Fucosyltransferase 3: Difference between revisions

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Template:PBB Galactoside 3(4)-L-fucosyltransferase is an enzyme that in humans is encoded by the FUT3 gene.^[1]^[2]^[3]

Template:PBB Summary

References

^ Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB (1990). "A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase". Genes Dev. 4 (8): 1288–303. doi:10.1101/gad.4.8.1288. PMID 1977660. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
^ Weston BW, Nair RP, Larsen RD, Lowe JB (1992). "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities". J Biol Chem. 267 (6): 4152–60. PMID 1740457. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
^ "Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)".

External links

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[pmid1977660-1] Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB (1990). "A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase". Genes Dev. 4 (8): 1288–303. doi:10.1101/gad.4.8.1288. PMID 1977660. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

[pmid1740457-2] Weston BW, Nair RP, Larsen RD, Lowe JB (1992). "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities". J Biol Chem. 267 (6): 4152–60. PMID 1740457. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

[entrez-3] "Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)".

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[2]

[3]

@@ Line 5: / Line 5: @@
 {{PBB_Summary
 | section_title =
-| summary_text = The [[Lewis_blood-group_system | Lewis histo-blood group system]] comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| accessdate = }}</ref>
+| summary_text = The [[Lewis_blood-group_system | Lewis histo-blood group system]] comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.<ref name="entrez" />
 }}
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 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112–22 |year= 1995 |pmid= 7650030 |doi=10.1074/jbc.270.34.20112  }}
+*{{cite journal  | author=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112–22 |year= 1995 |pmid= 7650030 |doi=10.1074/jbc.270.34.20112  }}
-*{{cite journal  | author=Reguigne-Arnould I, Couillin P, Mollicone R, ''et al.'' |title=Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19. |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 158–62 |year= 1995 |pmid= 7656588 |doi=10.1159/000134098  }}
+*{{cite journal  | author=Reguigne-Arnould I |title=Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19 |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 158–62 |year= 1995 |pmid= 7656588 |doi=10.1159/000134098  | author-separator=,  | author2=Couillin P  | author3=Mollicone R  | display-authors=3  | last4=Faur&Eacute;  | first4=S.  | last5=Fletcher  | first5=A.  | last6=Kelly  | first6=R.J.  | last7=Lowe  | first7=J.B.  | last8=Oriol  | first8=R.  }}
-*{{cite journal  | author=Nishihara S, Nakazato M, Kudo T, ''et al.'' |title=Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 1 |pages= 42–6 |year= 1993 |pmid= 7916594 |doi= 10.1006/bbrc.1993.1008 }}
+*{{cite journal  | author=Nishihara S |title=Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19 |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 1 |pages= 42–6 |year= 1993 |pmid= 7916594 |doi= 10.1006/bbrc.1993.1008  | author-separator=,  | author2=Nakazato M  | author3=Kudo T  | display-authors=3  | last4=Kimura  | first4=H.  | last5=Ando  | first5=T.  | last6=Narimatsu  | first6=H. }}
-*{{cite journal  | author=Nishihara S, Narimatsu H, Iwasaki H, ''et al.'' |title=Molecular genetic analysis of the human Lewis histo-blood group system. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29271–8 |year= 1994 |pmid= 7961897 |doi=  }}
+*{{cite journal  | author=Nishihara S |title=Molecular genetic analysis of the human Lewis histo-blood group system |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29271–8 |year= 1994 |pmid= 7961897 |doi=  | author-separator=,  | author2=Narimatsu H  | author3=Iwasaki H  | display-authors=3  | last4=Yazawa  | first4=S  | last5=Akamatsu  | first5=S  | last6=Ando  | first6=T  | last7=Seno  | first7=T  | last8=Narimatsu  | first8=I  }}
-*{{cite journal  | author=Mollicone R, Reguigne I, Kelly RJ, ''et al.'' |title=Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20987–94 |year= 1994 |pmid= 8063716 |doi=  }}
+*{{cite journal  | author=Mollicone R |title=Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20987–94 |year= 1994 |pmid= 8063716 |doi=  | author-separator=,  | author2=Reguigne I  | author3=Kelly RJ  | display-authors=3  | last4=Fletcher  | first4=A  | last5=Watt  | first5=J  | last6=Chatfield  | first6=S  | last7=Aziz  | first7=A  | last8=Cameron  | first8=HS  | last9=Weston  | first9=BW  }}
-*{{cite journal  | author=Koda Y, Kimura H, Mekada E |title=Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals. |journal=Blood |volume=82 |issue= 9 |pages= 2915–9 |year= 1993 |pmid= 8219240 |doi=  }}
+*{{cite journal  | author=Koda Y, Kimura H, Mekada E |title=Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals |journal=Blood |volume=82 |issue= 9 |pages= 2915–9 |year= 1993 |pmid= 8219240 |doi=  }}
-*{{cite journal  | author=Elmgren A, Rydberg L, Larson G |title=Genotypic heterogeneity among Lewis negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 515–20 |year= 1993 |pmid= 8240322 |doi= 10.1006/bbrc.1993.2280 }}
+*{{cite journal  | author=Elmgren A, Rydberg L, Larson G |title=Genotypic heterogeneity among Lewis negative individuals |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 515–20 |year= 1993 |pmid= 8240322 |doi= 10.1006/bbrc.1993.2280 }}
-*{{cite journal  | author=Nishihara S, Yazawa S, Iwasaki H, ''et al.'' |title=Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 624–31 |year= 1993 |pmid= 8240337 |doi= 10.1006/bbrc.1993.2295 }}
+*{{cite journal  | author=Nishihara S |title=Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 624–31 |year= 1993 |pmid= 8240337 |doi= 10.1006/bbrc.1993.2295  | author-separator=,  | author2=Yazawa S  | author3=Iwasaki H  | display-authors=3  | last4=Nakazato  | first4=M.  | last5=Kudo  | first5=T.  | last6=Ando  | first6=T.  | last7=Narimatsu  | first7=H. }}
-*{{cite journal  | author=Elmgren A, Börjeson C, Svensson L, ''et al.'' |title=DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system. |journal=Vox Sang. |volume=70 |issue= 2 |pages= 97–103 |year= 1996 |pmid= 8801770 |doi=10.1111/j.1423-0410.1996.tb01300.x  }}
+*{{cite journal  | author=Elmgren A |title=DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system |journal=Vox Sang. |volume=70 |issue= 2 |pages= 97–103 |year= 1996 |pmid= 8801770 |doi=10.1111/j.1423-0410.1996.tb01300.x  | author-separator=,  | author2=Börjeson C  | author3=Svensson L  | display-authors=3  | last4=Rydberg  | first4=Lennart  | last5=Larson  | first5=Göran  }}
-*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791  }}
+*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791  }}
-*{{cite journal  | author=Orntoft TF, Vestergaard EM, Holmes E, ''et al.'' |title=Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 32260–8 |year= 1997 |pmid= 8943285 |doi=10.1074/jbc.271.50.32260  }}
+*{{cite journal  | author=Orntoft TF |title=Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 32260–8 |year= 1997 |pmid= 8943285 |doi=10.1074/jbc.271.50.32260  | author-separator=,  | author2=Vestergaard EM  | author3=Holmes E  | display-authors=3  | last4=Jakobsen  | first4=JS  | last5=Grunnet  | first5=N  | last6=Mortensen  | first6=M  | last7=Johnson  | first7=P  | last8=Bross  | first8=P  | last9=Gregersen  | first9=N  }}
-*{{cite journal  | author=Elmgren A, Mollicone R, Costache M, ''et al.'' |title=Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 21994–8 |year= 1997 |pmid= 9268337 |doi=10.1074/jbc.272.35.21994  }}
+*{{cite journal  | author=Elmgren A |title=Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 21994–8 |year= 1997 |pmid= 9268337 |doi=10.1074/jbc.272.35.21994  | author-separator=,  | author2=Mollicone R  | author3=Costache M  | display-authors=3  | last4=Börjeson  | first4=C  | last5=Oriol  | first5=R  | last6=Harrington  | first6=J  | last7=Larson  | first7=G  }}
-*{{cite journal  | author=Pang H, Liu Y, Koda Y, ''et al.'' |title=Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa. |journal=Hum. Genet. |volume=102 |issue= 6 |pages= 675–80 |year= 1998 |pmid= 9703429 |doi=10.1007/s004390050760  }}
+*{{cite journal  | author=Pang H |title=Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa |journal=Hum. Genet. |volume=102 |issue= 6 |pages= 675–80 |year= 1998 |pmid= 9703429 |doi=10.1007/s004390050760  | author-separator=,  | author2=Liu Y  | author3=Koda Y  | display-authors=3  | last4=Soejima  | first4=Mikiko  | last5=Jia  | first5=Jingtao  | last6=Schlaphoff  | first6=Terry  | last7=Du Toit  | first7=Ernette D.  | last8=Kimura  | first8=H.  }}
-*{{cite journal  | author=Nishihara S, Hiraga T, Ikehara Y, ''et al.'' |title=Molecular behavior of mutant Lewis enzymes in vivo. |journal=Glycobiology |volume=9 |issue= 4 |pages= 373–82 |year= 1999 |pmid= 10089211 |doi=10.1093/glycob/9.4.373  }}
+*{{cite journal  | author=Nishihara S |title=Molecular behavior of mutant Lewis enzymes in vivo |journal=Glycobiology |volume=9 |issue= 4 |pages= 373–82 |year= 1999 |pmid= 10089211 |doi=10.1093/glycob/9.4.373  | author-separator=,  | author2=Hiraga T  | author3=Ikehara Y  | display-authors=3  | last4=Iwasaki  | first4=H  | last5=Kudo  | first5=T  | last6=Yazawa  | first6=S  | last7=Morozumi  | first7=K  | last8=Suda  | first8=Y  | last9=Narimatsu  | first9=H  }}
-*{{cite journal  | author=Yazawa S, Tanaka S, Nishimura T, ''et al.'' |title=Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia. |journal=Exp. Clin. Immunogenet. |volume=16 |issue= 3 |pages= 125–30 |year= 1999 |pmid= 10394050 |doi=10.1159/000019104  }}
+*{{cite journal  | author=Yazawa S |title=Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia |journal=Exp. Clin. Immunogenet. |volume=16 |issue= 3 |pages= 125–30 |year= 1999 |pmid= 10394050 |doi=10.1159/000019104  | author-separator=,  | author2=Tanaka S  | author3=Nishimura T  | display-authors=3  | last4=Miyanaga  | first4=Kazuo  | last5=Kochibe  | first5=Naohisa  }}
-*{{cite journal  | author=Holmes EH, Yen TY, Thomas S, ''et al.'' |title=Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24237–45 |year= 2000 |pmid= 10816554 |doi= 10.1074/jbc.M000888200 }}
+*{{cite journal  | author=Holmes EH |title=Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24237–45 |year= 2000 |pmid= 10816554 |doi= 10.1074/jbc.M000888200  | author-separator=,  | author2=Yen TY  | author3=Thomas S  | display-authors=3  | last4=Joshi  | first4=R  | last5=Nguyen  | first5=A  | last6=Long  | first6=T  | last7=Gallet  | first7=F  | last8=Maftah  | first8=A  | last9=Julien  | first9=R }}
-*{{cite journal  | author=Grahn A, Elmgren A, Aberg L, ''et al.'' |title=Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples. |journal=Hum. Mutat. |volume=18 |issue= 4 |pages= 358–9 |year= 2002 |pmid= 11668626 |doi= 10.1002/humu.1204 }}
+*{{cite journal  | author=Grahn A |title=Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples |journal=Hum. Mutat. |volume=18 |issue= 4 |pages= 358–9 |year= 2002 |pmid= 11668626 |doi= 10.1002/humu.1204  | author-separator=,  | author2=Elmgren A  | author3=Aberg L  | display-authors=3  | last4=Svensson  | first4=Lola  | last5=Jansson  | first5=Per-Anders  | last6=l�Nnroth  | first6=Peter  | last7=Larson  | first7=G�ran }}
-*{{cite journal  | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168–75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
+*{{cite journal  | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168–75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
 }}
 {{refend}}

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Fucosyltransferase 3: Difference between revisions

Revision as of 08:51, 25 September 2011

See also

References

Further reading

External links