The adhesive protein secreted by marine sessile animals can resist the resistance of water and exert stickiness under the humid environment. It has become a candidate for the development of high-performance materials in the field of biomedicine and bionics. Barnacles are as one of the marine macrofoulers that can be firmly attached to the underwater substrate materials with different surface characteristics through its cement proteins. To date, the adhesion process of barnacle has been understood in-depth, but the specific underwater adhesion mechanism has not been elucidated and needs further exploration. This review first presented an overview of barnacle and its adhesion process, followed by summarizing the advances of barnacle adhesive protein, its production methods, and applications. Moreover, challenges and future perspectives were prospected.
Animals ; Thoracica/metabolism* ; Proteins/metabolism* ; Adhesives/metabolism*

Carrier Proteins ; metabolism ; Humans ; Microfilament Proteins ; metabolism ; Neoplasm Proteins ; metabolism ; Thyroid Neoplasms ; metabolism ; pathology

Nogo-B receptor (NgBR) is a specific receptor of Nogo-B, a member of reticulon 4 protein family. It is widely expressed in many tissues and mainly located in cell membrane and endoplasmic reticulum. Previous studies have revealed that NgBR is involved in a variety of physiological and pathophysiological processes, such as dolichol synthesis, lipid metabolism, cholesterol trafficking, insulin resistance, vascular remodeling and angiogenesis, tumorigenesis and nervous system diseases. Further studies on the molecular characteristics and biological function of NgBR might be of great significance to understand its role in diverse diseases and provide possible clinical strategies for the treatment of diseases.
Carrier Proteins/metabolism* ; Endoplasmic Reticulum/metabolism* ; Lipid Metabolism ; Nogo Proteins/metabolism* ; Receptors, Cell Surface/metabolism*

No abstract available.
Acetyltransferases/metabolism ; Animal ; Carrier Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Human ; Nuclear Proteins/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism* ; Repressor Proteins/metabolism*n ; Trans-Activators/metabolism* ; Transcription Factors/metabolism

Humans ; Telomere ; metabolism ; Telomere-Binding Proteins ; metabolism

Capsid Proteins ; genetics ; metabolism ; Simplexvirus ; genetics ; metabolism

Urease decomposes urea to ammonia, and has application potential in agriculture and medical treatment. Urease proteins include structural proteins (UreA, UreB and UreC) and accessory proteins (UreD/UreH, UreE, UreF and UreG), each of them has its own unique role in urease maturation. The structural proteins form the active center of urease, and the accessory proteins are responsible for the delivery of nickel. We review here the structure and function of bacterial urease complexes, and how each protein interacts to complete the activation process. We hope to provide theoretical basis for the regulation of urease activity and the development of urease inhibitors.
Bacterial Proteins ; Nickel ; Urease ; metabolism

Membrane Proteins/metabolism* ; Protein Binding

Carrier Proteins ; Autophagy ; Lipid Metabolism

In Gram-negative bacteria, lipopolysaccharide transport (Lpt) protein LptA and LptC form a complex to transport LPS from the inner membrane (IM) to the outer membrane (OM). Blocking the interaction between LptA and LptC will lead to the defect of OM and cell death. Therefore, Lpt protein interaction could be used as a target to screen new drugs for killing Gram-negative bacteria. Here we used biolayer interferometry (BLI) assay to detect the interaction between LptA and LptC, with the aim to develop a method for screening the LptA/LptC interaction blockers in vitro. Firstly, LptC and LptA with or without signal peptide (LptAfull or LptAno signal) were expressed in E. coli BL21(DE3). The purified proteins were then labeled with biotin and the super streptavidin (SSA) biosensor was blocked with diluent. The biotin labeled protein sample was mixed with the sensor, and then the binding of the protein with a series of diluted non biotinylated protein was detected. At the same time, non-biotinylated protein was used as a control. The binding of biotinylated protein to a small molecule IMB-881 and the blocking of interaction were also detected by the same method. In the blank control, the biosensor without biotinylated protein was used to detect the serially diluted samples. The signal response constant was calculated by using steady analysis. The results showed that biotinylated LptC had a good binding activity with LptAfull and LptAno signal with KD value 2.9e⁻⁷±7.9e⁻⁸ and 6.0e⁻⁷±2.8e⁻⁸, respectively; biotinylated LptAno signal had a good binding activity with LptC, with a KD value of 9.6e⁻⁷±7.2e⁻⁸. All binding curves showed obvious fast binding and fast dissociation morphology. The small molecule compound IMB-881 can bind to LptA to block the interaction between LptA and LptC, but has no binding activity with LptC. In summary, we developed a method for detecting the LptA/LptC interaction based on the BLI technology, and confirmed that this method can be used to evaluate the blocking activity of small molecule blockers, providing a new approach for the screening of LptA/LptC interaction blockers.
Carrier Proteins ; Escherichia coli/metabolism* ; Escherichia coli Proteins/metabolism* ; Interferometry ; Membrane Proteins/metabolism*