Robert S. Haltiwanger mostly deals with Biochemistry, Cell biology, O-Linked β-N-acetylglucosamine, Glycosylation and Notch signaling pathway. His research integrates issues of Epidermal growth factor, Peptide sequence and Chinese hamster ovary cell in his study of Cell biology. The O-Linked β-N-acetylglucosamine study combines topics in areas such as Galactosyltransferase, Uridine diphosphate N-acetylglucosamine, Cytoplasm and Tandem repeat.
His work carried out in the field of Glycosylation brings together such families of science as Drosophila melanogaster, Genome, Function, Metabolic labeling and Glycoconjugate. In general Notch signaling pathway study, his work on Notch proteins, JAG1 and Notch binding often relates to the realm of Ligand, thereby connecting several areas of interest. Robert S. Haltiwanger studied Notch proteins and EGF-like domain that intersect with Molecular biology, Mutation, Cell membrane and Regulation of gene expression.
Robert S. Haltiwanger mainly focuses on Biochemistry, Cell biology, Glycosylation, Notch signaling pathway and Fucose. His work is dedicated to discovering how Cell biology, NODAL are connected with Cripto and other disciplines. His research in Glycosylation focuses on subjects like Cytoplasm, which are connected to O-Linked β-N-acetylglucosamine, Glycoprotein, Chromatin and Phosphorylation.
His Notch signaling pathway research includes elements of Endoplasmic reticulum and EGF-like domain. As a part of the same scientific study, he usually deals with the EGF-like domain, concentrating on Molecular biology and frequently concerns with Mutation. Many of his research projects under Fucose are closely connected to LFNG with LFNG, tying the diverse disciplines of science together.
His main research concerns Cell biology, Fucose, Notch signaling pathway, EGF-like domain and Glycosylation. His Cell biology research includes themes of Receptor, Fucosylation and Secretion. His research on Fucose concerns the broader Biochemistry.
In his study, DNA Mutational Analysis is strongly linked to Cancer research, which falls under the umbrella field of Notch signaling pathway. His research investigates the link between Glycosylation and topics such as Epidermal growth factor that cross with problems in Cell signaling, Cell fate determination and Maltose-binding protein. His study in Extracellular is interdisciplinary in nature, drawing from both Cell, In vitro, Notch binding, Notch proteins and JAG1.
Cell biology, Notch signaling pathway, Fucose, EGF-like domain and Biochemistry are his primary areas of study. Robert S. Haltiwanger is studying Signal transduction, which is a component of Cell biology. His Signal transduction research integrates issues from Acquired immune system, Epidermal growth factor, Function, Regulator and Major histocompatibility complex.
His Notch signaling pathway study frequently links to other fields, such as Glycosylation. His studies deal with areas such as Proteases and Fucosylation, Glycan as well as Glycosylation. The various areas that Robert S. Haltiwanger examines in his Fucose study include Mutation, Glucosyltransferase, Consensus sequence and Serine.
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Fringe is a glycosyltransferase that modifies Notch
Daniel J. Moloney;Vladislav M. Panin;Stuart H. Johnston;Stuart H. Johnston;Jihua Chen.
Role of Glycosylation in Development
Robert S Haltiwanger;John B Lowe.
Annual Review of Biochemistry (2003)
Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
G. D. Holt;C. M. Snow;A. Senior;R. S. Haltiwanger.
Journal of Cell Biology (1987)
Glycosylation in the nucleus and cytoplasm
Gerald W. Hart;Robert S. Haltiwanger;Gordon D. Holt;William G. Kelly.
Annual Review of Biochemistry (1989)
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.
Robert S. Haltiwanger;Mellissa A. Blomberg;Gerald Warren Hart.
Journal of Biological Chemistry (1992)
Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase.
Robert S. Haltiwanger;Gordon D. Holt;Gerald Warren Hart.
Journal of Biological Chemistry (1990)
Mammalian Notch1 Is Modified with Two Unusual Forms ofO-Linked Glycosylation Found on Epidermal Growth Factor-like Modules
Daniel J. Moloney;Louisa H. Shair;Frederick M. Lu;Jie Xia.
Journal of Biological Chemistry (2000)
Modulation of O-LinkedN-Acetylglucosamine Levels on Nuclear and Cytoplasmic Proteins in Vivo Using the PeptideO-GlcNAc-β-N-acetylglucosaminidase InhibitorO-(2-Acetamido-2-deoxy-dglucopyranosylidene)amino-N-phenylcarbamate
Robert S. Haltiwanger;Kathleen Grove;Glenn A. Philipsberg.
Journal of Biological Chemistry (1998)
Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling
Melih Acar;Hamed Jafar-Nejad;Hideyuki Takeuchi;Akhila Rajan.
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase.
Yang Wang;Li Shao;Shaolin Shi;Reed J. Harris.
Journal of Biological Chemistry (2001)
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