The Journal of Biological Chemistry welcomes high-quality science that seeks to elucidate the molecular and cellular basis of biological processes. Papers published in JBC can therefore fall under the umbrellas of not only biological chemistry, chemical biology, or biochemistry, but also allied disciplines such as biophysics, systems biology, RNA biology, immunology, microbiology, neurobiology, epigenetics, computational biology, ’omics, and many more. The outcome of our focus on papers that contribute novel and important mechanistic insights, rather than on a particular topic area, is that JBC is truly a melting pot for scientists across disciplines. In addition, JBC welcomes papers that describe methods that will help scientists push their biochemical inquiries forward and resources that will be of use to the research community.
生物化学杂志欢迎高质量的科学,寻求阐明生物过程的分子和细胞基础。因此,在JBC发表的论文不仅可以归入生物化学、化学生物学或生物化学,还可以归入相关学科,如生物物理学、系统生物学、RNA生物学、免疫学、微生物学、神经生物学、表观遗传学、计算生物学、组学等。我们专注于那些贡献新颖和重要的机械学见解的论文,而不是专注于某个特定的主题领域,结果是JBC确实是跨学科科学家的熔炉。此外,JBC欢迎描述方法的论文,这些方法将有助于科学家推动他们的生物化学研究向前发展,并提供对研究界有用的资源。
The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6N3D/PDB
A conserved and buried edge-to-face aromatic interaction in small ubiquitin-like modifier (SUMO) has a role in SUMO stability and function.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6J4I/PDB
Two complementary alpha-fucosidases fromStreptococcus pneumoniaepromote complete degradation of host-derived carbohydrate antigens.
来源期刊:Journal of Biological ChemistryDOI:10.2210/pdb6orh/pdb
A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6DO7/PDB
Structural analysis of a vibrio phospholipase reveals an unusual Ser-His-chloride catalytic triad.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6JL0/PDB
Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6O11/PDB
Identification of functionally important residues and structural features in a bacterial lignostilbene dioxygenase.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6OJT/PDB
Molecular and structural basis of nucleoside diphosphate kinase-mediated regulation of spore and sclerotia development in the fungusAspergillus flavus.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6K3H/PDB
Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6OND/PDB
Engineering nanomolar peptide ligands that differentially modulate EphA2 receptor signaling
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6NKP/PDB
Productive reorientation of a bound oxime reactivator revealed in room-temperature X-ray structures of native and VX-inhibited human acetylcholinesterase.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6O66/PDB
X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1‐deoxy‐d‐xylulose 5-phosphate synthase reaction coordinate.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6OUV/PDB
Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6N20/PDB
Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6AHF/PDB
Structural insights into the catalytic mechanism of lovastatin hydrolase
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6KJC/PDB
The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6OK1/PDB
Structural basis of the target-binding mode of the G protein-coupled receptor kinase-interacting protein in the regulation of focal adhesion dynamics.
来源期刊:Journal of Biological ChemistryDOI:10.2210/PDB6IUI/PDB