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NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure

Journal of structural and Functional Genomics 2005年第1期6卷 51-62页

作者： Hervé Du Penhoat, Catherine Li, Zhaohui Atreya, Hanudatta S. Kim, Seho Yee, Adelinda Xiao, Rong Murray, Diana Arrowsmith, Cheryl H. Szyperski, Thomas Department of Chemistry University of Buffalo State University of New York Buffalo NY 14260 United States Department of Microbiology and Immunology Institute for Computational Biomedicine B-314 Weill Medical College of Cornell University New York NY 10021 1300 York Avenue United States Division of Molecular and Structural Biology Ontario Cancer Institute Toronto Ont. Canada Department of Medical Biophysics University of Toronto Toronto Ont. Canada Center for Advanced Biotechnology and Medicine Department of Molecular Biology and Biochemistry Rutgers University Piscataway NJ 08854 679 Hoes Lane United States Northeast Structural Genomics Consortium Rutgers University Piscataway NJ 08854 610 Taylor Road United States Chemistry Department Rutgers University Piscataway NJ 08854 610 Taylor Road United States

The 150-residue protein TM1509 is encoded in gene YF09_THEMA of Thermotoga maritima. TM1509 has so far no functional annotation and belongs to protein family UPF0054 (PFAM accession number: PF02130) which contains at least 146 members. The NMR structure of TM1509 reveals an α+β fold comprising a four stranded β-sheet with topology A(↑), B(↑), D(↑), C(↓) as well as five α-helices I-V. The structures of most members of family PF02130 can be reliably constructed using the TM1509 NMR structure, demonstrating high leverage for exploration of fold space. A multiple sequence alignment of TM1509 with homologues of family UPF0054 shows that three polypeptide segments, as well as a putative zinc-binding consensus motif HGXLHLXGYDH located at the C-terminal end of α-helix IV, are highly conserved. The spatial arrangement of the three His residues of this UPF0054 consensus motif is similar to the arrangement found for the His residues in the HEXXHXXGXXH zinc-binding consensus motif of matrix metallo-proteases (MMPs). Moreover, the other conserved polypeptide segments form a large cavity which encloses the putative Zn-binding pocket and might confer specificity during catalysis. However, TM1509 and the other members of the UPF0054 family do not have the crucial Glu residue in position 2 of the MMP consensus motif. Intriguingly, the TM1509 structure indicates that the Asp in the UPF0054 consensus motif (Asp 111 in TM1509) may overtake the catalytic role of the Glu. This suggests that protein family UPF0054 might contain members of a hitherto uncharacterized class of metalloproteases. © Springer 2005.

关键词： Matrix metalloproteinase structural genomics Thermotoga maritima TM1509 UPF0054 Zinc-binding protein

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BPS2025 - Development and benchmarking of the open force field initiative self-consistent force field for proteins and small molecules

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Biophysical Journal 2025年第3期124卷 483a-484a页

作者： Chapin E. Cavender Pavan K. Behara Anika J. Friedman Joshua T. Horton Alexandra R. McIsaac Louis G. Smith Matthew W. Thompson Jeffrey Wagner Lily Wang Brent R. Westbrook John D. Chodera Daniel Cole David L. Mobley Michael R. Shirts Michael K. Gilson Skaggs School of Pharmacy and Pharmaceutical Sciences University of California San Diego La Jolla CA USA Center for Neurotherapeutics University of California Irvine Irvine CA USA Department of Chemical and Biological Engineering University of Colorado Boulder Boulder CO USA School of Natural and Environmental Sciences Newcastle University Newcastle upon Tyne United Kingdom Open Force Field Consortium Open Molecular Software Foundation Davis CA USA Department of Biochemistry and Biophysics University of Pennsylvania Philadelphia PA USA Computational & Systems Biology Program Memorial Sloan Kettering Cancer Center New York NY USA Department of Pharmaceutical Sciences and Department of Chemistry University of California Irvine Irvine CA USA

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Cryo-EM structure and biochemical analysis reveal the basis of the functional difference between human PI3KC3-C1 and-C2

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细胞研究（英文版） 2017年第8期27卷 989-1001页

作者： Meisheng Ma Jun-Jie Liu Yan Li Yuwei Huang Na Ta Yang Chen Hua Fu Ming-Da Ye Yuehe Ding Weijiao Huang Jia Wang Meng-Qiu Dong Li Yu Hong-Wei Wang The State Key Laboratory of Membrane Biology Tsinghua University-Peking University Joint Center for Life Sciences School of Life Sciences Tsinghua University Beijing 100084 China Molecular Biophysics and Integrated Bioimaging Division Lawrence Berkeley National Laboratory Berkeley CA 94720 USA Ministry of Education Key Laboratory of Protein Sciences Tsinghua-Peking Joint Center for Life Sciences Beijing Advanced Innovation Center for Structural Biology School of Life SciencesTsinghua University Beijing 100084 China The State Key Laboratory of Membrane Biology Tsinghua University-Peking University Joint Center for Life Sciences School of Life Sciences Tsinghua University Beijing 100084 China Joint Graduate Program of Peking-Tsinghua-National Institute of Biological Science Tsinghua University Beijing 100084 China MOH Key Laboratory of Systems Biology of Pathogens Institute of Pathogen Biology Chinese Academy of Medical Sciences & Peking Union Medical College Beijing 100730 China National Institute of Biological Sciences Beijing 102206 China

Phosphatidylinositol 3-phosphate (PI3P) plays essential roles in vesicular trafficking,organelle biogenesis and *** class Ⅲ phosphatidylinositol 3-kinase (PI3KC3) complexes have been identified in mammals,the ATG14L complex (PI3KC3-C1) and the UVRAG complex (PI3KC3-C2).PI3KC3-C1 is crucial for autophagosome biogenesis,and PI3KC3-C2 is involved in various membrane trafficking *** we report the cryo-EM structures of human PI3KC3-C1 and PI3KC3-C2 at sub-nanometer *** two structures share a common L-shaped overall architecture with distinct *** examination revealed that PI3KC3-C1 "stands up" on lipid monolayers,with the ATG14L BATs domain and the VPS34 C-terminal domain (CTD) directly contacting the *** dissection indicated that the ATG14L BATs domain is responsible for membrane anchoring,whereas the CTD of VPS34 determines the ***,PI3KC3-C2 binds much more weakly than PI3KC3-C1 to both PI-containing liposomes and purified endoplasmic reticulum (ER) vesicles,a property that is specifically determined by the ATG14L BATs *** in vivo ER localization analysis indicated that the BATs domain was required for ER localization of *** propose that the different lipid binding capacity is the key factor that differentiates the functions of PI3KC3-C1 and PI3KC3-C2 in autophagy.

关键词： PI3KC3 ATG14L UVRAG autophagy PI cryo-EM

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Microano-fabrication technologies for cell biology

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Medical & Biological Engineering & Computing 2010年第10期48卷 1023-1032页

作者： Qian, Tongcheng Wang, Yingxiao Department of Bioengineering and the Beckman Institute for Advanced Science and Technology University of Illinois at Urbana–Champaign Urbana USA Department of Biomedical Engineering Peking University Beijing People’s Republic of China Department of Integrative and Molecular Physiology Center for Biophysics and Computational Biology Institute for Genomic Biology Neuroscience Program University of Illinois at Urbana–Champaign Urbana USA

Micro/nano-fabrication techniques, such as soft lithography and electrospinning, have been well-developed and widely applied in many research fields in the past decade. Due to the low costs and simple procedures, these techniques have become important and popular for biological studies. In this review, we focus on the studies integrating micro/nano-fabrication work to elucidate the molecular mechanism of signaling transduction in cell biology. We first describe different micro/nano-fabrication technologies, including techniques generating three-dimensional scaffolds for tissue engineering. We then introduce the application of these technologies in manipulating the physical or chemical micro/nano-environment to regulate the cellular behavior and response, such as cell life and death, differentiation, proliferation, and cell migration. Recent advancement in integrating the micro/nano-technologies and live cell imaging are also discussed. Finally, potential schemes in cell biology involving micro/nano-fabrication technologies are proposed to provide perspectives on the future research activities.

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Distinct mechanisms of FAK mechanoactivation by different extracellular matrix proteins

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医用生物力学 2013年第S1期28卷 69-71页

作者： Jihye Seong Arash Tajik Jie Sun Jun-Lin Guan Martin J.Humphries Susan E.Craig Asha Shekaran Andrs J.García Ning Wang Yingxiao Wang Neuroscience Program University of Illinois Department of Mechanical Science and Engineering University of Illinois Department of Bioengineering & Beckman Institute for Advanced Science and Technology University of Illinois Division of Molecular Medicine and Genetics Departments of Internal Medicine and Cell & DevelopmentalBiologyUniversity of Michigan Medical School Wellcome Trust Centre for Cell-Matrix Research Faculty of Life SciencesUniversity of Manchester Woodruff School of Mechanical Engineering and Petit Institute for Bioengineering and Bioscience Georgia Institute of Technology Department of Biomedical Engineering School of Life Science and TechnologyHuazhong University of Science and Technology Department of Integrative and Molecular Physiology Center for Biophysics and Computational BiologyInstitute for Genomic BiologyUniversity of Illinois Department of Bioengineering University of California

Introduction Cells can sense and respond to the mechanical microenvironment by converting forces into biochemical signals inside the cells,***[1-3].Focal adhesions are the major sites of interaction between a cell and... 详细信息

Introduction Cells can sense and respond to the mechanical microenvironment by converting forces into biochemical signals inside the cells,***^[1-3].Focal adhesions are the major sites of interaction between a cell and its extracellular matrix（ECM）microenvironment,thus outside mechanical signals can be sensed at focal adhesions through transmembrane receptor *** particular,it has been shown that matrix elasticity can control the cell fate^[4]by modulating the interactions between ECM proteins and their receptor integrins^[5,6].For example,different rigidity of polyacrylamide（PA）gels can lead to different density of ECM ancho-

关键词： integrin converting transmembrane biochemical modulating elasticity rigidity polyacrylamide outside purchased

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ϕ-Value Analysis for Ultrafast Folding Proteins by NMR Relaxation Dispersion

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Journal of the American Chemical Society 2009年第2期132卷 450-451页

作者： Jae-Hyun Cho Nichole O’Connell Daniel P. Raleigh Arthur G. Palmer, III Department of Biochemistry and Molecular Biophysics Columbia University 630 West 168th Street New York New York 10032 and Department of Chemistry and Graduate Program in Biochemistry and Structural Biology State University of New York at Stony Brook Stony Brook New York 11794

Proteins that fold rapidly, on the (sub-) microsecond time scale, offer the prospect of direct comparison between experimental data and molecular dynamics simulations. However, experimental studies for such proteins frequently are hindered because folding rates are too fast to measure using conventional stopped-flow methods. To overcome this impediment, NMR spin relaxation dispersion experiments are used to quantify mutational effects on kinetics (ΔΔG°), stability (ΔΔG°), and ϕ-values (ΔΔG†/ΔΔG°) for proteins exhibiting chemical exchange line broadening that is fast on the NMR chemical shift time scale. The accuracy of ϕ-value analysis is enhanced because mutational effects on denatured or intermediate states can be detected through changes in line broadening. The transition and intermediate states of the villin headpiece domain, HP67, are characterized in varying solvent conditions to validate the method.

关键词： Kinetic parameters Genetics Colloids Quantum mechanics Nuclear magnetic resonance spectroscopy

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Identifying interaction sites in "Recalcitrant" proteins: Predicted protein and RNA binding sites in REV proteins of HIV-1 and EIAV agree with experimental data

Identifying interaction sites in "Recalcitrant" proteins: Pr...

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11th Pacific Symposium on Biocomputing 2006, PSB 2006

作者： Terribllini, Michael Lee, Jae-Hyung Yan, Changhui Jernigan, Robert L. Carpenter, Susan Honavar, Vasant Dobbs, Drena Bioinformatics and Computational Biology Graduate Program LH. Baker Center for Bioinformatics and Biological Statistics Iowa State University Ames IA 50010 United States Department of Computer Science Iowa State University Ames IA 50010 United States Department of Biochemistry Biophysics and Molecular Biology Iowa State University Ames IA 50010 United States Department of Genetics Development and Cell Biology Iowa State University Ames IA 50010 United States Artificial Intelligence Research Laboratory Center for Computational Intelligence Learning and Discovery Iowa State University Ames IA 50010 United States Department of Veterinary Microbiology and Pathology Washington State University Pullman WA. 99164 United States

ISBN: (纸本)9812564632

Protein-protein and protein nucleic acid interactions are vitally important for a wide range of biological processes, including regulation or gene expression, protein synthesis, and replication and assembly of many viruses. We have developed machine learning approaches for predicting which amino acids of a protein participate in its interactions with other proteins and/or nucleic acids, using only the proiein sequence as input. In this paper, we describe an application of classifiers trained on datasets of well-characterized protein-protein and protein-RNA complexes for which experimental structures are available. We apply these classifiers to the problem of predicting protein and RNA binding sites in the sequence of a clinically important protein for which the structure is not known: the regulatory protein Rev, essential for the replication of HIV-I and other lentiviruses. We compare our predictions with published biochemical, genetic and partial structural information for HIV-1 and EIAV Rev and with our own published experimental mapping of RNA binding sites in EIAV Rev. The predicted and experimentally determined binding sites are in very good agreement. The ability to predict reliably the residues of a protein that directly contribute to specific binding events - without the requirement for structural information regarding either the protein or complexes in which it participates - can potentially generate new disease intervention strategies.

关键词： Binding sites

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Causes of evolutionary divergence in prostate cancer

arXiv

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arXiv 2025年

作者： Esentürk, Emre Sahli, Atef Haberland, Valeriia Ziuboniewicz, Aleksandra Wirth, Christopher Bova, G. Steven Bristow, Robert G. Brook, Mark N. Brors, Benedikt Butler, Adam Cancel-Tassin, Géraldine Cheng, Kevin C.L. Cooper, Colin S. Corcoran, Niall M. Cussenot, Olivier Eeles, Ros A. Favero, Francesco Gerhauser, Clarissa Gihawi, Abraham Girma, Etsehiwot G. Gnanapragasam, Vincent J. Gruber, Andreas J. Hamid, Anis Hayes, Vanessa M. He, Housheng Hansen Hovens, Christopher M. Imada, Eddie Luidy Jakobsdottir, G. Maria Jung, Chol-Hee Khani, Francesca Kote-Jarai, Zsofia Lamy, Philippe Leeman, Gregory Loda, Massimo Lutsik, Pavlo Marchionni, Luigi Molania, Ramyar Papenfuss, Anthony T. Pellegrina, Diogo Pope, Bernard Queiroz, Lucio R. Rausch, Tobias Reimand, Jüri Robinson, Brian Schlomm, Thorsten Sørensen, Karina D. Uhrig, Sebastian Weischenfeldt, Joachim Xu, Yaobo Yamaguchi, Takafumi N. Zanettini, Claudio Lynch, Andy G. Wedge, David C. Brewer, Daniel S. Woodcock, Dan J. Nuffield Department of Medicine University of Oxford United Kingdom Manchester Cancer Research Centre The University of Manchester United Kingdom Norwich Medical School University of East Anglia United Kingdom Nuffield Department of Surgical Sciences University of Oxford United Kingdom Prostate Cancer Research Center Faculty of Medicine and Health Technology Tampere University Finland Manchester Cancer Research Centre Cancer Research UK Manchester Institute The University of Manchester United Kingdom Christie NHS Foundation Trust United Kingdom Div Cancer Sciences Faculty of Biology Medicine & Health University of Manchester United Kingdom The Institute of Cancer Research United Kingdom Germany Germany Medical Faculty Heidelberg Faculty of Biosciences Heidelberg University Germany Wellcome Sanger Institute United Kingdom France Sorbonne Université GRC n°5 Predictive Onco-Urology APHP Tenon Hospital France Computational Biology Program Ontario Institute for Cancer Research Canada Department of Medical Biophysics University of Toronto Canada Department of Urology Royal Melbourne Hospital Australia Department of Surgery The University of Melbourne Australia Department of Urology Western Health Australia The Royal Marsden NHS Foundation Trust London United Kingdom University of Copenhagen Denmark Finsen Laboratory Copenhagen University Hospital - Rigshospitalet Denmark Germany Cambridge Biomedical Campus Addenbrooke's Hospital Site S Wards Building United Kingdom University of Konstanz Germany School of Medical Sciences University of Sydney Faculty of Medicine & Health Australia School of Health Systems & Public Health University of Pretoria South Africa Manchester Cancer Research Centre University of Manchester United Kingdom Princess Margaret Cancer Centre University Health Network Department of Medical Biophysics University of Toronto Canada Department of Surgery The Collaborative Centre for Genomic Cancer Medicine The University of Melbourne

Cancer progression involves the sequential accumulation of genetic alterations that cumulatively shape the tumour phenotype. In prostate cancer, tumours can follow divergent evolutionary trajectories that lead to distinct subtypes, but the causes of this divergence remain unclear. While causal inference could elucidate the factors involved, conventional methods are unsuitable due to the possibility of unobserved confounders and ambiguity in the direction of causality. Here, we propose a method that circumvents these issues and apply it to genomic data from 829 prostate cancer patients. We identify several genetic alterations that drive divergence as well as others that prevent this transition, locking tumours into one trajectory. Further analysis reveals that these genetic alterations may cause each other, implying a positive-feedback loop that accelerates divergence. Our findings provide insights into how cancer subtypes emerge and offer a foundation for genomic surveillance strategies aimed at monitoring the progression of prostate cancer. © 2025, CC BY-NC-SA.

关键词： Lung cancer

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Fast, accurate, and versatile data analysis platform for the quantification of molecular spatiotemporal signals

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Cell 2025年第10期188卷 2794-2809.e21页

作者： Mi, Xuelong Chen, Alex Bo-Yuan Duarte, Daniela Carey, Erin Taylor, Charlotte R. Braaker, Philipp N. Bright, Mark Almeida, Rafael G. Lim, Jing-Xuan Ruetten, Virginia M.S. Wang, Yizhi Wang, Mengfan Zhang, Weizhan Zheng, Wei Reitman, Michael E. Huang, Yongkang Wang, Xiaoyu Li, Lei Deng, HanFei Shi, Song-Hai Poskanzer, Kira E. Lyons, David A. Nimmerjahn, Axel Ahrens, Misha B. Yu, Guoqiang Bradley Department of Electrical and Computer Engineering Virginia Polytechnic Institute and State University Arlington 22203 VA United States Janelia Research Campus Howard Hughes Medical Institute Ashburn 20147 VA United States Department of Molecular and Cellular Biology Harvard University Cambridge 02138 MA United States Graduate Program in Neuroscience Harvard Medical School Boston 02115 MA United States Waitt Advanced Biophotonics Center The Salk Institute for Biological Studies La Jolla 92037 CA United States Department of Biochemistry & Biophysics University of California San Francisco San Francisco CA United States Neuroscience Graduate Program University of California San Francisco San Francisco CA United States Centre for Discovery Brain Sciences University of Edinburgh Edinburgh BioQuarter Edinburgh EH16 4SB United Kingdom Gatsby Computational Neuroscience Unit UCL London W1T 4JG United Kingdom Kavli Institute for Fundamental Neuroscience San Francisco CA United States Department of Automation Tsinghua University Beijing 100084 China IDG/McGovern Institute for Brain Research Tsinghua University Beijing 100084 China New Cornerstone Science Laboratory Tsinghua-Peking Center for Life Sciences Beijing Frontier Research Center for Biological Structure School of Life Sciences Tsinghua University Beijing 100084 China State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science Institutes of Brain Science Fudan University Shanghai 200032 China Beijing National Research Center for Information Science and Technology Beijing 100084 China

Optical recording of intricate molecular dynamics is becoming an indispensable technique for biological studies, accelerated by the development of new or improved biosensors and microscopy technology. This creates major computational challenges to extract and quantify biologically meaningful spatiotemporal patterns embedded within complex and rich data sources, many of which cannot be captured with existing methods. Here, we introduce activity quantification and analysis (AQuA2), a fast, accurate, and versatile data analysis platform built upon advanced machine-learning techniques. It decomposes complex live-imaging-based datasets into elementary signaling events, allowing accurate and unbiased quantification of molecular activities and identification of consensus functional units. We demonstrate applications across a wide range of biosensors, cell types, organs, animal models, microscopy techniques, and imaging approaches. As exemplar findings, we show how AQuA2 identified drug-dependent interactions between neurons and astroglia, as well as distinct sensorimotor signal propagation patterns in the mouse spinal cord. © 2025 The Author(s)

关键词： AQuA2 astrocytes cell interaction analysis functional units glial cells image analysis machine learning molecular spatiotemporal signals neurons time-lapse imaging

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Origin of Overstretching Transitions in Single-Stranded Nucleic Acids

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Physical Review Letters 2013年第18期111卷 188302-188302页

作者： Zackary N. Scholl Mahir Rabbi David Lee Laura Manson Hanna S-Gracz Piotr E. Marszalek Program in Computational Biology and Bioinformatics Duke University Durham North Carolina 27708 USA Department of Mechanical Engineering and Materials Science Center for Biologically Inspired Materials and Material Systems Duke University Durham North Carolina 27708 USA Department of Molecular and Structural Biochemistry North Carolina State University Raleigh North Carolina 27708 USA

We combined single-molecule force spectroscopy with nuclear magnetic resonance measurements and molecular mechanics simulations to examine overstretching transitions in single-stranded nucleic acids. In single-stranded DNA and single-stranded RNA there is a low-force transition that involves unwinding of the helical structure, along with base unstacking. We determined that the high-force transition that occurs in polydeoxyadenylic acid single-stranded DNA is caused by the cooperative forced flipping of the dihedral angle formed between four atoms, O5’-C5’-C4’-C3’ (γ torsion), in the nucleic acid backbone within the canonical B-type helix. The γ torsion also flips under force in A-type helices, where the helix is shorter and wider as compared to the B-type helix, but this transition is less cooperative than in the B type and does not generate a high-force plateau in the force spectrums of A-type helices. We find that a similar high-force transition can be induced in polyadenylic acid single-stranded RNA by urea, presumably due to disrupting the intramolecular hydrogen bonding in the backbone. We hypothesize that a pronounced high-force transition observed for B-type helices of double stranded DNA also involves a cooperative flip of the γ torsion. These observations suggest new fundamental relationships between the canonical structures of single-and double-stranded DNA and the mechanism of their molecular elasticity.

关键词： NUCLEAR magnetic resonance spectroscopy SINGLE-stranded DNA NUCLEOTIDE sequence DEOXYRIBOSE ATOMIC force microscopy

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