[GH116]] <cite>PMID20427274</cite>.	+	Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family [[GH116]] <cite>PMID20427274</cite>.

@@ Line 1: / Line 1: @@
 Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).
-She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of ^^^Marco Moracci^^^ at IBP.
+She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of Marco Moracci at IBP.
-From 2001 she is staff scientist at IBP in the group of Marco Moracci. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
+From 2001 she is staff scientist at IBP in the group of [[Marco Moracci]]. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
 She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.