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  1. AU="Pan, Jia-fu"
  2. AU="Fareed, Zeeshan"
  3. AU="Watkins, A Claire"
  4. AU="Taggart, Michael"
  5. AU="Boone, William J"

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  1. Article: Rapid synthesis of oligomannosides with orthogonally protected monosaccharides

    Chang, Sue-Ming / Jan, Hau-Ming / Lin, Chun-Hung / Pan, Jia-Fu / Tu, Zhijay

    Chemical communications. 2013 Apr. 18, v. 49, no. 39

    2013  

    Abstract: We developed a facile synthesis to yield orthogonally protected mannose building blocks with high overall yields. The protection/glycosylation steps can be carried out in a successive manner without purification of intermediate products. This developed ... ...

    Abstract We developed a facile synthesis to yield orthogonally protected mannose building blocks with high overall yields. The protection/glycosylation steps can be carried out in a successive manner without purification of intermediate products. This developed synthesis led to formation of linear/branched tri-, penta- and heptasaccharides.
    Keywords chemical communication ; chemical compounds ; glycosylation ; mannose
    Language English
    Dates of publication 2013-0418
    Size p. 4265-4267.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c2cc37099a
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: Karyomapping in preimplantation genetic testing for β-thalassemia combined with HLA matching: a systematic summary.

    Wang, Jing / Lu, Bao-Min / Li, Rong / Guo, Jing / Xu, Yan / Pan, Jia-Fu / Zeng, Yan-Hong / Zhou, Can-Quan / Xu, Yan-Wen

    Journal of assisted reproduction and genetics

    2019  Volume 36, Issue 12, Page(s) 2515–2523

    Abstract: Purpose: To investigate the validity, accuracy, and clinical outcomes of Karyomapping in preimplantation genetic testing (PGT) for β-thalassemia combined with human leukocyte antigen (HLA) matching.: Methods: A total of 128 cycles from January 2014 ... ...

    Abstract Purpose: To investigate the validity, accuracy, and clinical outcomes of Karyomapping in preimplantation genetic testing (PGT) for β-thalassemia combined with human leukocyte antigen (HLA) matching.
    Methods: A total of 128 cycles from January 2014 to December 2017 were identified, and 1205 embryos were biopsied. The case group included 88 cycles using Karyomapping for PGT-HLA, compared with 40 cycles using polymerase chain reaction-short tandem repeat (PCR-STR) as the control group.
    Results: There were significant differences in the HLA matching rate (21.34 vs. 14.37%), the matched transferable embryo rate (9.79 vs. 14.07%), the clinical pregnancy rate (65.08 vs. 41.86%), and the spontaneous miscarriage rate (2.44 vs. 22.22%) between the case and control groups. In the case group, nearly 1/3 (33.37%) of the embryos showed aneuploidy. According to the results of single nucleotide polymorphism (SNP) haplotype analysis, the recombination rates of HBB (hemoglobin subunit beta) and HLA were 11.46% and 5.61% respectively. HLA gene recombination was mostly distributed between HLA-A and HLA-B and the downstream region of HLA-DQB1. In addition, STR analysis could be considered in the case of copy-neutral loss of heterozygosity (LOH) in the region where the HLA gene is located.
    Conclusion: Karyomapping contributes to accurate selection of matched embryos, along with aneuploidy screening. However, STRs assist identification in cases of LOH in the target region.
    MeSH term(s) Adult ; Biopsy ; Embryo Transfer ; Female ; HLA-A Antigens/genetics ; HLA-B Antigens/genetics ; HLA-DQ beta-Chains/genetics ; Hemoglobin Subunits/genetics ; Humans ; Karyotyping/methods ; Loss of Heterozygosity/genetics ; Pregnancy ; Pregnancy Rate ; Preimplantation Diagnosis ; beta-Thalassemia/diagnosis ; beta-Thalassemia/genetics ; beta-Thalassemia/pathology
    Chemical Substances HLA-A Antigens ; HLA-B Antigens ; HLA-DQ beta-Chains ; HLA-DQB1 antigen ; Hemoglobin Subunits
    Language English
    Publishing date 2019-11-22
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1112577-9
    ISSN 1573-7330 ; 1058-0468
    ISSN (online) 1573-7330
    ISSN 1058-0468
    DOI 10.1007/s10815-019-01595-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Rapid synthesis of oligomannosides with orthogonally protected monosaccharides.

    Chang, Sue-Ming / Tu, Zhijay / Jan, Hau-Ming / Pan, Jia-Fu / Lin, Chun-Hung

    Chemical communications (Cambridge, England)

    2013  Volume 49, Issue 39, Page(s) 4265–4267

    Abstract: We developed a facile synthesis to yield orthogonally protected mannose building blocks with high overall yields. The protection/glycosylation steps can be carried out in a successive manner without purification of intermediate products. This developed ... ...

    Abstract We developed a facile synthesis to yield orthogonally protected mannose building blocks with high overall yields. The protection/glycosylation steps can be carried out in a successive manner without purification of intermediate products. This developed synthesis led to formation of linear/branched tri-, penta- and heptasaccharides.
    MeSH term(s) Benzoic Acid/chemistry ; Catalysis ; Glycosylation ; Hydrolysis ; Monosaccharides/chemistry ; Oligosaccharides/chemical synthesis ; Oligosaccharides/chemistry ; Pyridines/chemistry ; Sulfonic Acids/chemistry
    Chemical Substances Monosaccharides ; Oligosaccharides ; Pyridines ; Sulfonic Acids ; oligomannoside ; Benzoic Acid (8SKN0B0MIM) ; pyridine (NH9L3PP67S)
    Language English
    Publishing date 2013-05-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c2cc37099a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Stereoselective glycosylation of endo-glycals by microwave- and AlCl₃-assisted catalysis

    Lin, Hui-Chang / Pan, Jia-Fu / Chen, Yen-Bo / Lin, Zi-Ping / Lin, Chun-Hung

    Tetrahedron. 2011 Aug. 26, v. 67, no. 34

    2011  

    Abstract: α-2-Deoxyglycosides were synthesized in good to excellent yields by microwave-assisted reaction of endo-glycals with various O-nucleophiles in the presence of catalytic amount of AlCl₃. These glycosyl additions occurred with high α-stereoselectivity and ... ...

    Abstract α-2-Deoxyglycosides were synthesized in good to excellent yields by microwave-assisted reaction of endo-glycals with various O-nucleophiles in the presence of catalytic amount of AlCl₃. These glycosyl additions occurred with high α-stereoselectivity and were complete in 5–35 min in 65–93% yield.
    Keywords catalytic activity ; chemical structure ; glycosylation ; microwave treatment ; organic compounds
    Language English
    Dates of publication 2011-0826
    Size p. 6362-6368.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 204285-x
    ISSN 1464-5416 ; 0040-4020 ; 0563-2064
    ISSN (online) 1464-5416
    ISSN 0040-4020 ; 0563-2064
    DOI 10.1016/j.tet.2011.05.124
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Rapid characterization of sugar-binding specificity by in-solution proximity binding with photosensitizers

    Chang, Chuan-Fa / Pan, Jia-Fu / Lin, Chun-Nan / Wu, I. Lin / Wong, Chi-Huey / Lin, Chun-Hung

    Glycobiology. 2011 July, v. 21, no. 7

    2011  

    Abstract: Cell-surface carbohydrates are known to participate in many important physiological and pathological activities by interacting with their corresponding proteins or receptors. Although several methods have been developed for studying carbohydrate-protein ... ...

    Abstract Cell-surface carbohydrates are known to participate in many important physiological and pathological activities by interacting with their corresponding proteins or receptors. Although several methods have been developed for studying carbohydrate-protein interactions, one major problem originates from the weak bindings of carbohydrates/proteins that are often lost during repeating wash steps. Herein, we established a homogeneous solution carbohydrate array in which polyacrylamide-based glycans are used for offering a multivalent environment. The method requires no wash step and can be carried out in a high-throughput manner. We characterized the carbohydrate-binding specificities of 11 lectins and 7 antibodies, the majority of which displayed the binding patterns in consistence with previous reports. These results demonstrate that our developed solution carbohydrate array provides a useful alternative that is better than or comparable with the current available methods.
    Keywords antibodies ; carbohydrate binding ; lectins ; photosensitizing agents ; polysaccharides ; receptors
    Language English
    Dates of publication 2011-07
    Size p. 895-902.
    Document type Article
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwr021
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Rapid characterization of sugar-binding specificity by in-solution proximity binding with photosensitizers.

    Chang, Chuan-Fa / Pan, Jia-Fu / Lin, Chun-Nan / Wu, I-Lin / Wong, Chi-Huey / Lin, Chun-Hung

    Glycobiology

    2011  Volume 21, Issue 7, Page(s) 895–902

    Abstract: Cell-surface carbohydrates are known to participate in many important physiological and pathological activities by interacting with their corresponding proteins or receptors. Although several methods have been developed for studying carbohydrate-protein ... ...

    Abstract Cell-surface carbohydrates are known to participate in many important physiological and pathological activities by interacting with their corresponding proteins or receptors. Although several methods have been developed for studying carbohydrate-protein interactions, one major problem originates from the weak bindings of carbohydrates/proteins that are often lost during repeating wash steps. Herein, we established a homogeneous solution carbohydrate array in which polyacrylamide-based glycans are used for offering a multivalent environment. The method requires no wash step and can be carried out in a high-throughput manner. We characterized the carbohydrate-binding specificities of 11 lectins and 7 antibodies, the majority of which displayed the binding patterns in consistence with previous reports. These results demonstrate that our developed solution carbohydrate array provides a useful alternative that is better than or comparable with the current available methods.
    MeSH term(s) Acrylic Resins/metabolism ; Antibodies/chemistry ; Antibodies/metabolism ; Humans ; Lectins/chemistry ; Lectins/metabolism ; Microarray Analysis ; Photosensitizing Agents ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism
    Chemical Substances Acrylic Resins ; Antibodies ; Lectins ; Photosensitizing Agents ; Polysaccharides ; Proteins ; polyacrylamide (9003-05-8)
    Language English
    Publishing date 2011-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwr021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Chiral Lewis acid-catalyzed asymmetric Baylis-Hillman reactions.

    Yang, Kung-Shuo / Lee, Wei-Der / Pan, Jia-Fu / Chen, Kwunmin

    The Journal of organic chemistry

    2003  Volume 68, Issue 3, Page(s) 915–919

    Abstract: An effective chiral Lewis acid-catalyzed asymmetric Baylis-Hillman reaction is described. Good to high enantioselectivities were obtained using 3 mol % chiral catalyst. Novel camphor-derived dimerized ligands were prepared from the condensation of (+)- ... ...

    Abstract An effective chiral Lewis acid-catalyzed asymmetric Baylis-Hillman reaction is described. Good to high enantioselectivities were obtained using 3 mol % chiral catalyst. Novel camphor-derived dimerized ligands were prepared from the condensation of (+)-ketopinic acid with the corresponding diamines and hydrazine under acidic conditions. When alpha-naphthyl acrylate was used as a Michael acceptor, the reaction is complete within 20 min with high stereoselectivity and in reasonable chemical yields.
    Language English
    Publishing date 2003-02-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/jo026318m
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Structure and Mechanism of Helicobacter pylori Fucosyltransferase: A BASIS FOR LIPOPOLYSACCHARIDE VARIATION AND INHIBITOR DESIGN

    Sun, Han-Yu / Lin, Sheng-Wei / Ko, Tzu-Ping / Pan, Jia-Fu / Liu, Chia-Ling / Lin, Chun-Nan / Wang, Andrew H.-J / Lin, Chun-Hung

    Journal of biological chemistry. 2007 Mar. 30, v. 282, no. 13

    2007  

    Abstract: Helicobacter pylori α1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to ... ...

    Abstract Helicobacter pylori α1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to escape host immune surveillance. We report here three x-ray crystal structures of FucT, including the FucT·GDP-fucose and FucT·GDP complexes. The protein structure is typical of the glycosyltransferase-B family despite little sequence homology. We identified a number of catalytically important residues, including Glu-95, which serves as the general base, and Glu-249, which stabilizes the developing oxonium ion during catalysis. The residues Arg-195, Tyr-246, Glu-249, and Lys-250 serve to interact with the donor substrate, GDP-fucose. Variations in the protein and ligand conformations, as well as a possible FucT dimer, were also observed. We propose a catalytic mechanism and a model of polysaccharide binding not only to explain the observed variations in H. pylori lipopolysaccharides, but also to facilitate the development of potent inhibitors.
    Language English
    Dates of publication 2007-0330
    Size p. 9973-9982.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  9. Article: Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.

    Sun, Han-Yu / Lin, Sheng-Wei / Ko, Tzu-Ping / Pan, Jia-Fu / Liu, Chia-Ling / Lin, Chun-Nan / Wang, Andrew H-J / Lin, Chun-Hung

    The Journal of biological chemistry

    2007  Volume 282, Issue 13, Page(s) 9973–9982

    Abstract: Helicobacter pylori alpha1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to ...

    Abstract Helicobacter pylori alpha1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to escape host immune surveillance. We report here three x-ray crystal structures of FucT, including the FucT.GDP-fucose and FucT.GDP complexes. The protein structure is typical of the glycosyltransferase-B family despite little sequence homology. We identified a number of catalytically important residues, including Glu-95, which serves as the general base, and Glu-249, which stabilizes the developing oxonium ion during catalysis. The residues Arg-195, Tyr-246, Glu-249, and Lys-250 serve to interact with the donor substrate, GDP-fucose. Variations in the protein and ligand conformations, as well as a possible FucT dimer, were also observed. We propose a catalytic mechanism and a model of polysaccharide binding not only to explain the observed variations in H. pylori lipopolysaccharides, but also to facilitate the development of potent inhibitors.
    MeSH term(s) Crystallography, X-Ray ; Enzyme Inhibitors/chemical synthesis ; Fucosyltransferases/antagonists & inhibitors ; Fucosyltransferases/chemistry ; Fucosyltransferases/physiology ; Helicobacter pylori/chemistry ; Helicobacter pylori/enzymology ; Lipopolysaccharides/antagonists & inhibitors ; Lipopolysaccharides/biosynthesis ; Lipopolysaccharides/chemistry ; Protein Conformation ; Sequence Homology, Amino Acid
    Chemical Substances Enzyme Inhibitors ; Lipopolysaccharides ; Fucosyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2007-01-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M610285200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book ; Online: Study on laboratory breeding of Anopheles balabacensis balabacensis baisas / by Jia-fu Pan, Tian-rong Yu, Hong-kan Zhu

    Pan, Jia-fu / World Health Organization

    1982  

    Abstract: Documents : WHO/MAL/82.976-82.989, WHO/MAL/83.990-83.991, WHO/MAL/83.992 (WHO/VBC/83.873), WHO/MAL/83.993-83.998, WHO/MAL/83.999 (WHO/VBC/83.878), WHO/MAL/83.1000-83.1003, WHO/MAL/84.1004-84.1006, WHO/MAL/84.1007 (WHO/VBC/84.898), WHO/MAL84.1008 (WHO/VBC/ ...

    Abstract Documents : WHO/MAL/82.976-82.989, WHO/MAL/83.990-83.991, WHO/MAL/83.992 (WHO/VBC/83.873), WHO/MAL/83.993-83.998, WHO/MAL/83.999 (WHO/VBC/83.878), WHO/MAL/83.1000-83.1003, WHO/MAL/84.1004-84.1006, WHO/MAL/84.1007 (WHO/VBC/84.898), WHO/MAL84.1008 (WHO/VBC/84.899), WHO/MAL(84.1009-84.1012, WHO/MAL/84.1013 (WHO/VBC/84.905), WHO/MAL/84.1014-84.1015, WHO/MAL/84.1016 (WHO/VBC/84.908), WHO/MAL/85.1017 (WHO/VBC/85.910), WHO/MAL/85.1018-85.1021, WHO/MAL/86.1022-86.1033, WHO/MAL/87.1034-87.1036, WHO/MAL/87.1037 (WHO/VBC/87.944), WHO/MAL/87.1038-87.1040, WHO/MAL/87.1041 (WHO/VBC/87.951), WHO/MAL/87.1042, WHO/MAL/88.1043-88.1050, WHO/MAL/89.1051 (WHO/VBC/89.966), WHO/MAL/89.1052-89.1054, WHO/MAL/90.1055-90.1057, WHO/MAL/90.1058 (WHO/VBC/90.985), WHO/MAL/90.1059-90.1060, WHO/MAL/90.1061 (WHO/VBC/90.989), WHO/MAL/91.1062 (WHO/VBC/91.994), WHO/MAL/91.1063, bound in 1 vol

    Summary in French p. 3

    WHO/MAL/82.989

    3 p.
    Keywords Malaria ; Anopheles ; Laboratory techniques and procedures ; Entomology ; Parasitic Diseases and their Control ; prevention and control ; growth and development
    Language English
    Publisher Geneva : World Health Organization
    Document type Book ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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