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    • Mass Spectrometry
    • Nicolle H Packer
    • Nicolle H Packer: Influence Statistics

      Nicolle H Packer

      Nicolle H Packer

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      Institute for Glycomics, Griffith University, Southport, QLD, 4222, Australia | School of Natural Sciences, Centre of Excellence for Nanoscale BioPhotonics, Macquarie ...

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      Nicolle H Packer:Expert Impact

      Concepts for whichNicolle H Packerhas direct influence:Mass spectrometry,Gel electrophoresis,Glycan structures,Membrane proteins,Protein glycosylation,Cystic fibrosis,Cancer cell,Glycoprotein sialylation.

      Nicolle H Packer:KOL impact

      Concepts related to the work of other authors for whichfor which Nicolle H Packer has influence:Mass spectrometry,Protein glycosylation,Liquid chromatography,Glycan structures,Human milk,Escherichia coli,Ovarian cancer.

      KOL Resume for Nicolle H Packer

      Year
      2022

      Institute for Glycomics, Griffith University, Southport, QLD, 4222, Australia

      2021

      Biomolecular Discovery and Design Research Centre, Department of Molecular Sciences, Faculty of Science & Engineering, Macquarie University, Sydney, NSW Australia

      ARC Centre of Excellence for Nanoscale BioPhotonics, Griffith University

      2020

      Institute for Glycomics, Gold Coast Campus, Griffith University, 4215, Gold Coast, QLD, Australia

      ARC Centre of Excellence for Nanoscale BioPhotonics

      2019

      ARC Centre of Nanoscale Biophotonics, Macquarie University, Sydney, NSW, Australia

      Macquarie University, CORE

      Centre for Nanoscale BioPhotonics

      2018

      Institute for Glycomics, Griffith University, Southport, Queensland, 4215, Australia

      2017

      Department of Chemistry and Biomolecular Sciences Macquarie University Sydney NSW Australia

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      Sample of concepts for which Nicolle H Packer is among the top experts in the world.
      Concept World rank
      biological cbg nglycans #1
      oligosaccharides liquid electrophoresis #1
      carbon microcolumn #1
      glycoproteins complex mixtures #1
      precipitation oligosaccharides #1
      gene assignment gp300 #1
      mass hose #1
      glycoproteins therapeutic targets #1
      database glycan #1
      αdgs glycosylation status #1
      glycomics datasets #1
      13 mucin genes #1
      composite agarose gel #1
      partly core #1
      glycan hydroxyl #1
      regulated nglycans #1
      unique glycan determinants #1
      grown angiosperm seedlings #1
      mrabs #1
      glycosylation sputum mucins #1
      elution behaviour nglycans #1
      initial step proteins #1
      function glycomics glycoproteomics #1
      protein nglycosylation applications #1
      heavy chain monomer #1
      cellular glycan surfaces #1
      unicarbkb functional #1
      sugarbinddb sugarbinddb #1
      major plasma glycoproteins #1
      bec membrane proteins #1
      pmgs tumor tissues #1
      substructure search tool #1
      human colostrum siga #1
      characterisation glycoproteins #1
      sweat secretory fluids #1
      pthglycoamino acids #1
      analysis enriched glycopeptides #1
      secretor status mass #1
      uptake fluorescent nanodiamonds #1
      western chromatography mannosides #1
      glycoproteins glycospectrumscan #1
      secreted proteins glycans #1
      polysia expression ngf #1
      annotated glycan structures #1
      disease glycomics #1
      esiitms tandem #1
      pgc based #1
      fastmigrating fm components #1
      glycomic mass #1
      pmg level #1
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      Prominent publications by Nicolle H Packer

      KOL-Index: 14642

      Escherichia coli K-12 has long been known not to produce an O antigen. We recently identified two independent mutations in different lineages of K-12 which had led to loss of O antigen synthesis (D. Liu and P. R. Reeves, Microbiology 140:49-57, 1994) and constructed a strain with all rfb (O antigen) genes intact which synthesized a variant of O antigen O16, giving cross-reaction with anti-O17 antibody. We determined the structure of this O antigen to be ...

      Known for Rfb Gene | Escherichia Coli | Antigen Synthesis | Carbohydrate Sequence | Reading Frames
      KOL-Index: 13987

      Campylobacter jejuni is a gastrointestinal pathogen that is able to modify membrane and periplasmic proteins by the N-linked addition of a 7-residue glycan at the strict attachment motif (D/E)XNX(S/T). Strategies for a comprehensive analysis of the targets of glycosylation, however, are hampered by the resistance of the glycan-peptide bond to enzymatic digestion or β-elimination and have previously concentrated on soluble glycoproteins compatible with lectin affinity and gel-based ...

      Known for Campylobacter Jejuni | Cid Hcd | Electron Transfer Dissociation | Hydrophilic Interaction | Higher Energy
      KOL-Index: 12664

      Epithelial ovarian cancer is the fifth most common cause of cancer in women worldwide bearing the highest mortality rate among all gynecological cancers. Cell membrane glycans mediate various cellular processes such as cell signaling and become altered during carcinogenesis. The extent to which glycosylation changes are influenced by aberrant regulation of gene expression is nearly unknown for ovarian cancer and remains crucial in understanding the development and progression of this ...

      Known for Gene Expression | Ovarian Cancer | Glycan Structures | Membrane Proteins | Dna Methylation
      KOL-Index: 12172

      Ovarian cancer is a fatal gynaecological malignancy in adult women with a five-year overall survival rate of only 30%. Glycomic and glycoproteomic profiling studies have reported extensive protein glycosylation pattern alterations in ovarian cancer. Therefore, spatio-temporal investigation of these glycosylation changes may unearth tissue-specific changes that occur in the development and progression of ovarian cancer. A novel method for investigating tissue-specific N-linked glycans is ...

      Known for Ovarian Cancer | Mass Spectrometry | Glycan Maldi | Fixed Paraffin | Tissue Regions
      KOL-Index: 10991

      A technique with subpicomolar sensitivity was developed for analyzing O-linked oligosaccharides released from glycoproteins separated by gel electrophoresis. The protocol involves gel electrophoresis, electroblotting to poly-(vinylidene fluoride) membrane, reductive beta-elimination, and analysis of released oligosaccharides by liquid chromatography coupled to negative ion electrospray mass spectrometry. It was also found that N-linked oligosaccharides could be recovered under the same ...

      Known for Gel Electrophoresis | Linked Oligosaccharides | Electrospray Ionization | Liquid Chromatography | Mucins Separated
      KOL-Index: 9846

      This study aimed to characterize human salivary glycoforms and the natural glycosylation variation of the major ABO blood group bearing high molecular weight glycoprotein fraction MG1, which mainly consists of MUC5B mucin. Reduced and alkylated mucins from individuals of blood group A, B, and O were purified by sodium dodecyl sulfate-agarose/polyacrylamide composite gel electrophoresis (SDS-AgPAGE), blotted to polyvinylidene fluoride (PVDF) membranes, and visualized with alcian blue. ...

      Known for Secretor Status | Human Saliva | Abo Blood | Sulfated Oligosaccharides | Liquid Chromatography
      KOL-Index: 9779

      Mucosal epithelial surfaces, such as line the oral cavity, are common sites of microbial colonization by bacteria, yeast and fungi. The microbial interactions involve adherence between the glycans on the host cells and the carbohydrate-binding proteins of the pathogen. Saliva constantly bathes the buccal cells of the epithelial surface of the mouth and we postulate that the sugars on the salivary glycoproteins provide an innate host immune mechanism against infection by competitively ...

      Known for Candida Albicans | Salivary Glycoproteins | Host Cells | Saliva Glycans | Structural Analysis
      KOL-Index: 9204

      Recent developments in spatial proteomics have paved the way for retrospective in situ mass spectrometry (MS) analyses of formalin-fixed paraffin-embedded clinical tissue samples. This type of analysis is commonly referred to as matrix-assisted laser desorption/ionization (MALDI) imaging. Recently, formalin-fixed paraffin-embedded MALDI imaging analyses were augmented to allow in situ analyses of tissue-specific N-glycosylation profiles. In the present study, we outline an improved ...

      Known for Maldi Imaging | Mass Spectrometry | Linked Glycans | Fixed Paraffin | Liquid Chromatography
      KOL-Index: 9168

      Two-dimensional (2-D) electrophoresis is the preferred method for separating the glycoforms of proteins. The isoforms usually present as 'trains' of spots in the first dimension and may also differ in molecular weight. The primary goal for analyzing the carbohydrate content of glycoprotein spots is to understand the 'rules' which govern the migration of glycoproteins in 2-D electrophoresis. These rules can then be used to produce predictive vectors to interpret changes in glycosylation ...

      Known for Gel Electrophoresis | Glycoproteins Separated | Protein Spots | Nlinked Oligosaccharides | Molecular Weight
      KOL-Index: 8787

      The incorporation of radioactive aminolevulinic acid (ALA) into chlorophyll (Chl) a and b, as well as protochlorophyllide (Pchlide) in light-grown barley seedlings (Hordeum vulgare L. cv. Clipper) transferred to darkness is demonstrated. In the experiments described, 6-day-old, glasshouse-grown seedlings were transferred to darkness and incubated in [14C]- or [3H]- ALA for 18 h. Chl a and b were extracted and purified to constant specific radioactivity by HPLC and TLC of their ...

      Known for Chl Darkness | Barley Seedlings | Aminolevulinic Acid | Magnesiumfree Derivatives | Light Grown
      KOL-Index: 8603

      The small envelope proteins (HBsAgS) derived from hepatitis B virus (HBV) represent the antigenic components of the HBV vaccine and are platforms for the delivery of foreign antigenic sequences. To investigate structure-immunogenicity relationships for the design of improved immunization vectors, we have generated biochemically modified virus-like particles (VLPs) exhibiting glycoengineered HBsAgS. For the generation of hypoglycosylated VLPs, the wild-type (WT) HBsAgS N146 glycosylation ...

      Known for Enhanced Immunogenicity | Hepatitis Virus | Hyperglycosylated Vlps | Foreign Antigenic Sequences | Immune Responses
      KOL-Index: 8595

      Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the Human Proteome Organisation (HUPO) Human ...

      Known for Glycoprotein Glycans | Disease Glycomics | Proteome Initiative | Oligosaccharide Analysis | Hupo Human
      KOL-Index: 8583

      Site-specific structural characterization of glycoproteins is important for understanding the exact functional relevance of protein glycosylation. Resulting partly from the multiple layers of structural complexity of the attached glycans, the system-wide site-specific characterization of protein glycosylation, defined as glycoproteomics, is still far from trivial leaving the N- and O-linked glycoproteomes significantly under-defined. However, recent years have seen significant advances ...

      Known for Protein Glycosylation | Liquid Chromatography | Sample Preparation | Advances Glycoproteomics | Intact Glycopeptides
      KOL-Index: 8027

      GlycoSuiteDB is a relational database that curates information from the scientific literature on glyco-protein derived glycan structures, their biological sources, the references in which the glycan was described and the methods used to determine the glycan structure. To date, the database includes most published O:-linked oligosaccharides from the last 50 years and most N:-linked oligosaccharides that were published in the 1990s. For each structure, information is available concerning ...

      Known for Biological Sources | Relational Database | Glycan Structure | Storage Retrieval | Literature References
      KOL-Index: 8011

      Extracellular and cell surface proteins are generally modified with N-linked glycans and glycopeptide enrichment is an attractive tool to analyze these proteins. The role of N-linked glycoproteins in cardiovascular disease, particularly ischemia and reperfusion injury, is poorly understood. Observation of glycopeptides by mass spectrometry is challenging due to the presence of abundant, nonglycosylated analytes, and robust methods for purification are essential. We employed digestion ...

      Known for Myocardial Ischemia | Extracellular Environment | Cardiac Remodeling | Mass Spectrometry | Linked Glycoproteins

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      Institute for Glycomics, Griffith University, Southport, QLD, 4222, Australia | School of Natural Sciences, Centre of Excellence for Nanoscale BioPhotonics, Macquarie University, Sydney, NSW 2109, Australia | Biomolecular Discovery and Design Researc

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