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Select item 14152801.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 23580522.

Probe Reports from the NIH Molecular Libraries Program [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2010-.

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Select item 54829303.

Glycoscience Protocols (GlycoPODv2) [Internet].

Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors.

Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-.

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Select item 34012944.

Endotext [Internet].

Feingold KR, Anawalt B, Blackman MR, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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Select item 53216725.

Essentials of Glycobiology [Internet]. 4th edition.

Varki A, Cummings RD, Esko JD, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022.

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Select item 18813826.

Basic Neurochemistry: Molecular, Cellular and Medical Aspects. 6th edition.

Siegel GJ, Agranoff BW, Albers RW, et al., editors.

Philadelphia: Lippincott-Raven; 1999.

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Select item 44036687.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2024 Jan-.

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Select item 18602428.

WormBook: The Online Review of C. elegans Biology [Internet].

Pasadena (CA): WormBook; 2005-2018.

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Select item 15027929.

Molecular Imaging and Contrast Agent Database (MICAD) [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013.

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Select item 166869010.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 236397411.

Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis.

Arvin A, Campadelli-Fiume G, Mocarski E, et al., editors.

Cambridge: Cambridge University Press; 2007.

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Select item 168684012.

Retroviruses.

Coffin JM, Hughes SH, Varmus HE, editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Select item 290269013.

Assay Guidance Manual [Internet].

Markossian S, Grossman A, Arkin M, et al., editors.

Bethesda (MD): Eli Lilly & Company and the National Center for Advancing Translational Sciences; 2004-.

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Select item 145898414.

GeneReviews® [Internet].

Adam MP, Feldman J, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2024.

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Select item 144161815.

Helicobacter pylori: Physiology and Genetics.

Mobley HLT, Mendz GL, Hazell SL, editors.

Washington (DC): ASM Press; 2001.

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Select item 150206816.

Annual Reviews Collection [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2002 Nov.

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Select item 446506417.

Autoimmunity: From Bench to Bedside [Internet].

Anaya JM, Shoenfeld Y, Rojas-Villarraga A, et al., editors.

Bogota (Colombia): El Rosario University Press; 2013 Jul 18.

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Select item 540176818.

Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition.

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.

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Select item 307786219.

Enterococci: From Commensals to Leading Causes of Drug Resistant Infection [Internet].

Gilmore MS, Clewell DB, Ike Y, et al., editors.

Boston: Massachusetts Eye and Ear Infirmary; 2014-.

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Select item 140036220.

Hepatitis C Viruses: Genomes and Molecular Biology.

Tan SL, editor.

Norfolk (UK): Horizon Bioscience; 2006.

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FIGURE 5.2

Phylogenetic tree of the mouse DHHC protein family and summary of screening. DHHC proteins apparently have substrate specificity. Among them, DHHC-3 and DHHC-7 palmitoylate PSD-95, GAP43, G_s, and SNAP-25, suggesting that DHHC-3 and DHHC-7 show broad substrate specificity. DHHC-3 is also known as GODZ. DHHC-17 is an orthologue of yeast Akr1p and also known as Hip14 (Huntingtin-interacting protein 14).

Protein Palmitoylation by DHHC Protein Family.

Kittler JT, Moss SJ, editors. The Dynamic Synapse: Molecular Methods in Ionotropic Receptor Biology. Boca Raton (FL): CRC Press/Taylor & Francis; 2006.
Figure 1:

Substrate specificity of each FUT enzyme. Only the FUT7 enzyme can synthesize sialyl Lewis x antigen (lower). The FUT9 enzyme preferentially synthesizes (distal) Lewis x antigen at the nonreducing end, and the other FUT3–6 preferentially synthesize internal Lewis x antigen (upper).

Enzyme assay of α1,3/4-fucosyltransferase.

Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors. Glycoscience Protocols (GlycoPODv2) [Internet]. Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-.
Figure 1:

Substrate specificity of heparin lyases
The arrows indicate the glycosidic linkages cleaved by heparinase (A), heparitinase I (B), and heparitinase II (C). The hexuronate residues (marked by asterisks) are either D-glucuronic acid (GlcA) or L-iduronic acid (IdoA). C-2 NH₂ of the D-glucosamine (GlcN) and C-2 OH of the hexuronate residue should be sulfated for sensitivity to heparinase (A). C-3 OH of GlcN adjacent to the disaccharide cleavage site (marked by #) must be free for sensitivity to heparitinases I and II (B, C). Heparitinase I recognizes nonsulfated hexuronate (C-2 OH should be free as marked by #) and prefers GlcA to IdoA as a substrate (B).

Preparation of heparin/heparan sulfate oligosaccharides.

Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors. Glycoscience Protocols (GlycoPODv2) [Internet]. Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-.
FIGURE 6.1.

The strict acceptor substrate specificity of glycosyltransferases is illustrated by the human B blood group α1-3 galactosyltransferase. The B transferase adds galactose in α1-3-linkage to the H antigen (top). This enzyme requires the α1-2-linked fucose modification of the H antigen for activity because the B transferase does not add to an unmodified type-2 precursor (middle), or precursors modified by sialyl residues (bottom) or other monosaccharides (not shown). (For the monosaccharide symbol code, see Figure 1.5.)

Glycosyltransferases and Glycan-Processing Enzymes.

Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015-2017.