自引率: 1.2%
被引量: 5711
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审稿周期: 3.76
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Bioscience Reports provides a home for sound scientific research in all areas of cell biology and molecular life sciences.This fully Open Access journal publishes all papers under the liberal CC BY licence, giving the life science community quality research to share and discuss.Articles are assessed on soundness alone, providing a home for valid findings and data.We welcome papers that span disciplines (e.g. chemistry, medicine), including papers describing:new methodologiestools and reagents to probe biological questionsmechanistic detailsdisease mechanismsmetabolic processes and their regulationstructure and functionbioenergetics Open Access informationBioscience Reports is a full Open Access journal, and every article carries a Gold Open Access Article Publishing Charge (APC). All articles are published under a Creative Commons CC BY licence.Article Publishing Charges are:£820 (£575 discounted rate for Biochemical Society members and for authors who are from an institution that subscribes to a journal in the Portland Press portfolio)$1350 ($945 discounted rate for Biochemical Society members and for authors who are from an institution that subscribes to a journal in the Portland Press portfolio)
期刊描述简介:
Bioscience Reports provides a home for sound scientific research in all areas of cell biology and molecular life sciences. Since 2012, Bioscience Reports has been fully Open Access and publishes all papers under the liberal CC BY licence, giving the life science community quality research to share and discuss. Bioscience Reports adheres to the Budapest Open Access Initiative (BOAI) definition of open access: that users have the right to read, download, copy, distribute, print, search, or link to the full texts of open access articles published in the Journal.
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Asynchronous changes of hydrogen sulfide and its generating enzymes in most tissues with the aging process.
被引量：- 发表：2024
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MCM proteins are up-regulated in placentas of women with reduced insulin sensitivity.
被引量：- 发表：2024
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Retraction: MIR600HG suppresses metastasis and enhances oxaliplatin chemosensitivity by targeting ALDH1A3 in colorectal cancer.
被引量：- 发表：2024
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Retraction: Ultrasonic irradiation and SonoVue microbubbles-mediated RNA interfering targeting PRR11 inhibits breast cancer cells proliferation and metastasis but promotes apoptosis.
被引量：- 发表：2024
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Interaction with IP6K1 supports pyrophosphorylation of substrate proteins by the inositol pyrophosphate 5-InsP7.
Inositol pyrophosphates (PP-InsPs) are a sub-family of water soluble inositol phosphates that possess one or more diphosphate groups. PP-InsPs can transfer their β-phosphate group to a phosphorylated Ser residue to generate pyrophosphorylated Ser. This unique post-translational modification occurs on Ser residues that lie in acidic stretches within an intrinsically disordered protein sequence. Serine pyrophosphorylation is dependent on the presence of Mg2+ ions, but does not require an enzyme for catalysis. The mechanisms by which cells regulate PP-InsP-mediated pyrophosphorylation are still unknown. We performed mass spectrometry to identify interactors of IP6K1, an enzyme responsible for the synthesis of the PP-InsP 5-InsP7. Interestingly, IP6K1 interacted with several proteins that are known to undergo 5-InsP7-mediated pyrophosphorylation, including the nucleolar proteins NOLC1, TCOF and UBF1, and AP3B1, the β subunit of the AP3 adaptor protein complex. The IP6K1 interactome also included CK2, a protein kinase that phosphorylates Ser residues prior to pyrophosphorylation. We observe the formation of a protein complex between IP6K1, AP3B1, and the catalytic α-subunit of CK2, and show that disrupting IP6K1 binding to AP3B1 lowers its in vivo pyrophosphorylation. We propose that assembly of a substrate-CK2-IP6K complex would allow for coordinated pre-phosphorylation and pyrophosphorylation of the target serine residue, and provide a mechanism to regulate this enzyme-independent modification.
被引量：1 发表：2024
