Results 11 to 20 of about 1,164,783 (293)
Anchor Peptide of Transferrin-binding Protein B Is Required for Interaction with Transferrin-binding Protein A [PDF]
Gram-negative bacterial pathogens belonging to the Pasteurellaceae, Moraxellaceae, and Neisseriaceae families rely on an iron acquisition system that acquires iron directly from host transferrin (Tf). The process is mediated by a surface receptor composed of transferrin-binding proteins A and B (TbpA and TbpB).
Xue, Yang +4 more
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Transferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a ...
Jun Cao
doaj +1 more source
The interaction behavior of Fe3+ with transferrin and apotransferrin (iron-free form) was investigated in this study using affinity capillary electrophoresis.
Mohammed Al Bratty +5 more
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This study systematically reviews and characterizes the existing literature on transferrin/transferrin receptor-mediated drug delivery. Transferrin is an iron-binding protein. It can be used as a ligand to deliver various proteins, genes, ions, and drugs
Tarnjot Kaur +4 more
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Structural Variations within the Transferrin Binding Site on Transferrin-binding Protein B, TbpB [PDF]
Pathogenic bacteria acquire the essential element iron through specialized uptake pathways that are necessary in the iron-limiting environments of the host. Members of the Gram-negative Neisseriaceae and Pasteurellaceae families have adapted to acquire iron from the host iron binding glycoprotein, transferrin (Tf), through a receptor complex comprised ...
Calmettes, Charles +6 more
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Identification of human transferrin-binding sites within meningococcal transferrin-binding protein B [PDF]
Transferrin-binding protein B (TbpB) from Neisseria meningitidis binds human transferrin (hTf) at the surface of the bacterial cell as part of the iron uptake process. To identify hTf binding sites within the meningococcal TbpB, defined regions of the molecule were produced in Escherichia coli by a translational fusion expression system and the ability
G, Renauld-Mongénie +6 more
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Iron-Induced Oxidative Stress in Human Diseases
Iron is responsible for the regulation of several cell functions. However, iron ions are catalytic and dangerous for cells, so the cells sequester such redox-active irons in the transport and storage proteins.
Teruyuki Kawabata
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An insight into the changes in human plasma proteome on adaptation to hypobaric hypoxia. [PDF]
Adaptation to hypobaric hypoxia is required by animals and human in several physiological and pathological situations. Hypobaric hypoxia is a pathophysiological condition triggering redox status disturbances of cell organization leading, via oxidative ...
Yasmin Ahmad +5 more
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Background: Obesity is characterized by adipose tissue dysregulation and predisposes individuals to insulin resistance and type 2 diabetes. At the molecular level, adipocyte dysfunction has been linked to obesity-triggered oxidative stress and protein ...
M. Carmen Navarro-Ruiz +12 more
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