700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ ReadersThis Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
Journal Impact Factor 1.8*
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Journal of Glycobiology is a peer reviewed journal that publishes studies related to structure, biosynthesis, biology and functions of different saccharides, glycans, oligosaccharides or the different proteins which interact with the glycans.
Journal of Glycobiology is a Open Access Scientific Journal that offers an interesting publishing platform globally and aims to keep scientists, researchers, and students informed and updated on the ongoing research in the relevant area. Outstanding quality articles are welcome to maintain the highest standard of the journal and to achieve high impact factor.
Journal of Glycobiology is using Editorial Manager System for maintaining the quality in peer review process. Editorial Manager is an online manuscript submission, review and tracking system. Review processing is performed by the editorial board members of Journal of Glycobiology: Current Research or by outside experts. At least two independent reviewers approval followed by editor approval is required for acceptance of any citable manuscript. Authors may submit manuscripts and track their progress through the system, hopefully to publication. Reviewers can download manuscripts and submit their opinions to the editor. Editors can manage the whole submission/review/revise/publish process.
A bacterial product that enables bacteria to adhere to and colonize a host. Adherence is often an essential step in pathogenesis. Adhenins are attractive candidates for vaccines and/or components of accellular vaccines such as those for pertussis. their susceptibility to reversal of such binding activities in the presence of mannose. negative bacteria function as adhenins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhenin. In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhenin
Related Journals of Adhenins
Biochemistry & Molecular Biology Journal, Glycobiology, Plant Biochemistry & Physiology, Biochemistry Journal, Microbial Biotechnology, Advances in Applied Microbiology, Polish Journal of Microbiology, Brazilian Journal of Microbiology, Glycobiology.
Glycosylation is the binding of carbohydrate molecules to proteins .is a post translational modification which provides greater proteomic diversity than other post translational modifications. Glycosylation is critical for a wide range of biological processes, including cell attachment to the extracellular matrix and protein-ligand interactions in the cell. Glycosylation types are classified based on the identity of the atom of the amino acid which binds the carbohydrate chain, i.e. C-linked, N-linked or O-linked. N- and C-glycosylation take place.
Related Journals of Glycosylation
Molecular Biology Journal, Biochemistry & Molecular Biology Journal, Membrane Science & Technology, Metabonomics & Metabolites, Glycosylation & Disease, BBA General Subjects, Journal of Bioscience and Bioengineering, Annual Review of Biochemistry.
Glycoproteins consists of oligosaccharide chains which are covalently attached to the polypeptide side chains. The saccharide chains, referred to as glycans, can be linked to the polypeptide in two major ways. The first class of glycoproteins is the O-linked glycans. These usually contain an N-acetylgalactosamine which is attached through a glycosidic bond to the O-terminus of either threonine or serine. The other classes of glycoproteins are the N-linked glycans. These involve a glycosidic bond between N-acetylglucosamine and the N-terminus of an asparagine residue
Related Journals of Glycoproteins
Organic & Inorganic Chemistry, Metabolomics:Open Access, Chemical Biology Journal, Organic Chemistry: Current Research, Progress in Lipid Research, Protein Science, Protein and Cell, Protein Journal, Proteins: Structure, Function, and Genetics, Nature Chemical Biology.
Proteoglycans are also known as mucoproteins and are formed of glycosaminoglycan’s which are covalently attached to the core proteins. They are found in all connective tissues, extracellular matrix and on the surfaces of many cell types. Hydrated proteoglycans form the highly viscous fluid of mucus and the matrix of the intercellular ground substance of connective tissue.
Related Journals of Proteoglycans
Biochemistry Journal, Structural Chemistry Journal, Organic & Inorganic Chemistry, Proteomics & Enzymology, Molecular and Cellular Proteomics, Journal of Proteome Research, Acta - Proteins and Proteomics, Journal of Proteomics, Genomics Proteomics Bioinformatics, Journal of Biological Chemistry, Chemical Reviews.
Glycolipids are the lipids which attached to the carbohydrate molecules. The glycolipids are yet another division of lipids that is utilised by the human as well as other forms of life. Glycolipids are named in reference to their chemical structure: practically all glycolipids are derivatives of ceramides. Ceremides are a fatty acid bonded or connected to the amino alcohol sphingosine. In fact, although the class of lipids we discussed called phospholipids, are chemically different from glycolipids, the phospholipid we call sphingomyelin, also is derived from ceramides.
Related Journals of Glycolipids
Molecular Biology Journal, Chemical Biology Journal, Glycobiology, Proteomics & Enzymology, Journal of Lipid Research , Prostaglandins and Other Lipid Mediators, Chemistry and Physics of Lipids, Lipids, Lipid Insights, Biological & Pharmaceutical Bulletin.
The term glycomics is defined as the study of the structure and function of carbohydrates (sugars) in biological systems. Glycomics is the comprehensive study of the Glycome. This includes the entire molecules of sugars of an organism such as glycans attached to proteins and lipids, glycosaminoglycans and polysaccharides, including genetic, physiologic, pathologic, and other aspects.
Related Journals of Glycomics
Chemical Biology Journal, Molecular Biology Journal, Glycobiology, Plant Biochemistry & Physiology, Journal of Glycomics & Lipidomics, Journal of Glycomics And Metabolism, Open Glycoscience, Trends in Glycoscience and Glycotechnology, ChemBioChem, Science.
Hemagglutinins are the substances which are caused to agglutinate the RBC. Antibodies and lectins are the commonly known hemagglutinins. hemagglutinin is composed of two different types of chains, the blue chains are the targeting mechanism: they search for specific sugar chains on our cellular proteins. When they find the proper one, hemagglutinin binds to the cell and the orange chains initiate the attack
Related Journals of Hemagglutinin
Biochemistry & Molecular Biology Journal, Steroids & Hormonal Science, Metabonomics & Metabolites,Biochemistry Journal, Blood, British Journal of Haematology, Indian Journal of Hematology and Blood Transfusion, Journal of Coagulation Disorders, Open Hematology Journal, Chemical Society Reviews.
Hyaluronan is also known as Hyaluronic acid or Hyaluronate. is a high-molecular-mass polysaccharide found in the extracellular matrix, especially of soft connective tissues. It is synthesized in the plasma membrane of fibroblasts and other cells by addition of sugars to the reducing end of the polymer, whereas the nonreducing end protrudes into the pericellular space.
Related Journals of Hyaluronan
Biochemistry Journal, Molecular Biology Journal, Biochemistry & Analytical Biochemistry, Chemical Sciences Journal, Carbohydrate Polymers, Bioactive Carbohydrates and Dietary Fibre, Scientific Reports.
The chief function of lectins in animals is to facilitate cell-cell contact. A lectin usually contains two or more binding sites for carbohydrate units; some lectins form oligomeric structures with multiple binding sites. The binding sites of lectins on the surface of one cell interact with arrays of carbohydrates displayed on the surface of another cell
Related Journals of Lectins
Chemical Sciences Journal, Organic & Inorganic Chemistry, Plant Biochemistry & Physiology, Molecular Biology Journal, Lectins, Biology, Biochemistry, Clinical Biochemistry, Acta Histochemica, BMC Biology, Chemical Science, Nature.
Sialic acids are are typically found to be terminating branches of N-glycans, O-glycans, and glycosphingolipids. Human milk also contains a high concentration of sialic acid attached to the terminal end of free oligosaccharides. Sialic acids also differ from other sugars in that they are less commonly utilized as an energy source but are critical to development, cellular recognition, cell-cell attachment, and signaling
Related Journals of Sialic acid
Biochemistry Journal, Structural Chemistry Journal, Organic Chemistry: Current Research, Organic & Inorganic Chemistry,
Protein Expression and Purification, Asian Journal of Pharmaceutical Sciences, Chemistry & Biology.
Glycoconjugates are biologically important molecules with diverse functions. They consist of carbohydrates of varying size and complexity, attached to a non-sugar moiety as a lipid or a protein. Glycoconjugate structures are often very complex and their intricate biosynthetic pathways makes overexpression difficult. While the biosynthesis of proteins and nucleic acids follows a template, the assembly of the oligosaccharides is more complex and depends on which glycosylating-enzymes that are active in the cell and if they are capable of glycosylating the substrate
Related Journals of Glycoconjugates
Molecular Biology Journal, Chemical Biology Journal, Membrane Science & Technology, Plant Biochemistry & Physiology, Glycoconjugate Journal, Glyco Journals, Recent Advances in Carbohydrates and Glycoconjugates, Biochimica et Biophysica Acta.
C-type lectin receptors (CLRs) are a diverse family of soluble and transmembrane proteins that contain one or more C-type lectin-like domains (CTLD). Multiple members of the CLR family are considered to be pattern recognition receptors (PRRs) due to their ability to recognize pathogen-associated molecules and induce intracellular signaling pathways that regulate the immune response
Related Journals of C-type
Membrane Science & Technology, Chemical Biology Journal, Chemical Informatics, Structural Chemistry Journal, Lectins Immunobiology, Molecular Biology of the Cell, BMC Biology, Protein and Peptide Letters, Current Opinion in Structural Biology.
The P-type lectins play an essential role in the generation of functional lysosomes within the cells of higher eukaryotes by directing newly synthesized lysosomal enzymes bearing the mannose 6-phosphate (M6P) signal to lysosomes. cation-independent mannose 6-phosphate receptor (CI-MPR) is also referred as insulin-like growth factor 2 receptor (IGF2R) or IGF2/MPR
Related Journals of P-Type Lectins
Chemical Biology Journal, Steroids & Hormonal Science, Chemical Sciences Journal, Plant Biochemistry & Physiology, Glycobiology, Molecular and Cellular Biology, Journal of Structural Biology. Journal of Peptide Science, Carbohydrate Research.
I-Type lectins are glycan binding proteins that belong to the immunoglobulin superfamily (IgSF), excluding antibodies and T-cell receptors. A number of disparate immunoglobulin superfamily members may bind carbohydrate ligands, but the best characterized of the I-type lectins are members of the siglec family of sialic acid-binding cell surface adhesion receptors
Related Journals of I-Type lectins
Proteomics & Enzymology, Chemical Biology Journal, Structural Chemistry Journal, Medicinal Chemistry, Journal of Glycobiology, Journal of Lipid Research, Proteins: Structure, Function and Genetics, Current Protocols in Protein Science, Nature Structural & Molecular Biology.
Cells are endowed with a rich surface coat of glycans that are carried as glycoproteins and glycolipids on the outer leaflets of their plasma membranes and constitute a major molecular interface between cells and their environment. Each cell's glycome, the sum of its diverse glycan structures, comprises a distinct cellular signature defined by expression levels of the enzymes responsible for glycan biosynthesis. This signature can be read by complementary glycan-binding proteins (GBPs) that translate glycan recognition into function.
Related Journals of Glycan Binding Proteins
Chemical Biology Journal, Organic & Inorganic Chemistry, Biochemistry Journal, Glycobiology, Calcium Binding Proteins, Glycobiology Insights, Cell Adhesion and Migration, Glycoconjugate Journal.
Glycosaminoglycans have high degrees of heterogeneity with regards to molecular mass, disaccharide construction, and sulfation due to the fact that GAG-synthesis, unlike proteins or nucleic acids, is not template driven, and dynamically modulated by processing enzymes. glycosaminoglycan chains are linear polysaccharides, whose disaccharide building blocks consist of an amino sugar N-substituted, or a uronic acid or galactose.
Related Journals of Glycosaminoglycans
Molecular Biology Journal, Chemical Biology Journal, Molecular Biology Journal, Biology Journal, glycosaminoglycan, Progress in Biophysics & Molecular Biology, Clinica Chimica Acta, Carbohydrate Research, Analytical Biochemistry.
Heparan sulfate proteoglycans are found at the cell surface and in the extracellular matrix, where they interact with a plethora of ligands.These are glycoproteins, with the common characteristic of containing one or more covalently attached heparan sulfate chains, a type of glycosaminoglycan. Heparan sulfate proteoglycan (HSPG) is a receptor of diverse macromolecular cargo, endocytosis is involved in infectious disease, lipid metabolism cancer and HSPG represents an interesting target for macromolecular drug delivery.
Related Journals of Heparan Sulfate
Structural Chemistry Journal, Biochemistry Journal, Proteomics & Enzymology, Plant Biochemistry & Physiology, Molecular and Cellular Biology, Molecular Biology of the Cell, Cell Adhesion and Migration, Current Topis in Membranes, Journal of Biological Chemistry.
*2016 Journal Impact Factor was established by dividing the number of articles published in 2014 and 2015 with the number of times they are cited in 2016 based on Google search and the Scholar Citation Index database. If 'X' is the total number of articles published in 2014 and 2015, and 'Y' is the number of times these articles were cited in indexed journals during 2016 then, impact factor = Y/X