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  1. Article: Making nucleic acid structures and schematics.

    Lai, Lien B / Gopalan, Venkat / Jansson, Martin D / Chen, Qi / Zhang, Xudong / Wolfram-Schauerte, Maik / Höfer, Katharina

    Trends in biochemical sciences

    2023  Volume 48, Issue 8, Page(s) 655–658

    MeSH term(s) Software ; Nucleic Acids ; Nucleic Acid Conformation
    Chemical Substances Nucleic Acids
    Language English
    Publishing date 2023-07-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2023.05.005
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  2. Article: The many faces of RNA-based RNase P, an RNA-world relic.

    Phan, Hong-Duc / Lai, Lien B / Zahurancik, Walter J / Gopalan, Venkat

    Trends in biochemical sciences

    2021  Volume 46, Issue 12, Page(s) 976–991

    Abstract: RNase P is an essential enzyme that catalyzes removal of the 5' leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of ... ...

    Abstract RNase P is an essential enzyme that catalyzes removal of the 5' leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protein cofactors. Recent cryo-electron microscopy structures of representative archaeal and eukaryotic (nuclear) RNase P holoenzymes bound to tRNA substrate/product provide high-resolution detail on subunit organization, topology, and substrate recognition in these large, multisubunit catalytic RNPs. These structures point to the challenges in understanding how proteins modulate the RNA functional repertoire and how the structure of an ancient RNA-based catalyst was reshaped during evolution by new macromolecular associations that were likely necessitated by functional/regulatory coupling.
    MeSH term(s) Cryoelectron Microscopy ; Nucleic Acid Conformation ; RNA ; RNA, Catalytic/metabolism ; RNA, Transfer/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism
    Chemical Substances RNA, Catalytic ; RNA (63231-63-0) ; RNA, Transfer (9014-25-9) ; Ribonuclease P (EC 3.1.26.5)
    Language English
    Publishing date 2021-09-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2021.07.005
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  3. Article: Ribozyme-Mediated Downregulation Uncovers DNA Integrity Scanning Protein A (DisA) as a Solventogenesis Determinant in

    Ujor, Victor Chinomso / Lai, Lien B / Okonkwo, Christopher Chukwudi / Gopalan, Venkat / Ezeji, Thaddeus Chukwuemeka

    Frontiers in bioengineering and biotechnology

    2021  Volume 9, Page(s) 669462

    Abstract: Carbon catabolite repression (CCR) limits microbial utilization of lignocellulose-derived pentoses. To relieve CCR ... ...

    Abstract Carbon catabolite repression (CCR) limits microbial utilization of lignocellulose-derived pentoses. To relieve CCR in
    Language English
    Publishing date 2021-06-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2719493-0
    ISSN 2296-4185
    ISSN 2296-4185
    DOI 10.3389/fbioe.2021.669462
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  4. Article ; Online: Ramping Recombinant Protein Expression in Bacteria.

    Zahurancik, Walter J / Szkoda, Blake E / Lai, Lien B / Gopalan, Venkat

    Biochemistry

    2020  Volume 59, Issue 23, Page(s) 2122–2124

    MeSH term(s) Bacterial Proteins/genetics ; Enterobacter/genetics ; Escherichia coli/genetics ; Green Fluorescent Proteins/genetics ; Klebsiella oxytoca/genetics ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics ; Saccharomyces cerevisiae/genetics
    Chemical Substances Bacterial Proteins ; Recombinant Proteins ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2020-06-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00411
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    Zs.A 217: Show issues Location:
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  5. Article ; Online: Structural basis for impaired 5' processing of a mutant tRNA associated with defects in neuronal homeostasis.

    Lai, Lien B / Lai, Stella M / Szymanski, Eric S / Kapur, Mridu / Choi, Edric K / Al-Hashimi, Hashim M / Ackerman, Susan L / Gopalan, Venkat

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 10, Page(s) e2119529119

    Abstract: SignificanceUnderstanding and treating neurological disorders are global priorities. Some of these diseases are engendered by mutations that cause defects in the cellular synthesis of transfer RNAs (tRNAs), which function as adapter molecules that ... ...

    Abstract SignificanceUnderstanding and treating neurological disorders are global priorities. Some of these diseases are engendered by mutations that cause defects in the cellular synthesis of transfer RNAs (tRNAs), which function as adapter molecules that translate messenger RNAs into proteins. During tRNA biogenesis, ribonuclease P catalyzes removal of the transcribed sequence upstream of the mature tRNA. Here, we focus on a cytoplasmic tRNA
    MeSH term(s) Animals ; Base Pairing ; Cerebral Cortex/enzymology ; Homeostasis ; Magnesium/metabolism ; Mice ; Models, Molecular ; Neurons/metabolism ; Nucleic Acid Conformation ; Point Mutation ; Protein Processing, Post-Translational ; RNA, Transfer/chemistry ; RNA, Transfer/genetics ; RNA, Transfer/metabolism ; Ribonuclease P/isolation & purification ; Ribonuclease P/metabolism ; Substrate Specificity
    Chemical Substances RNA, Transfer (9014-25-9) ; Ribonuclease P (EC 3.1.26.5) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2022-03-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2119529119
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    Zs.A 1148: Show issues Location:
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  6. Article: Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein.

    Lai, Lien B / Phan, Hong-Duc / Zahurancik, Walter J / Gopalan, Venkat

    Trends in biochemical sciences

    2020  Volume 45, Issue 10, Page(s) 825–828

    Abstract: The high-resolution structures of yeast RNase for mitochondrial RNA processing (MRP), a catalytic ribonucleoprotein (RNP), recently reported by Lan et al. and Perederina et al. illustrate how RNA-mediated selection of alternative protein conformations, ... ...

    Abstract The high-resolution structures of yeast RNase for mitochondrial RNA processing (MRP), a catalytic ribonucleoprotein (RNP), recently reported by Lan et al. and Perederina et al. illustrate how RNA-mediated selection of alternative protein conformations, sampled during stochastic excursions by polymorphic/metamorphic proteins, enabled RNAs and proteins to mutually influence their functional repertoires and shape RNP evolution.
    MeSH term(s) Endoribonucleases/metabolism ; RNA ; RNA Precursors ; RNA Processing, Post-Transcriptional ; RNA, Ribosomal ; Ribonucleases ; Ribonucleoproteins/genetics ; Ribonucleoproteins/metabolism
    Chemical Substances RNA Precursors ; RNA, Ribosomal ; Ribonucleoproteins ; RNA (63231-63-0) ; Endoribonucleases (EC 3.1.-) ; Ribonucleases (EC 3.1.-) ; mitochondrial RNA-processing endoribonuclease (EC 3.1.-)
    Language English
    Publishing date 2020-09-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2020.08.002
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    Zs.A 1207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: RNAs undergo phase transitions with lower critical solution temperatures.

    Wadsworth, Gable M / Zahurancik, Walter J / Zeng, Xiangze / Pullara, Paul / Lai, Lien B / Sidharthan, Vaishnavi / Pappu, Rohit V / Gopalan, Venkat / Banerjee, Priya R

    Nature chemistry

    2023  Volume 15, Issue 12, Page(s) 1693–1704

    Abstract: Co-phase separation of RNAs and RNA-binding proteins drives the biogenesis of ribonucleoprotein granules. RNAs can also undergo phase transitions in the absence of proteins. However, the physicochemical driving forces of protein-free, RNA-driven phase ... ...

    Abstract Co-phase separation of RNAs and RNA-binding proteins drives the biogenesis of ribonucleoprotein granules. RNAs can also undergo phase transitions in the absence of proteins. However, the physicochemical driving forces of protein-free, RNA-driven phase transitions remain unclear. Here we report that various types of RNA undergo phase separation with system-specific lower critical solution temperatures. This entropically driven phase separation is an intrinsic feature of the phosphate backbone that requires Mg
    MeSH term(s) Temperature ; RNA ; RNA, Catalytic ; RNA-Binding Proteins ; Phosphates ; Phase Transition
    Chemical Substances RNA (63231-63-0) ; RNA, Catalytic ; RNA-Binding Proteins ; Phosphates
    Language English
    Publishing date 2023-11-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2464596-5
    ISSN 1755-4349 ; 1755-4330
    ISSN (online) 1755-4349
    ISSN 1755-4330
    DOI 10.1038/s41557-023-01353-4
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  8. Article ; Online: Reducing Falls Among Community-Dwelling Older Adults From Clinicians' Perspectives: A Systems Modeling Approach.

    Koh, Vanessa Jean Wen / Matchar, David B / Chan, Angelique Wei-Ming / Lee, June May-Ling / Lai, Wei Xuan / Rosario, Dulcie / George, Anne / Ho, Vanda / Ismail, Noor Hafizah Bte / Lien, Christopher Tsung Chien / Merchant, Reshma A / Tan, Shuyan Melissa / Wong, Chek Hooi / Xu, Tianma

    Innovation in aging

    2023  Volume 7, Issue 7, Page(s) igad077

    Abstract: Background and objectives: Falls among older adults are a significant health problem globally. Studies of multicomponent fall prevention programs in randomized controlled trials demonstrate effectiveness in reducing falls; however, the translation of ... ...

    Abstract Background and objectives: Falls among older adults are a significant health problem globally. Studies of multicomponent fall prevention programs in randomized controlled trials demonstrate effectiveness in reducing falls; however, the translation of research into the community remains challenging. Although there is an increasing interest to understand the factors contributing to implementation barriers, the dynamic relationships between factors are less well examined. Furthermore, evidence on implementation barriers from Asia is lacking as most of these studies originate from the West. As such, this study aims to engage stakeholders in uncovering the factors that facilitate or inhibit implementing community-based fall prevention programs in Singapore, with a focus on the interrelationship between those factors.
    Research design and methods: Health care professionals familiar with fall prevention programs were invited to discuss the enablers and challenges to the implementation. This effort was facilitated using a systems modeling methodology of Group Model Building (GMB) to share ideas and create a common conceptual model of the challenges. The GMB employs various engagement techniques to draw on the experiences and perceptions of all stakeholders involved.
    Results: This process led to the development of a Causal Loop Diagram (CLD), a qualitative conceptual model of the dynamic relationships between the barriers and facilitators of implementing fall prevention programs. Results from the CLD show that implementation is influenced by two main drivers: health care provider factors that influenced referrals, and patient factors that influenced referral acceptance and long-term adherence. Key leverage points for potential interventions were identified as well.
    Discussion and implications: The overall recommendation emphasized closer coordination and collaboration across providers to ensure sustainable and effective community-based fall prevention programs. This has to be supported by a national effort, involving a multidisciplinary stakeholder advisory group. These findings generated would be promising to guide future approaches to fall prevention.
    Language English
    Publishing date 2023-07-20
    Publishing country England
    Document type Journal Article
    ISSN 2399-5300
    ISSN (online) 2399-5300
    DOI 10.1093/geroni/igad077
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  9. Article: Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein

    Lai, Lien B / Phan, Hong-Duc / Zahurancik, Walter J / Gopalan, Venkat

    Trends in biochemical sciences. 2020 Oct., v. 45, no. 10

    2020  

    Abstract: The high-resolution structures of yeast RNase for mitochondrial RNA processing (MRP), a catalytic ribonucleoprotein (RNP), recently reported by Lan et al. and Perederina et al. illustrate how RNA-mediated selection of alternative protein conformations, ... ...

    Abstract The high-resolution structures of yeast RNase for mitochondrial RNA processing (MRP), a catalytic ribonucleoprotein (RNP), recently reported by Lan et al. and Perederina et al. illustrate how RNA-mediated selection of alternative protein conformations, sampled during stochastic excursions by polymorphic/metamorphic proteins, enabled RNAs and proteins to mutually influence their functional repertoires and shape RNP evolution.
    Keywords evolution ; mitochondrial RNA ; ribonucleases ; ribonucleoproteins ; yeasts
    Language English
    Dates of publication 2020-10
    Size p. 825-828.
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2020.08.002
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 78/716: Show issues

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  10. Article: The many faces of RNA-based RNase P, an RNA-world relic

    Phan, Hong-Duc / Lai, Lien B. / Zahurancik, Walter J. / Gopalan, Venkat

    Trends in biochemical sciences. 2021 Dec., v. 46, no. 12

    2021  

    Abstract: RNase P is an essential enzyme that catalyzes removal of the 5′ leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of ... ...

    Abstract RNase P is an essential enzyme that catalyzes removal of the 5′ leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protein cofactors. Recent cryo-electron microscopy structures of representative archaeal and eukaryotic (nuclear) RNase P holoenzymes bound to tRNA substrate/product provide high-resolution detail on subunit organization, topology, and substrate recognition in these large, multisubunit catalytic RNPs. These structures point to the challenges in understanding how proteins modulate the RNA functional repertoire and how the structure of an ancient RNA-based catalyst was reshaped during evolution by new macromolecular associations that were likely necessitated by functional/regulatory coupling.
    Keywords Archaea ; catalysts ; cryo-electron microscopy ; ribonucleases ; ribonucleoproteins ; ribozymes ; topology
    Language English
    Dates of publication 2021-12
    Size p. 976-991.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2021.07.005
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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