Howard R. Morris
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Howard R. Morris has a total of 30 co-authors. Here are the top co-authors by number of shared publications:
- Anne Dell
Department of Life Sciences, Imperial College London, London SW7 2AZ, UK
3 shared publications Alessio Ceroni
Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London, SW7 2AZ, United Kingdom
1 shared publicationAnne Dell
Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK
1 shared publicationAntonietta Capone
Dept. Evolutionary Biology, University of Siena, Via A. Moro 2, 53100 Siena, Italy
1 shared publication- Aristotelis Antonopoulos
Department of Life Sciences, Imperial College London, London SW7 2AZ, UK
1 shared publication Bérangère Tissot
Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, United Kingdom
1 shared publication
Latest Publications
- Open Access
- 3 September 2020
- Published by Oxford University Press (OUP) in Glycobiology
- Vol. 31 (3) , 181-187
Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain
The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.
- 3 September 2020
- Published by Oxford University Press (OUP) in Glycobiology
- Vol. 31 (3) , 181-187
Open AccessSite-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain
The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.
- Open Access
- 27 March 2009
- Published by Wiley in FEBS Letters
- Vol. 583 (11) , 1728-1735
Glycoproteomics: Past, present and future
This invited paper reviews the study of protein glycosylation, commonly known as glycoproteomics, beginning with the origins of the subject area in the early 1970s shortly after mass spectrometry was...
- 27 March 2009
- Published by Wiley in FEBS Letters
- Vol. 583 (11) , 1728-1735
Open AccessGlycoproteomics: Past, present and future
This invited paper reviews the study of protein glycosylation, commonly known as glycoproteomics, beginning with the origins of the subject area in the early 1970s shortly after mass spectrometry was...
- 10 June 1996
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 10 (8) , 889-896
High Sensitivity Collisionally‐activated Decomposition Tandem Mass Spectrometry on a Novel Quadrupole/Orthogonal‐acceleration Time‐of‐flight Mass Spectrometer
- 10 June 1996
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 10 (8) , 889-896
High Sensitivity Collisionally‐activated Decomposition Tandem Mass Spectrometry on a Novel Quadrupole/Orthogonal‐acceleration Time‐of‐flight Mass Spectrometer
- Open Access
- 1 June 1996
- Published by Wiley in European Journal of Biochemistry
- Vol. 238 (2) , 357-367
Occurrence and Structural Analysis of Highly Sulfated Multiantennary N‐linked Glycan Chains Derived from a Fertilization‐Associated Carbohydrate‐Rich Glycoprotein in Unfertilized Eggs of Tribolodon hakonensis
This study represents the first detailed investigation of the nature of highly sulfated (keratan-sulfate-like) complex-type asparagine-linked glycans having a tetraantennary core structure and shows the effectiveness of fast-atom-bombardment mass spectrometric (FAB-MS) methods incorporating derivatization and mild methanolysis for analyzing such complex types of sulfated glycans. The structure of the N-glycan chains was unambiguously established by a combination of compositional analysis, methylation analysis, mild methanolysis for desulfation, hydrazinolysis/nitrous acid deamination, enzymatic (endo-β-galactosidase and peptide: N-glycosidase F) digestions, and instrumental analyses (1H-NMR spectroscopy and FAB-MS) which revealed the novel repeating sulfated carbohydrate sequences, ±Galβ1 → 4Galβ1[→ 4(HSO3→ 6)GlcNAcβ1 → 3(±Galβ1 → 4)Galβ1]n→ (see Structure I; p+q+r+s ≈ 14). This sequence is unique in: (a) the skeletal structure is similar to that of keratan sulfate but is completely devoid of 6-O-sulfated Gal residues and (b) the presence of branched Gal residues in the sequence → 4GlcNAcβ1 → 3(Galβ1 → 4)Galβ1→.
- 1 June 1996
- Published by Wiley in European Journal of Biochemistry
- Vol. 238 (2) , 357-367
Open AccessOccurrence and Structural Analysis of Highly Sulfated Multiantennary N‐linked Glycan Chains Derived from a Fertilization‐Associated Carbohydrate‐Rich Glycoprotein in Unfertilized Eggs of Tribolodon hakonensis
This study represents the first detailed investigation of the nature of highly sulfated (keratan-sulfate-like) complex-type asparagine-linked glycans having a tetraantennary core structure and shows the effectiveness of fast-atom-bombardment mass spectrometric (FAB-MS) methods incorporating derivatization and mild methanolysis for analyzing such complex types of sulfated glycans. The structure of the N-glycan chains was unambiguously established by a combination of compositional analysis, methylation analysis, mild methanolysis for desulfation, hydrazinolysis/nitrous acid deamination, enzymatic (endo-β-galactosidase and peptide: N-glycosidase F) digestions, and instrumental analyses (1H-NMR spectroscopy and FAB-MS) which revealed the novel repeating sulfated carbohydrate sequences, ±Galβ1 → 4Galβ1[→ 4(HSO3→ 6)GlcNAcβ1 → 3(±Galβ1 → 4)Galβ1]n→ (see Structure I; p+q+r+s ≈ 14). This sequence is unique in: (a) the skeletal structure is similar to that of keratan sulfate but is completely devoid of 6-O-sulfated Gal residues and (b) the presence of branched Gal residues in the sequence → 4GlcNAcβ1 → 3(Galβ1 → 4)Galβ1→.