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  1. May 18, 2023 · Over the past decade extensive studies have established functional roles of Olig1 and Olig2 in development as well as in cancer. Olig2 overexpression drives glioma proliferation and resistance to radiation and chemotherapy. In this review, we summarize the biological functions of the Olig family in brain cancer and how targeting Olig family ...

  2. Apr 29, 2024 · The family serves important biological functions by providing for the care, nurturing, and socialization of offspring. It also contributes to the passing down of genetic material and cultural ...

  3. Abstract. The SPARC family of proteins represents a diverse group of proteins that modulate cell interaction with the extracellular milieu. The eight members of the SPARC protein family are modular in nature. Each shares a follistatin-like domain and an extracellular calcium binding E–F hand motif.

  4. Jun 1, 2010 · Many family researchers also fear that incorporating or focusing on biological explanations for behavior promote extreme views on biological reductionism, wherein social factors are ignored at the expense of biological explanations (Duster, 2006). Concerns about extreme biological reductionism are not unfounded, as some writers advancing ...

  5. Jun 16, 2023 · PARP proteins are typically involved in the modification of proteins and nucleic acids through mono or poly (ADP-ribosyl)ation, but this function can be modulated by the presence of various auxiliary protein domains. Our analysis provides a comprehensive view of the structured domains and long intrinsically disordered regions within human PARPs ...

  6. Jan 18, 2022 · The current research is still insufficient and many potential TFs are waiting to be discovered. In recent years, with the rise of whole genome sequencing, the whole genome characteristics of the MYB TF family have been completed in many plant species, which greatly promotes the research on the function of the MYB TF family, as shown in Table 1 ...

  7. The bromodomain-containing proteins in family IV include seven members (BRPF1, BRPF2, BRPF3, BRD7, BRD9, ATAD2, and ATAD2b). The bromodomains of each of these proteins recognize and bind acetyllysine residues on histone tails protruding from the nucleosome. However, the histone marks recognized by each bromodomain protein can be very different.

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