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  1. Article ; Online: The critical importance of conditions: Reconciling GPCR functionality and biophysical findings.

    Reith, Melissa A / Rainey, Jan K

    Structure (London, England : 1993)

    2024  Volume 32, Issue 5, Page(s) 517–519

    Abstract: G-protein-coupled receptor (GPCR) activation relies on conformational sampling, a nuanced but functionally key behavior well suited to elucidation by nuclear magnetic resonance (NMR) spectroscopy. In this issue of Structure, Thakur et al. ...

    Abstract G-protein-coupled receptor (GPCR) activation relies on conformational sampling, a nuanced but functionally key behavior well suited to elucidation by nuclear magnetic resonance (NMR) spectroscopy. In this issue of Structure, Thakur et al.
    MeSH term(s) Receptors, G-Protein-Coupled/metabolism ; Receptors, G-Protein-Coupled/chemistry ; Humans ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Magnetic Resonance Spectroscopy/methods
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2024-04-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2024.04.007
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  2. Article ; Online: A recombinant chimeric spider pyriform-aciniform silk with highly tunable mechanical performance.

    Ghimire, Anupama / Xu, Lingling / Liu, Xiang-Qin / Rainey, Jan K

    Materials today. Bio

    2024  Volume 26, Page(s) 101073

    Abstract: Spider silks are natural protein-based biomaterials which are renowned for their mechanical properties and hold great promise for applications ranging from high-performance textiles to regenerative medicine. While some spiders can produce several ... ...

    Abstract Spider silks are natural protein-based biomaterials which are renowned for their mechanical properties and hold great promise for applications ranging from high-performance textiles to regenerative medicine. While some spiders can produce several different types of silks, most spider silk types - including pyriform and aciniform silks - are relatively unstudied. Pyriform and aciniform silks have distinct mechanical behavior and physicochemical properties, with materials produced using combinations of these silks currently unexplored. Here, we introduce an engineered chimeric fusion protein consisting of two repeat units of pyriform (Py) silk followed by two repeat units of aciniform (W) silk named Py
    Language English
    Publishing date 2024-04-27
    Publishing country England
    Document type Journal Article
    ISSN 2590-0064
    ISSN (online) 2590-0064
    DOI 10.1016/j.mtbio.2024.101073
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  3. Article ; Online: Structural features, intrinsic disorder, and modularity of a pyriform spidroin 1 core repetitive domain.

    Simmons, Jeffrey R / Gasmi-Seabrook, Geneviève / Rainey, Jan K

    Biochemistry and cell biology = Biochimie et biologie cellulaire

    2023  Volume 101, Issue 4, Page(s) 271–283

    Abstract: Orb-weaving spiders produce up to seven silk types, each with distinct biological roles, protein compositions, and mechanics. Pyriform (or piriform) silk is composed of pyriform spidroin 1 (PySp1) and is the fibrillar component of attachment discs that ... ...

    Abstract Orb-weaving spiders produce up to seven silk types, each with distinct biological roles, protein compositions, and mechanics. Pyriform (or piriform) silk is composed of pyriform spidroin 1 (PySp1) and is the fibrillar component of attachment discs that attach webs to substrates and to each other. Here, we characterize the 234-residue repeat unit (the "Py unit") from the core repetitive domain of
    MeSH term(s) Animals ; Fibroins/chemistry ; Silk/chemistry ; Spiders/chemistry ; Protein Conformation, alpha-Helical
    Chemical Substances spidroin 1 ; Fibroins (9007-76-5) ; Silk
    Language English
    Publishing date 2023-02-21
    Publishing country Canada
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 54104-7
    ISSN 1208-6002 ; 0829-8211
    ISSN (online) 1208-6002
    ISSN 0829-8211
    DOI 10.1139/bcb-2022-0338
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  4. Article ; Online: Localized apelin-17 analogue-bicelle interactions as a facilitator of membrane-catalyzed receptor recognition and binding.

    Phạm, Trần Thanh Tâm / Murza, Alexandre / Marsault, Éric / Frampton, John P / Rainey, Jan K

    Biochimica et biophysica acta. Biomembranes

    2024  Volume 1866, Issue 3, Page(s) 184289

    Abstract: The apelinergic system encompasses two peptide ligand families, apelin and apela, along with the apelin receptor (AR or APJ), a class A G-protein-coupled receptor. This system has diverse physiological effects, including modulating heart contraction, ... ...

    Abstract The apelinergic system encompasses two peptide ligand families, apelin and apela, along with the apelin receptor (AR or APJ), a class A G-protein-coupled receptor. This system has diverse physiological effects, including modulating heart contraction, vasodilation/constriction, glucose regulation, and vascular development, with involvement in a variety of pathological conditions. Apelin peptides have been previously shown to interact with and become structured upon binding to anionic micelles, consistent with a membrane-catalyzed mechanism of ligand-receptor binding. To overcome the challenges of observing nuclear magnetic resonance (NMR) spectroscopy signals of a dilute peptide in biological environments,
    MeSH term(s) Humans ; Apelin/metabolism ; Ligands ; HEK293 Cells ; Peptide Hormones/chemistry ; Catalysis
    Chemical Substances Apelin ; Ligands ; Peptide Hormones
    Language English
    Publishing date 2024-01-24
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2024.184289
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  5. Article ; Online: 1

    Song, Qinyan / Liu, Xiang-Qin / Rainey, Jan K

    Biomolecular NMR assignments

    2022  Volume 16, Issue 1, Page(s) 171–178

    Abstract: The human MDMX protein, also known as MDM4, plays a pivotal role in regulating the activity of the tumor suppressor protein p53 by restricting p53 transcriptional activity and stimulating the E3 ubiquitin ligase activity of another key regulatory protein, ...

    Abstract The human MDMX protein, also known as MDM4, plays a pivotal role in regulating the activity of the tumor suppressor protein p53 by restricting p53 transcriptional activity and stimulating the E3 ubiquitin ligase activity of another key regulatory protein, MDM2, to promote p53 degradation. MDMX is ubiquitously expressed in most tissue types and overexpression of MDMX has been implicated in many forms of cancer. MDMX has been shown to require an intact N-terminal p53-binding domain and C-terminal RING domain to exert inhibitory effects on p53. The presence of a tryptophan-rich sequence in the central acidic domain of MDMX has also been implicated in regulating the interaction between MDMX and p53, directly interacting with the p53 DNA-binding domain. To date, little structural information has been obtained for this acidic region of MDMX that encompasses the Trp-rich sequence. In order to gain insight into the structure and function of this region, we have carried out solution-state NMR spectroscopy studies utilizing the segment of MDMX spanning residues 181-300-with bounds specifically chosen through multiple sequence alignment-which encompasses nearly 25% of MDMX. Here, we report the
    MeSH term(s) Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Humans ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2/chemistry ; Proto-Oncogene Proteins c-mdm2/genetics ; Proto-Oncogene Proteins c-mdm2/metabolism ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ubiquitination
    Chemical Substances Cell Cycle Proteins ; MDM4 protein, human ; Proto-Oncogene Proteins ; Tumor Suppressor Protein p53 ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
    Language English
    Publishing date 2022-04-01
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-022-10081-8
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  6. Article ; Online: 1

    Song, Qinyan / Liu, Xiang-Qin / Rainey, Jan K

    Biomolecular NMR assignments

    2022  Volume 17, Issue 1, Page(s) 9–16

    Abstract: The human MDM2 protein regulates the tumor suppressor protein p53 by restricting its transcriptional activity and by promoting p53 degradation. MDM2 is ubiquitously expressed, with its overexpression implicated in many forms of cancer. The inhibitory ... ...

    Abstract The human MDM2 protein regulates the tumor suppressor protein p53 by restricting its transcriptional activity and by promoting p53 degradation. MDM2 is ubiquitously expressed, with its overexpression implicated in many forms of cancer. The inhibitory effects of MDM2 on p53 have been shown to involve its N-terminal p53-binding domain and its C-terminal RING domain. The presence of an intact central acidic domain of MDM2 has also been shown to regulate p53 ubiquitination, with this domain shown to directly interact with the p53 DNA-binding domain to regulate the DNA binding activity of p53. To date, little structural information has been obtained for the MDM2 acidic domain. Thus, to gain insight into the structure and function relationship of this region, we have applied solution-state NMR spectroscopy to characterize the segment of MDM2 spanning residues 215-300. These boundaries for the acidic domain were determined on the basis of consensus observed in multiple sequence alignment. Here, we report the
    MeSH term(s) Humans ; Proto-Oncogene Proteins c-mdm2/genetics ; Tumor Suppressor Protein p53/genetics ; Nuclear Magnetic Resonance, Biomolecular ; Ubiquitination ; Protein Binding ; DNA/metabolism
    Chemical Substances Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Tumor Suppressor Protein p53 ; DNA (9007-49-2) ; MDM2 protein, human (EC 2.3.2.27)
    Language English
    Publishing date 2022-10-29
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-022-10112-4
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  7. Article ; Online: The MDMX acidic domain competes with the p53 transactivation domain for MDM2 N-terminal domain binding.

    Song, Qinyan / Liu, Xiang-Qin / Rainey, Jan K

    Biochimica et biophysica acta. Molecular cell research

    2022  Volume 1869, Issue 10, Page(s) 119319

    Abstract: The tumor suppressor protein p53 governs many cellular pathways to control genome integrity, metabolic homeostasis, and cell viability. The critical roles of p53 highlight the importance of proper control over p53 in maintaining normal cellular function, ...

    Abstract The tumor suppressor protein p53 governs many cellular pathways to control genome integrity, metabolic homeostasis, and cell viability. The critical roles of p53 highlight the importance of proper control over p53 in maintaining normal cellular function, with the negative regulators MDM2 and MDMX playing central roles in regulating p53 activity. The interaction between p53 and either MDM2 or MDMX involves the p53 transactivation domain (p53TD) and the N-terminal domains (NTD) of MDM2 or MDMX. Recently, the acidic domain (AD) of MDMX was found to bind to its own NTD, inhibiting the p53-MDMX interaction. Given the established structural and functional similarity between the MDM2 and MDMX NTDs, we hypothesized that the MDMX AD would also directly bind to MDM2 NTD to inhibit p53-MDM2 interaction. Through solution-state nuclear magnetic resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC), we show that the MDMX AD can indeed directly interact with the MDM2 NTD and, as a result, can compete for p53 binding. The MDMX AD is thus able to serve as a regulatory domain to inhibit the MDM2-p53 interaction and may also play a direct role in p53 activation.
    MeSH term(s) Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-mdm2/genetics ; Proto-Oncogene Proteins c-mdm2/metabolism ; Transcriptional Activation ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances Nuclear Proteins ; Proto-Oncogene Proteins ; Tumor Suppressor Protein p53 ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
    Language English
    Publishing date 2022-06-30
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2022.119319
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  8. Article ; Online: Loading and Release of Quercetin from Contact-Drawn Polyvinyl Alcohol Fiber Scaffolds.

    Visser, Zachary B / Verma, Surendra Kumar / Rainey, Jan K / Frampton, John P

    ACS pharmacology & translational science

    2022  Volume 5, Issue 12, Page(s) 1305–1317

    Abstract: Polymeric drug releasing systems have numerous applications for the treatment of chronic diseases and traumatic injuries. In this study, a simple, cost-effective, and scalable method for dry spinning of crosslinked polyvinyl alcohol (PVA) fibers is ... ...

    Abstract Polymeric drug releasing systems have numerous applications for the treatment of chronic diseases and traumatic injuries. In this study, a simple, cost-effective, and scalable method for dry spinning of crosslinked polyvinyl alcohol (PVA) fibers is presented. This method utilizes an entangled solution of PVA to form liquid bridges that are drawn into rapidly drying fibers through extensional flow. The fibers are crosslinked by a one-pot reaction in which glyoxal is introduced to the PVA solution prior to contact drawing. Failure analysis of fiber formation is used to understand the interplay of polymer concentration, glyoxal concentration, and crosslinking time to identify appropriate formulations for the production of glyoxal-crosslinked PVA fibers. The small molecule quercetin (an anti-inflammatory plant flavonoid) can be added to the one-pot reaction and is shown to be incorporated into the fibers in a concentration-dependent manner. Upon rehydration in an aqueous medium, the glyoxal-crosslinked PVA fiber scaffolds retain their morphology and slowly degrade, as measured over the course of 10 days. As the scaffolds degrade, they release the loaded quercetin, reaching a cumulative release of 56 ± 6% of the loaded drug after 10 days. The bioactivity of the released quercetin is verified by combining quercetin-loaded fibers with contact-drawn polyethylene oxide-type I collagen (PEO-Col) fibers and monitoring the growth of PC12 cells on the fibers. PC12 cells readily attach to the PEO-Col fibers and display increased nerve growth factor-induced elongation and neurite formation in the presence of quercetin-loaded PVA fibers relative to substrates formed from only PEO-Col fibers or PEO-Col and PVA fibers without quercetin.
    Language English
    Publishing date 2022-11-29
    Publishing country United States
    Document type Journal Article
    ISSN 2575-9108
    ISSN (online) 2575-9108
    DOI 10.1021/acsptsci.2c00191
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  9. Article ; Online: On-cell nuclear magnetic resonance spectroscopy to probe cell surface interactions.

    Phạm, Trần Thanh Tâm / Rainey, Jan K

    Biochemistry and cell biology = Biochimie et biologie cellulaire

    2021  Volume 99, Issue 6, Page(s) 683–692

    Abstract: Nuclear magnetic resonance (NMR) spectroscopy allows the determination of atomic-level information on intermolecular interactions, molecular structure, and molecular dynamics in the cellular environment. This may be broadly divided into studies focused ... ...

    Abstract Nuclear magnetic resonance (NMR) spectroscopy allows the determination of atomic-level information on intermolecular interactions, molecular structure, and molecular dynamics in the cellular environment. This may be broadly divided into studies focused on obtaining detailed molecular information in the intracellular context ("in-cell") or those focused on characterizing molecules or events at the cell surface ("on-cell"). In this review, we outline some key NMR techniques applied for on-cell NMR studies through both solution- and solid-state NMR and survey studies that have used these techniques to uncover key information. In particular, we focus on the application of on-cell NMR spectroscopy to characterize ligand interactions with cell surface membrane proteins such as G-protein coupled receptors (GPCRs) and receptor tyrosine kinases. These techniques allow for quantification of binding affinities, competitive binding assays, delineation of ligands involved in binding, ligand bound-state conformational determination, evaluation of receptor structuring and dynamics, and inference of distance constraints characteristic of the ligand-receptor bound state. Interestingly, it is possible to avoid the barriers of production and purification of membrane proteins while obtaining directly physiologically relevant information through on-cell NMR. We also provide a brief survey of the applicability of on-cell NMR approaches to other classes of cell surface molecules.
    MeSH term(s) Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Receptors, G-Protein-Coupled/metabolism
    Chemical Substances Ligands ; Receptors, G-Protein-Coupled
    Language English
    Publishing date 2021-05-04
    Publishing country Canada
    Document type Journal Article ; Review
    ZDB-ID 54104-7
    ISSN 1208-6002 ; 0829-8211
    ISSN (online) 1208-6002
    ISSN 0829-8211
    DOI 10.1139/bcb-2021-0052
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  10. Article ; Online: Influence of elevated pressure and pressurized fluids on microenvironment and activity of enzymes.

    Kumar, Pawan / Kermanshahi-Pour, Azadeh / Brar, Satinder Kaur / He, Quan Sophia / Rainey, Jan K

    Biotechnology advances

    2023  Volume 68, Page(s) 108219

    Abstract: Enzymes have great potential in bioprocess engineering due to their green and mild reaction conditions. However, there are challenges to their application, such as enzyme extraction and purification costs, enzyme recovery, and long reaction time. ... ...

    Abstract Enzymes have great potential in bioprocess engineering due to their green and mild reaction conditions. However, there are challenges to their application, such as enzyme extraction and purification costs, enzyme recovery, and long reaction time. Enzymatic reaction rate enhancement and enzyme immobilization have the potential to overcome some of these challenges. Application of high pressure (e.g., hydrostatic pressure, supercritical carbon dioxide) has been shown to increase the activity of some enzymes, such as lipases and cellulases. Under high pressure, enzymes undergo multiple alterations simultaneously. High pressure reduces the bond lengths of molecules of reaction components and causes a reduction in the activation volume of enzyme-substrate complex. Supercritical CO
    MeSH term(s) Enzymes, Immobilized/chemistry ; Lipase/chemistry ; Water ; Carbon Dioxide/chemistry
    Chemical Substances Enzymes, Immobilized ; Lipase (EC 3.1.1.3) ; Water (059QF0KO0R) ; Carbon Dioxide (142M471B3J)
    Language English
    Publishing date 2023-07-23
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 47165-3
    ISSN 1873-1899 ; 0734-9750
    ISSN (online) 1873-1899
    ISSN 0734-9750
    DOI 10.1016/j.biotechadv.2023.108219
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