User:John Samuelson - Revision history

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2021-12-18T21:35:13Z

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

Elizabeth Ficko-Blean at 07:27, 25 October 2019

2019-10-25T07:27:13Z

Elizabeth Ficko-Blean at 08:17, 24 October 2019

2019-10-24T08:17:33Z

Elizabeth Ficko-Blean at 08:15, 24 October 2019

2019-10-24T08:15:35Z

Elizabeth Ficko-Blean at 08:13, 24 October 2019

2019-10-24T08:13:24Z

Elizabeth Ficko-Blean at 08:09, 24 October 2019

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2019-10-24T08:00:15Z

Harry Brumer: Created page with "right '''This is an empty template to help you get started with composing your User page.''' You should begin by opening this page for ed..."

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<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Samuelson,John]]

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-John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with ^^^Breeanna Urbanowicz^^^ showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
+John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with [[User:Breeanna Urbanowicz|Breeanna Urbanowicz]] showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
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← Older revision		Revision as of 07:27, 25 October 2019
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	John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with ^^^Breeanna Urbanowicz^^^ showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.		John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with ^^^Breeanna Urbanowicz^^^ showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.

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 [[Image:Blank_user-200px.png|200px|right]]
-John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
+John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with ^^^Breeanna Urbanowicz^^^ showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
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 [[Image:Blank_user-200px.png|200px|right]]
-John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in Entamoeba histolytica, the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of Entamoeba are chitin-binding lectins and identified CBM55 at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of Giardia lamblia, cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of Toxoplasma gondii, cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the GH17 glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of Entamoeba, Giardia, and Plasmodium falciparum (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and GT41 domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of Acanthamoeba castellanii, cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
+John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of ''Entamoeba'' are chitin-binding lectins and identified [[CBM55]] at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of ''Giardia lamblia'', cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of ''Toxoplasma gondii'', cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the [[GH17]] glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of ''Entamoeba'', ''Giardia'', and ''Plasmodium falciparum'' (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of ''Toxoplasma'' that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and [[GT41]] domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of ''Acanthamoeba castellanii'', cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
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 [[Image:Blank_user-200px.png|200px|right]]
-John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in Entamoeba histolytica, the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of Entamoeba are chitin-binding lectins and identified CBM55 at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of Giardia lamblia, cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of Toxoplasma gondii, cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the GH17 glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of Entamoeba, Giardia, and Plasmodium falciparum (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose [11] and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and GT41 domains [12]. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of Acanthamoeba castellanii, cause of blindness, are cellulose- and chitin-binding lectins [13].
+John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in Entamoeba histolytica, the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of Entamoeba are chitin-binding lectins and identified CBM55 at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of Giardia lamblia, cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of Toxoplasma gondii, cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the GH17 glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of Entamoeba, Giardia, and Plasmodium falciparum (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose <cite>Bandini2016</cite> and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and GT41 domains <cite>Gas-Pascual2019</cite>. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of Acanthamoeba castellanii, cause of blindness, are cellulose- and chitin-binding lectins <cite>Magistrado-Coxen2019</cite>.
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@@ Line 17: / Line 16: @@
 #Ratner2008 pmid=18820077
 #Bushkin2010 pmid=19783771
+#Bandini2016 pmid=27663739
 </biblio>

@@ Line 2: / Line 2: @@
 '''This is an empty template to help you get started with composing your User page.'''
-John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in Entamoeba histolytica, the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of Entamoeba are chitin-binding lectins and identified CBM55 at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of Giardia lamblia, cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer [4]. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of Toxoplasma gondii, cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the GH17 glycoside hydrolase [5]. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes [6], demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen [7], and identified N-glycans of Entamoeba, Giardia, and Plasmodium falciparum (cause of malaria) [8-10]. With Giulia Bandini they discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose [11] and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and GT41 domains [12]. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of Acanthamoeba castellanii, cause of blindness, are cellulose- and chitin-binding lectins [13].
+John Samuelson received his M.D. and Ph.D. in Cell and Developmental Biology from Harvard Medical School. As a post-doctoral fellow and faculty member at the Harvard School of Public Health, he discovered extensive horizontal gene transfer from bacteria and a cryptic mitochondrion-derived organelle in Entamoeba histolytica, the protist that causes dysentery and liver abscess. With his move to Boston University, Dr. Samuelson got his real introduction to glycobiology in a 15 year collaboration with Phil Robbins. Together they showed the major cyst wall proteins of Entamoeba are chitin-binding lectins and identified CBM55 at the N-terminus of the chitinase <cite>Frisardi2000,VanDellen2002,Chatterjee2009 </cite>. They showed that the most abundant cyst wall proteins of Giardia lamblia, cause of diarrhea, have Leu-rich repeats that bind to fibrils of the unique β-1,3-linked GalNAc polymer <cite>Chatterjee2010</cite>. They demonstrated β-1,3-glucan in the inner layer of the oocyst wall of Toxoplasma gondii, cause of birth defects, and identified a unique glucan-binding domain at the N-terminus of the GH17 glycoside hydrolase <cite>Bushkin2012</cite>. In a separate line of experiments, Drs. Samuelson and Robbins showed that secondary loss of genes encoding Alg enzymes explains the diversity of N-glycan precursors among eukaryotes <cite>Samuelson2005</cite>, demonstrated Darwinian selection for N-glycan sites in secreted proteins of the vast majority of eukaryotes that have N-glycan-dependent quality control of glycoprotein folding in the ER lumen <cite>Cui2009</cite>, and identified N-glycans of Entamoeba, Giardia, and Plasmodium falciparum (cause of malaria) <cite>Magnelli2008,Ratner2008,Bushkin2010</cite>. With Giulia Bandini they discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose [11] and with Chris West showed that the O-fucosyltransferase is a homolog of plant Spindly, which contains TPR and GT41 domains [12]. Recently, Dr. Samuelson with Breeanna Urbanowicz showed the most abundant proteins in the cyst wall of Acanthamoeba castellanii, cause of blindness, are cellulose- and chitin-binding lectins [13].
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@@ Line 10: / Line 10: @@
 #VanDellen2002 pmid=12011021
 #Chatterjee2009 pmid=19578434
+#Chatterjee2010 pmid=20808847
 </biblio>