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Topic Review
Protein Tyrosine Phosphatases
Protein tyrosine kinases, especially receptor tyrosine kinases, have dominated the cancer therapeutics sphere as proteins that can be inhibited to selectively target cancer. However, protein tyrosine phosphatases (PTPs) are also an emerging target. Though historically known as negative regulators of the oncogenic tyrosine kinases, PTPs are now known to be both tumor-suppressive and oncogenic.
  • 576
  • 07 Dec 2021
Topic Review
Protein Tyrosine Phosphatase Receptor Gamma
Protein tyrosine phosphatase gamma (PTPRG) is an enzyme that remove phosphate groups from phosphotyrosine residues of specific intracellular targets. It belongs to the tyrosine phosphatase (PTP) family of proteins and it is widely expressed in human tissues. 
  • 654
  • 23 Feb 2022
Topic Review
Protein Structure Prediction
The new advances in deep learning methods have influenced many aspects of scientific research, including the study of the protein system. The prediction of proteins’ 3D structural components is now heavily dependent on machine learning techniques that interpret how protein sequences and their homology govern the inter-residue contacts and structural organization. Especially, methods employing deep neural networks have had a significant impact on recent CASP13 and CASP14 competition. Here, we explore the recent applications of deep learning methods in the protein structure prediction area. We also look at the potential opportunities for deep learning methods to identify unknown protein structures and functions to be discovered and help guide drug–target interactions. Although significant problems still need to be addressed, we expect these techniques in the near future to play crucial roles in protein structural bioinformatics as well as in drug discovery.
  • 648
  • 24 Jun 2021
Topic Review
Protein Structure Fluctuation
Proteins are indispensable to cellular communication and metabolism. The structure on which cells and tissues are developed is deciphered from proteins. To perform functions, proteins fold into a three-dimensional structural design, which is specific and fundamentally determined by their characteristic sequence of amino acids.
  • 861
  • 19 Apr 2022
Topic Review
Protein Quality Control Systems in SARS-CoV-2 Infection
SARS-CoV-2’s structure and mechanism of infection have been well characterized. The virus comprises a lipid envelope studded with spike (S) proteins. These spikes facilitate viral entry into host cells by binding to angiotensin-converting enzyme 2 (ACE2) receptors on the cell surface. Following attachment, the virus enters the cell by endocytosis. Its genetic material consists of a single-stranded RNA molecule, which encodes structural proteins, non-structural proteins (NSP), and accessory proteins. Once inside, the viral RNA is translated into proteins, including those for replication and the formation of new virus particles.
  • 277
  • 24 Jan 2024
Topic Review
Protein Phase Separation
Phase separation is a process by which a well-mixed solution of macromolecules such as proteins or nucleic acids spontaneously separates into two phases: a dense phase and a dilute phase.
  • 630
  • 06 Dec 2022
Topic Review
Protein Kinase D
Protein kinase D (PKD) is a family of serine/threonine protein kinases operating in the signaling network of the second messenger diacylglycerol. PKD belongs to the Calcium/calmodulin-dependent protein kinases superfamily and consists of three isoforms in mammals, notably, PKD1, PKD2 and PKD3. Activated PKD resides in diverse subcellular locations such as cytosol, Golgi apparatus, nucleus, mitochondria to regulate a number of cellular functions.
  • 727
  • 15 Apr 2021
Topic Review
Protein Kinase CK2
Protein kinase CK2 (CK2) is a ubiquitous holoenzyme involved in a wide array of developmental processes. The involvement of CK2 in events such as neurogenesis, cardiogenesis, skeletogenesis, and spermatogenesis is essential for the viability of almost all organisms, and its role has been conserved throughout evolution.
  • 586
  • 02 Sep 2022
Topic Review
Protein Glycosylation
Protein glycosylation is a highly conserved post-translational modification among organisms. It plays fundamental roles in many biological processes, ranging from protein trafficking and cell adhesion to host–pathogen interactions. According to the amino acid side chain atoms to which glycans are linked, protein glycosylation can be divided into two major categories: N-glycosylation and O-glycosylation. However, there are other types of modifications such as the addition of GPI to the C-terminal end of the protein. Besides the importance of glycoproteins in biological functions, they are a major component of the fungal cell wall and plasma membrane and contribute to pathogenicity, virulence, and recognition by the host immunity. Given that this structure is absent in host mammalian cells, it stands as an attractive target for developing selective compounds for the treatment of fungal infections.
  • 1.0K
  • 27 Oct 2021
Topic Review
Protective Genes against Cancer
Richard Peto’s paradox, first described in 1975 from an epidemiological perspective, established an inverse correlation between the probability of developing cancer in multicellular organisms and the number of cells. Larger animals exhibit fewer tumors compared to smaller ones, though exceptions exist. Mice are more susceptible to cancer than humans, while elephants and whales demonstrate significantly lower cancer prevalence rates than humans. How nature and evolution have addressed the issue of cancer in the animal kingdom remains largely unexplored. In the field of medicine, much attention has been devoted to cancer-predisposing genes, as they offer avenues for intervention, including blocking, downregulating, early diagnosis, and targeted treatment. Predisposing genes also tend to manifest clinically earlier and more aggressively, making them easier to identify. 
  • 174
  • 01 Feb 2024
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