Research Topics
Genomes and Genes
Species
| Daan M F van AaltenSummaryAffiliation: University of Dundee Country: UK Publications
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Detail Information
Publications
Conformational substates in different crystal forms of the photoactive yellow protein--correlation with theoretical and experimental flexibilityD M van Aalten
W M Keck Structural Biology, Cold Spring Harbor Laboratory, New York 11724, USA
Protein Sci 9:64-72. 2000..We show that these differences can be used to obtain a description of the flexibility of the protein that is consistent with the motions observed in solution...- Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolutionD M van Aalten
Biocenter Oulu, Department of Biochemistry, University of Oulu, Linnanmaa, FIN 90570 Oulu, Finland
Proc Natl Acad Sci U S A 97:5842-7. 2000..Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin... - Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding foldD M van Aalten
Wellcome Trust Biocentre, Department of Biochemistry, University of Dundee, Dow Street, Dundee DD1 5EH, UK
EMBO J 19:5167-77. 2000.... - The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadRD M van Aalten
Wellcome Trust Biocentre, Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK
EMBO J 20:2041-50. 2001..2 A in separation of the DNA recognition helices and the loss of DNA binding, revealing the molecular basis of acyl-CoA-responsive regulation... - Structural insights into the catalytic mechanism of a family 18 exo-chitinaseD M van Aalten
Wellcome Trust Biocentre, Department of Biochemistry, University of Dundee, Dundee DD1 5EH, Scotland
Proc Natl Acad Sci U S A 98:8979-84. 2001..These changes simultaneously contribute to stabilization of the reaction intermediate and alternation of the pKa of the catalytic acid during the catalytic cycle... 
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding proteinD M van Aalten
Wellcome Trust Biocentre, Department of Biochemistry University of Dundee, Scotland
J Mol Biol 309:181-92. 2001..These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site...- Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutantsDaan M F van Aalten
W M Keck Structural Biology, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA
J Biol Chem 277:6463-8. 2002.... - Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinasesFrancesco V Rao
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Chem Biol 12:65-76. 2005..The data show that it may be possible to develop specific chitinase inhibitors based on the argifin/argadin scaffolds... - Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1bHelen Attrill
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
J Biol Chem 281:32774-83. 2006.... - Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activationElton Zeqiraj
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Science 326:1707-11. 2009..The structure also reveals how mutations found in Peutz-Jeghers syndrome and in various sporadic cancers impair LKB1 function... - Human OGA binds substrates in a conserved peptide recognition grooveMarianne Schimpl
University of Dundee, Scotland, UK
Biochem J 432:1-7. 2010.... - Role of T-loop phosphorylation in PDK1 activation, stability, and substrate bindingDavid Komander
Division of Biological Chemistry and Molecular Microbiology and MRC Protein Phosphorylation Unit, MSI WTB complex, School of Life Sciences, University of Dundee, Scotland
J Biol Chem 280:18797-802. 2005..These findings reveal that the integrity of the alpha C-helix and HM-pocket in PDK1 is not regulated by T-loop phosphorylation... - Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding propertiesMarianne Schimpl
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
Biochem J 446:149-57. 2012.... - Analysis of the LKB1-STRAD-MO25 complexJerome Boudeau
MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee, DD1 5EH, Scotland
J Cell Sci 117:6365-75. 2004..Taken together, our findings reinforce the functional importance of the binding of LKB1 to STRAD, and provide a greater understanding of the mechanism by which LKB1 is regulated and activated through its interaction with STRAD and MO25... - TAK1-binding protein 1 is a pseudophosphataseSarah H Conner
MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Biochem J 399:427-34. 2006..Thus, it appears that TAB1 is a 'pseudophosphatase', possibly binding to and regulating accessibility of phosphorylated residues on substrates downstream of TAK1 or on the TAK1 complex itself... - Screening-based discovery and structural dissection of a novel family 18 chitinase inhibitorAlexander W Schuttelkopf
Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland
J Biol Chem 281:27278-85. 2006..The compound exhibits favorable chemical properties and is likely to be useful as a general scaffold for development of pan-family 18 chitinase inhibitors... - Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocketFabrizio Villa
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, DD1 5EH, Scotland
J Biol Chem 280:8180-7. 2005..Our studies provide the first molecular description of the PTPL1 catalytic domain and give new insight into the function of PTPL1... - The N-acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzymeMichael D Urbaniak
Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, The University of Dundee, Scotland, UK
J Biol Chem 280:22831-8. 2005..The characterization of GlcNAc-PI de-N-acetylase as a zinc metalloenzyme will facilitate the rational design of anti-protozoan parasite drugs... - Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphatesDavid Komander
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, Scotland, UK
EMBO J 23:3918-28. 2004.... - Molecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferaseRamon Hurtado-Guerrero
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Biochem J 426:281-92. 2010.... - Structural insights into the recognition of substrates and activators by the OSR1 kinaseFabrizio Villa
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
EMBO Rep 8:839-45. 2007..These results provide the first molecular insight into the mechanism by which the SPAK and OSR1 kinases specifically recognize their upstream activators and downstream substrates... - ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressorElton Zeqiraj
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland
PLoS Biol 7:e1000126. 2009..Thus, the function of STRADalpha is mediated through an active kinase conformation rather than kinase activity. It is possible that other pseudokinases exert their function through nucleotide binding and active conformations... - O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysisMarianne Schimpl
College of Life Sciences, University of Dundee, Dundee, UK
Nat Chem Biol 8:969-74. 2012..This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor... - Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamineDavid E Blair
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
FEBS Lett 570:13-9. 2004.... - Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysisFrancesco V Rao
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, UK
EMBO J 25:1569-78. 2006.... - The cyclic dipeptide CI-4 [cyclo-(l-Arg-d-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediateDouglas R Houston
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U K
Biochem J 368:23-7. 2002..The structure reveals that the cyclic dipeptide inhibits chitinases by structurally mimicking a reaction intermediate, and could, on the basis of its accessible chemistry, be a candidate for further optimization... - Substrate and product analogues as human O-GlcNAc transferase inhibitorsHelge C Dorfmueller
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland, UK
Amino Acids 40:781-92. 2011..While the novel analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation... - GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylationHelge C Dorfmueller
University of Dundee, Scotland, UK
Biochem J 420:221-7. 2009..Thus these compounds are potent selective tools to study the cell biology of O-GlcNAc... - The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activationMahaboobi Jaleel
MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
Biochem J 394:545-55. 2006..Taken together, these findings suggest that the UBA domains of AMPK-related kinases play an important role in regulating the conformation, activation and localization of these enzymes... - Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational changeChristine C Milburn
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Biochem J 375:531-8. 2003..Our data provides the first structural insight into the mechanism by which the interaction of PKB with PtdIns(3,4,5)P3/PtdIns(3,4)P2 induces conformational changes that could enable PKB to be activated by PDK1... - Synergy of peptide and sugar in O-GlcNAcase substrate recognitionMarianne Schimpl
Division of Cell Signalling and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Chem Biol 19:173-8. 2012..In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site... - Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidasesHelge C Dorfmueller
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD15EH, Scotland
Chem Biol 17:1250-5. 2010.... - Interactions of LY333531 and other bisindolyl maleimide inhibitors with PDK1David Komander
Division of Biological Chemistry and Molecular Microbiology, University of Dundee, Dundee DD1 5EH, Scotland
Structure 12:215-26. 2004..A combination of site-directed mutagenesis and essential dynamics analysis gives further insight into PDK1 and also PKC inhibition by these compounds, and may aid inhibitor design... 
Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferaseRamon Hurtado-Guerrero
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Biochem J 415:217-23. 2008..Mutagenesis targeting these differences revealed drastic effects on steady-state kinetics, suggesting that the differences could be exploitable with small-molecule inhibitors...- Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifinOle A Andersen
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Chem Biol 15:295-301. 2008..The data provide useful information that could lead to the generation of drug-like, natural product-based chitinase inhibitors... - Natural product-guided discovery of a fungal chitinase inhibitorChristina L Rush
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD15EH, Scotland
Chem Biol 17:1275-81. 2010..This work provides synthetically tractable plant-type family 18 chitinase inhibitors from the repurposing of a natural product... - Natural product family 18 chitinase inhibitorsOle A Andersen
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH
Nat Prod Rep 22:563-79. 2005 - Structural basis for UCN-01 (7-hydroxystaurosporine) specificity and PDK1 (3-phosphoinositide-dependent protein kinase-1) inhibitionDavid Komander
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Biochem J 375:255-62. 2003..This information could lead to opportunities for structure-based optimization of PDK1 inhibitors... - Structural insights into mechanism and specificity of O-GlcNAc transferaseAndrew J Clarke
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, UK
EMBO J 27:2780-8. 2008..On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates... - Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitorsRamon Hurtado Guerrero
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Chem Biol 14:589-99. 2007..Crystal structures of ScCTS1 in complex with inhibitors from three series reveal striking mimicry of carbohydrate substrate by small aromatic moieties and a pocket that could be further exploited in optimization of these inhibitors... - Acetazolamide-based fungal chitinase inhibitorsAlexander W Schuttelkopf
University of Dundee, Sir James Black Centre, UK
Bioorg Med Chem 18:8334-40. 2010..Although acetazolamide and its analogues are weak inhibitors of the enzyme, they have a high ligand efficiency and as such are interesting leads for future inhibitor development... - Structural and functional characterization of a putative polysaccharide deacetylase of the human parasite Encephalitozoon cuniculiJonathan E Urch
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland
Protein Sci 18:1197-209. 2009..Thus, it appears that the ECU11_0510 protein is not a carbohydrate deacetylase and may fulfill an as yet undiscovered role in the E. cuniculi parasite... - Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianumDavid E Blair
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Biochemistry 45:9416-26. 2006..The enzyme requires occupancy of at least the 0 and +1 subsites by (GlcNAc)(2) for activity and proceeds through a tetrahedral oxyanion intermediate... - Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffoldsHelge C Dorfmueller
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland, UK
FEBS Lett 584:694-700. 2010..These scaffolds provide attractive starting points for the development of non-carbohydrate, drug-like OGA inhibitors... - Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1Helge C Dorfmueller
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Acta Crystallogr D Biol Crystallogr 68:1019-29. 2012..The data unify the apparently contradictory earlier reports on the role of a cysteine in the GNA1 active site... - Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptorChristine C Milburn
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Nat Struct Mol Biol 11:193-200. 2004.... - Molecular mechanisms of yeast cell wall glucan remodelingRamon Hurtado-Guerrero
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
J Biol Chem 284:8461-9. 2009.... - Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complexRamon Hurtado Guerrero
Division of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, Scotland, UK
FEBS Lett 581:5597-600. 2007.... - Structural basis of reduction-dependent activation of human cystatin FAlexander W Schuttelkopf
Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland
J Biol Chem 281:16570-5. 2006.... - Structure-based exploration of cyclic dipeptide chitinase inhibitorsDouglas R Houston
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
J Med Chem 47:5713-20. 2004.... - Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesisSasala R Wickramasinghe
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Biochem J 393:447-57. 2006..Hexachlorophene (EC50 6.2 microM) and analogues such as bithionol also have antimalarial activity in vitro, suggesting they might be useful leads for further development... - Purification, crystallization and preliminary X-ray diffraction of a proteolytic fragment of PDK1 containing the pleckstrin homology domainDavid Komander
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
Acta Crystallogr D Biol Crystallogr 60:314-6. 2004..5 A at a synchrotron source. Diffraction data collected near the Au edge resulted in an anomalous Patterson map with a 30sigma peak... - Molecular mechanisms of O-GlcNAcylationRamon Hurtado-Guerrero
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Curr Opin Struct Biol 18:551-7. 2008.... - Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factorDavid E Blair
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, DD1 5EH Dundee, Scotland
Proc Natl Acad Sci U S A 102:15429-34. 2005..The data described here show that SpPgdA and the other family 4 carbohydrate esterases are metalloenzymes and present a step toward identification of mechanism-based inhibitors for this important class of enzymes... - Highly specific inhibition of leukaemia virus membrane fusion by interaction of peptide antagonists with a conserved region of the coiled coil of envelopeDaniel Lamb
The Biomedical Research Centre, College of Medicine, Ninewells Hospital, The University, Dundee, DD1 9SY, Scotland, UK
Retrovirology 5:70. 2008..For HTLV-1 and for several virus groups this process is sensitive to inhibition by peptides that mimic the C-terminal alpha-helical region of the trimer-of-hairpins... - Crystal structures of allosamidin derivatives in complex with human macrophage chitinaseFrancesco V Rao
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Scotland
J Biol Chem 278:20110-6. 2003..The data reported here represent a first step toward structure-based design of specific allosamidin derivatives... - An efficient synthesis of argifin: a natural product chitinase inhibitor with chemotherapeutic potentialMark J Dixon
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Bioorg Med Chem Lett 15:4717-21. 2005.... - The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor designHelen Attrill
Division of Biological Chemistry, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
Biochem J 397:271-8. 2006..A co-crystal of siglec-7 in complex with the sialoside inhibitor, oxamido-Neu5Ac [methyl alpha-9-(amino-oxalyl-amino)-9-deoxy-Neu5Ac] and inhibition data for the sialosides gives clear leads for future inhibitor design... - High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphateChristine C Thomas
Division of Biological Chemistry and Molecular Microbiology, Scotland, United Kingdom
Curr Biol 12:1256-62. 2002..The D5 phosphate faces the solvent and forms no significant interactions with any residue on the PH domain, and this explains why PKB interacts with similar affinity with both PtdIns(3,4,5)P3 and PtdIns(3,4)P2... - Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modesFrancesco V Rao
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Scotland
Chem Biol 12:973-80. 2005..Mutagenesis identified the key active site residues, conserved in mammalian chitinases, which contribute to inhibitor affinity. Enzyme assays also revealed that these methylxanthines are active against human chitinases... - Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolutionDaan M F van Aalten
W M Keck Structural Biology, Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA
Acta Crystallogr D Biol Crystallogr 58:585-90. 2002..In combination with available spectroscopic data, it is concluded that the caffeic acid chromophore binds to the protein in a strained conformation, which leads to a faster ejection from the chromophore-binding pocket upon pB formation... - GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levelsHelge C Dorfmueller
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
J Am Chem Soc 128:16484-5. 2006..This compound is able to raise O-GlcNAc levels in human HEK 293 and SH-SY5Y neuroblastoma cell lines and thus provides a novel, potent tool for the study of the role of O-GlcNAc in intracellular signal transduction pathways... - High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec familyMagnus S Alphey
Division of Cell Biology and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
J Biol Chem 278:3372-7. 2003..In the Siglec-7 structure, the ligand-binding pocket is occupied by a loop of a symmetry-related molecule, mimicking the interactions with sialic acid... - Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytesDouglas R Houston
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland
J Biol Chem 278:30206-12. 2003..Thus, HCGP39 could be a lectin that binds chitin-like oligosaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes... - Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell deathShalini Pathak
Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, Scotland
Chem Biol 15:799-807. 2008..This supports a general chemical poison mode of action for streptozotocin, suggesting the need for using more specific inhibitors to study protein O-GlcNAcylation... - Mutation of the PDK1 PH domain inhibits protein kinase B/Akt, leading to small size and insulin resistanceJose R Bayascas
MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland
Mol Cell Biol 28:3258-72. 2008..Our findings reveal how reduced activation of PKB isoforms impinges on downstream signaling pathways, causing diminution of size as well as insulin resistance...