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Journal articles on the topic 'Recombinant proteins Gold Protein binding'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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1

Breitwieser, Andreas, Philipp Siedlaczek, Helga Lichtenegger, Uwe B. Sleytr, and Dietmar Pum. "S-Layer Protein Coated Carbon Nanotubes." Coatings 9, no. 8 (2019): 492. http://dx.doi.org/10.3390/coatings9080492.

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Carbon nanotubes (CNTs) have already been considered for medical applications due to their small diameter and ability to penetrate cells and tissues. However, since CNTs are chemically inert and non-dispersible in water, they have to be chemically functionalized or coated with biomolecules to carry payloads or interact with the environment. Proteins, although often only randomly bound to the CNT surface, are preferred because they provide a better biocompatibility and present functional groups for binding additional molecules. A new approach to functionalize CNTs with a closed and precisely or

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2

Frevert, U., S. Sinnis, C. Cerami, and V. Nussenzweig. "Localization of cell-surface and basement-membrane heparan-sulfate proteoglycans using the malaria circumsporozoite protein." Proceedings, annual meeting, Electron Microscopy Society of America 52 (1994): 294–95. http://dx.doi.org/10.1017/s0424820100169201.

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Malaria sporozoites, which invade hepatocytes within minutes after transmission by an infected mosquito, are covered with the circumsporozoite (CS) protein, which in all Plasmodium species contains the conserved region II-plus. This region is also found as a cell-adhesive motif in a variety of host proteins like thrombospondin, properdin and the terminal complement components.The CS protein with its region II-plus specifically binds to heparan sulfate proteoglycans (HSPG) on the basolateral surface of hepatocytes in the space of Disse (FIG. 1), to certain basolateral cell membranes and basemen

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3

Ghitescu, L., Z. Galis, and M. Bendayan. "Protein AG-gold complex: an alternative probe in immunocytochemistry." Journal of Histochemistry & Cytochemistry 39, no. 8 (1991): 1057–65. http://dx.doi.org/10.1177/39.8.1856455.

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The purpose of this study was to evaluate the use of protein AG tagged with colloidal gold as a reliable immunocytochemical reagent. Protein AG is a recombinant of 47.3 KD molecular weight and pI = 4.3, which displays immunoglobulin Fc binding sites for both staphylococcal protein A and streptococcal protein G. It adsorbs to 10-nm colloidal gold particles with a lower affinity than does protein A, and is saturable. A maximal number of 12 protein AG molecules could be accommodated on the gold particle surface. Protein AG-gold conjugates yielded positive signals in post-embedding immunocytochemi

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Rezniczek, Günther A., José M. de Pereda, Siegfried Reipert та Gerhard Wiche. "Linking Integrin α6β4-based Cell Adhesion to the Intermediate Filament Cytoskeleton: Direct Interaction between the β4 Subunit and Plectin at Multiple Molecular Sites". Journal of Cell Biology 141, № 1 (1998): 209–25. http://dx.doi.org/10.1083/jcb.141.1.209.

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Recent studies with patients suffering from epidermolysis bullosa simplex associated with muscular dystrophy and the targeted gene disruption in mice suggested that plectin, a versatile cytoskeletal linker and intermediate filament-binding protein, may play an essential role in hemidesmosome integrity and stabilization. To define plectin's interactions with hemidesmosomal proteins on the molecular level, we studied its interaction with the uniquely long cytoplasmic tail domain of the β4 subunit of the basement membrane laminin receptor integrin α6β4 that has been implicated in connecting the t

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Molinková, D. "Purification of Escherichia coli-expressed HIS-tagged Maedi-Visna p25 core antigen by Ni2+-chelate affinity chromatography ." Veterinární Medicína 46, No. 2 (2001): 50–54. http://dx.doi.org/10.17221/7852-vetmed.

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In this study, recombinant histidine tagged p25 capsid protein of Maedi-Visna virus was developed. Part of the viral genome coding p25 protein was positioned downstream and in frame with a metal binding domain in pRSET-B vector. Recombinant protein was expressed in&nbsp;E. coli&nbsp;cells and soluble fraction of the protein was subsequently purified by Ni2+-chelate affinity chromatography. Purified protein was then used as antigen in an indirect ELISA test. One hundred fifty ovine serum samples were screened for antibodies to p25 protein of the virus. Immunoblot with whole virus antige

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6

GOBERT, G. N., D. J. STENZEL, M. K. JONES, and D. P. McMANUS. "Immunolocalization of the fatty acid-binding protein Sj-FABPc within adult Schistosoma japonicum." Parasitology 115, no. 1 (1997): 33–39. http://dx.doi.org/10.1017/s0031182097008925.

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This paper describes the first localization study of the 14·7 kDa fatty acid-binding protein in Schistosoma japonicum (Sj-FABPc) using transmission electron microscopy. A polyclonal antibody raised against recombinant Sj-FABPc was used in combination with a colloidal gold marker to determine the distribution of the protein within adult parasites. Sj-FABPc was localized within lipid droplets below the subtegumental region of the male parasite. Additionally, Sj-FABPc was present in the vitelline droplets of the vitelline glands of female parasites. There were no detectable levels of Sj-FABPc on

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7

Preobrazhenskaya, Y. V., A. I. Stenko, M. V. Shvarts, and V. Y. Lugovtsev. "Binding Stoichiometry of a Recombinant Selenophosphate Synthetase with One Synonymic Substitution E197D to a Fluorescent Nucleotide Analog of ATP, TNP-ATP." Journal of Amino Acids 2013 (January 30, 2013): 1–8. http://dx.doi.org/10.1155/2013/983565.

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The transformation of the strain DH5αTM-T1R with plasmid vector pET11a containing the cloned gene of bacterial selenophosphate synthetase (SPS), selD, from the E. coli BL21-Gold (DE3) strain gives an overproducing strain of SPS with one synonymic substitution, E197D. The transformation efficiency was estimated as 8 × 108 CFU/μg plasmid DNA. 28 mg of highly purified preparation of recombinant SPS capable of binding TNP-ATP was eluted from DEAE-Sephadex column in amount of 15 % from the total soluble protein in crude extract. The fluorescent derivative of ATP, 2′(3′)-O-(2,4,6-trinitrophenyl)aden

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8

Matsui, Hidehito, Hideaki Hanaki, Megumi Inoue, et al. "Development of an Immunochromatographic Strip for Simple Detection of Penicillin-Binding Protein 2′." Clinical and Vaccine Immunology 18, no. 2 (2010): 248–53. http://dx.doi.org/10.1128/cvi.00252-10.

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ABSTRACTInfections with methicillin-resistantStaphylococcus aureus(MRSA) and methicillin-resistant coagulase-negativeStaphylococcus(MR-CNS) are a serious problem in hospitals because these bacteria produce penicillin-binding protein 2′ (PBP2′ or PBP2a), which shows low affinity to β-lactam antibiotics. Furthermore, the bacteria show resistance to a variety of antibiotics. Identification of these pathogens has been carried out mainly by the oxacillin susceptibility test, which takes several days to produce a reliable result. We developed a simple immunochromatographic test that enabled the dete

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9

Heo, Yunseok, Hyeongseop Jeong, Youngki Yoo, et al. "Structural and Functional Characterizations of Cancer Targeting Nanoparticles Based on Hepatitis B Virus Capsid." International Journal of Molecular Sciences 22, no. 17 (2021): 9140. http://dx.doi.org/10.3390/ijms22179140.

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Cancer targeting nanoparticles have been extensively studied, but stable and applicable agents have yet to be developed. Here, we report stable nanoparticles based on hepatitis B core antigen (HBcAg) for cancer therapy. HBcAg monomers assemble into spherical capsids of 180 or 240 subunits. HBcAg was engineered to present an affibody for binding to human epidermal growth factor receptor 1 (EGFR) and to present histidine and tyrosine tags for binding to gold ions. The HBcAg engineered to present affibody and tags (HAF) bound specifically to EGFR and exterminated the EGFR-overexpressing adenocarc

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10

Gao, Jinlong, Daniele Vicari, Nan Li, and Charles Collyer. "Type II cleaved gingipain adhesins act in bacterial invasion." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C807. http://dx.doi.org/10.1107/s205327331409192x.

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Gingipains are multi domain peptidases that are primary virulence factors expressed by the keystone periodontal disease pathogen P. gingivalis. The adhesion regions of these proteases are multi-domain complexes that are comprised of a number of modules that belong to the type 1 (T1) family of gingipain adhesins (also known as cleaved adhesin domains). We have to date reported the crystal structures of three homologous variants of these 19 kDa T1 domains and shown that they recognise a number of host target proteins. We have proceeeded to predict from sequence analysis and binding data that in

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11

Thongkum, Weeraya, Umpa Yasamut, Koollawat Chupradit, et al. "Latticed Gold Nanoparticle Conjugation via Monomeric Streptavidin in Lateral Flow Assay for Detection of Autoantibody to Interferon-Gamma." Diagnostics 11, no. 6 (2021): 987. http://dx.doi.org/10.3390/diagnostics11060987.

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Adult-onset immunodeficiency syndrome (AOID) patients with autoantibodies (autoAbs) against interferon-gamma (IFN-γ) generally suffer from recurrent and recalcitrant disseminated non-tuberculous mycobacterial diseases. Since the early stages of AOID do not present specific symptoms, diagnosis and treatment of the condition are not practical. A simplified diagnostic method for differentiating AOID from other immunodeficiencies, such as HIV infection, was created. Anti-IFN-γ is generally identified using enzyme-linked immunosorbent assay (ELISA), which involves an instrument and a cumbersome pro

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12

Klassen, R. Bryan, Kimberly Crenshaw, Renata Kozyraki, et al. "Megalin mediates renal uptake of heavy metal metallothionein complexes." American Journal of Physiology-Renal Physiology 287, no. 3 (2004): F393—F403. http://dx.doi.org/10.1152/ajprenal.00233.2003.

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Although several heavy metal toxins are delivered to the kidney on the carrier protein metallothionein (MT), uncertainty as to how MT enters proximal tubular cells limits treatment strategies. Prompted by reports that MT-I interferes with renal uptake of the megalin ligand β2-microglobulin in conscious rats, we tested the hypothesis that megalin binds MT and mediates its uptake. Three lines of evidence suggest that binding of MT to megalin is critical in renal proximal tubular uptake of MT-bound heavy metals. First, MT binds megalin, but not cubilin, in direct surface plasmon resonance studies

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13

Sakaguchi, Nobuki, Michael T. Henzl, Isolde Thalmann, Ruediger Thalmann, and Bradley A. Schulte. "Oncomodulin Is Expressed Exclusively by Outer Hair Cells in the Organ of Corti." Journal of Histochemistry & Cytochemistry 46, no. 1 (1998): 29–39. http://dx.doi.org/10.1177/002215549804600105.

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Oncomodulin (OM) is a small, acidic calcium-binding protein first discovered in a rat hepatoma and later found in placental cytotrophoblasts, the pre-implantation embryo, and in a wide variety of neoplastic tissues. OM was considered to be exclusively an oncofetal protein until its recent detection in extracts of the adult guinea pig's organ of Corti. Here we report that light and electron microscopic immunostaining of gerbil, rat, and mouse inner ears with a monoclonal antibody against recombinant rat OM localizes the protein exclusively in cochlear outer hair cells (OHCs). At the ultrastruct

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14

Lower, Brian H., Liang Shi, Ruchirej Yongsunthon, Timothy C. Droubay, David E. McCready, and Steven K. Lower. "Specific Bonds between an Iron Oxide Surface and Outer Membrane Cytochromes MtrC and OmcA from Shewanella oneidensis MR-1." Journal of Bacteriology 189, no. 13 (2007): 4944–52. http://dx.doi.org/10.1128/jb.01518-06.

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ABSTRACT Shewanella oneidensis MR-1 is purported to express outer membrane cytochromes (e.g., MtrC and OmcA) that transfer electrons directly to Fe(III) in a mineral during anaerobic respiration. A prerequisite for this type of reaction would be the formation of a stable bond between a cytochrome and an iron oxide surface. Atomic force microscopy (AFM) was used to detect whether a specific bond forms between a hematite (Fe2O3) thin film, created with oxygen plasma-assisted molecular beam epitaxy, and recombinant MtrC or OmcA molecules coupled to gold substrates. Force spectra displayed a uniqu

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15

Zwier, Jurriaan M., Thomas Roux, Martin Cottet, et al. "A Fluorescent Ligand-Binding Alternative Using Tag-lite® Technology." Journal of Biomolecular Screening 15, no. 10 (2010): 1248–59. http://dx.doi.org/10.1177/1087057110384611.

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G-protein-coupled receptors (GPCRs) are crucial cell surface receptors that transmit signals from a wide range of extracellular ligands. Indeed, 40% to 50% of all marketed drugs are thought to modulate GPCR activity, making them the major class of targets in the drug discovery process. Binding assays are widely used to identify high-affinity, selective, and potent GPCR drugs. In this field, the use of radiolabeled ligands has remained so far the gold-standard method. Here the authors report a less hazardous alternative for high-throughput screening (HTS) applications by the setup of a nonradio

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16

Zhao, Lei, Jinjing Che, Qian Zhang, et al. "Identification of Novel Influenza Polymerase PB2 Inhibitors Using a Cascade Docking Virtual Screening Approach." Molecules 25, no. 22 (2020): 5291. http://dx.doi.org/10.3390/molecules25225291.

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To discover novel inhibitors that target the influenza polymerase basic protein 2 (PB2) cap-binding domain (CBD), commercial ChemBridge compound libraries containing 384,796 compounds were screened using a cascade docking of LibDock–LigandFit–GOLD, and 60 compounds were selected for testing with cytopathic effect (CPE) inhibition assays and surface plasmon resonance (SPR) assay. Ten compounds were identified to rescue cells from H1N1 virus-mediated death at non-cytotoxic concentrations with EC50 values ranging from 0.30 to 67.65 μM and could bind to the PB2 CBD of H1N1 with Kd values ranging f

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17

Pang, Jianan, Qiaofa Shi, Zhiqiang Liu, et al. "Resistin Induces Multidrug Resistance in Myeloma By Inhibiting Cell Death and Upregulating ABC Transporter Expression." Blood 128, no. 22 (2016): 5656. http://dx.doi.org/10.1182/blood.v128.22.5656.5656.

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Abstract Chemoresistance is a major hurdle in multiple myeloma. Most patients are prone to develop resistance to a wide spectrum of anticancer agents, significantly hampers the patients' long term outcome. Many studies point to bone marrow microenvironment as an important player in myeloma chemoresistance, in which marrow stromal cells and stromal-secreted soluble factors are shown to promote myeloma cell growth and survival. Our previous study has demonstrated that marrow-derived adipocytes protect myeloma cells against chemotherapy-induced apoptosis through adipocyte-secreted adipokines, one

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18

Behera, Sujit Kumar, Thankappan Sabarinath, Prasanta Kumar K. Mishra, et al. "Immunoinformatic Study of Recombinant LigA/BCon1-5 Antigen and Evaluation of Its Diagnostic Potential in Primary and Secondary Binding Tests for Serodiagnosis of Porcine Leptospirosis." Pathogens 10, no. 9 (2021): 1082. http://dx.doi.org/10.3390/pathogens10091082.

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Leptospirosis is responsible for hampering the productivity of swine husbandry worldwide. The aim of this study was to assess the efficacy of bioinformatics tools in predicting the three-dimensional structure and immunogenicity of recombinant LigBCon1-5 (rLigBCon1-5) antigen. A battery of bioinformatics tools such as I-TASSER, ProSA and SAVES v6.0 were used for the prediction and assessment of the predicted structure of rLigBCon1-5 antigen. Bepipred-2.0, DiscoTope v2.0 and ElliPro servers were used to predict linear and conformational epitopes while T-cell epitopes were predicted using NetMHCp

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Lai, Thung-S., Yusha Liu, Ho Young Lee, Eric Toone, and Charles S. Greenberg. "Human Tissue Transglutaminase Activity Is Inhibited by Protein Kinase Inhibitors: Potential Therapeutic Implication for Hematological Disorders." Blood 108, no. 11 (2006): 1614. http://dx.doi.org/10.1182/blood.v108.11.1614.1614.

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Abstract Tissue transglutaminase (TTG) is a multifunctional protein that plays a role in several different hematological processes. TTG is a unique member in transglutaminase gene family in that it exhibits multiple enzymatic properties including transglutaminase (TGase) and GTP/ATP hydrolysis activities. The Ca+2-dependent TGase activity catalyzes an isopeptide bond between a specific γ-glutamyl (Q) containing peptide and ε-amine group from a peptide-bound lysine (K) residue that functions to stabilize proteins and plays a role in wound healing, angiogenesis, cell proliferation, and apoptosis

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Pagani, S., F. Colombo, and C. Pitzalis. "POS0206 DESIGN AND CHARACTERISATION OF A THERAPEUTIC BISPECIFIC TANDEM scFv-Fc FUSION PROTEIN WITH ANTI-TNF AND SYNOVIUM-TARGETING SPECIFICITY FOR THE TREATMENT OF RHEUMATOID ARTHRITIS." Annals of the Rheumatic Diseases 80, Suppl 1 (2021): 319–20. http://dx.doi.org/10.1136/annrheumdis-2021-eular.3917.

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Background:Rheumatoid Arthritis (RA) is a systemic autoimmune disease with a prevalence of 0.5-1% worldwide1. Anti-cytokine antibodies, especially anti-Tumor Necrosis Factor (TNF) antibodies are considered the gold standard for RA therapy. However, there are some concerns regarding their lack of therapeutic efficacy in a significant proportion of patients2 and their potential systemic implications such as the risk of serious infections3. Developing novel agents with synovial targeting specificity might help to increase the therapeutic index while reducing systemic side effects of RA therapeuti

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Lupo, Maria Giovanna, Silvia Marchianò, Maria Pia Adorni, et al. "PCSK9 Induces Rat Smooth Muscle Cell Proliferation and Counteracts the Pleiotropic Effects of Simvastatin." International Journal of Molecular Sciences 22, no. 8 (2021): 4114. http://dx.doi.org/10.3390/ijms22084114.

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Human atherosclerotic plaque contains smooth muscle cells (SMCs) negative for the contractile phenotype (α-smooth muscle actin) but positive for proprotein convertase subtilisin/kexin type 9 (PCSK9). Thus, we generated rat SMCs which overexpressed human PCSK9 (SMCsPCSK9) with the aim of investigating the role of PCSK9 in the phenotype of SMCs. PCSK9 overexpression in SMCsPCSK9 led to a significant downregulation of the low-density lipoprotein receptor (Ldlr) as well as transgelin (Sm22α), a marker of the contractile phenotype. The cell proliferation rate of SMCsPCSK9 was significantly faster t

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Pecquet, Christian, Thomas Balligand, Ilyas Chachoua, et al. "Secreted Mutant Calreticulins As Rogue Cytokines Trigger Thrombopoietin Receptor Activation Specifically in CALR Mutated Cells: Perspectives for MPN Therapy." Blood 132, Supplement 1 (2018): 4. http://dx.doi.org/10.1182/blood-2018-99-118348.

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Abstract Background Mutant calreticulins carrying the sequence translated after a +1 frameshift at the C-terminus are major drivers of myeloproliferative neoplasms (MPNs). These mutant CALRs bind and activate TpoR/MPL in cells co-expressing TpoR and mutant CALRs, resulting in persistent JAK2-STAT5 signaling. Whether mutant CALR proteins are secreted, thus acting in trans on other cells, is not known. Aims Our objectives were to: 1) assess the direct TpoR-mutant CALR interaction both when expressed in the same or in different cells; 2) determine whether mutant CALRs are secreted; and 3) determi

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23

Morozova, Olga V., Olga N. Volosneva, Olga A. Levchenko, Nikolay A. Barinov, and Dmitry V. Klinov. "Protein Corona on Gold and Silver Nanoparticles." Materials Science Forum 936 (October 2018): 42–46. http://dx.doi.org/10.4028/www.scientific.net/msf.936.42.

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Gold or silver nanoparticles (NP) were covered with protein corona by: 1) direct binding with a number of proteins; 2) nanoprecipitation of proteins from their solutions in fluoroalcohols; 3) physisorption of proteins on the NP surface treated with poly (allylamine) s; 4) encapsulation of Ag or Au NP into SiO2 envelope and functionalization with organosilanes. Adsorption of proteins on surfaces of metal NP is reversible and up to 70% of the attached proteins can be eluted. Ag NP possess high affinity for binding with immunoglobulins and fibrinogens but not with any protein. Nanoprecipitation o

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Lira, André L., Rodrigo S. Ferreira, Ricardo J. S. Torquato, et al. "Binding kinetics of ultrasmall gold nanoparticles with proteins." Nanoscale 10, no. 7 (2018): 3235–44. http://dx.doi.org/10.1039/c7nr06810g.

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25

Pouw, R. B., M. C. Brouwer, C. M. Tang, D. Wouters, and T. W. Kuijpers. "Binding of recombinant factor H-related proteins to meningococcal factor H-binding protein." Molecular Immunology 56, no. 3 (2013): 313–14. http://dx.doi.org/10.1016/j.molimm.2013.05.205.

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De Roe, C., P. J. Courtoy, and P. Baudhuin. "A model of protein-colloidal gold interactions." Journal of Histochemistry & Cytochemistry 35, no. 11 (1987): 1191–98. http://dx.doi.org/10.1177/35.11.3655323.

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We prepared homogeneous populations of colloidal gold particles of various sizes. These were analyzed for size distribution and number of particles per unit volume. On exposure to increasing concentrations of insulin, myoglobin, protein A, peroxidase, serum albumin, galactosylated serum albumin, lactoferrin, transferrin, catalase, low-density lipoprotein, ferritin, and polymeric IgA, protein binding was a saturable process. Using serum albumin, we verified that a reversible equilibrium was reached within 15 minutes. Scatchard analysis of the interactions between all of these proteins and the g

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27

Huang, Li-Fen, Desyanti Saulina Sinaga, Chia-Chun Tan, Shu-Ju Micky Hsieh, and Chi-Hung Huang. "Expression of Recombinant Human Octamer-Binding Transcription Factor 4 in Rice Suspension Cells." International Journal of Molecular Sciences 22, no. 3 (2021): 1409. http://dx.doi.org/10.3390/ijms22031409.

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The rice cell suspension culture system is a good way to produce recombinant human proteins, owing to its high biosafety and low production cost. Human Octamer-binding Transcription Factor 4 (Oct4) is a fundamental transcription factor responsible for maintaining human pluripotent embryonic stem cells. Recombinant Oct4 protein has been used to induce pluripotent stem cells. In this study, recombinant Oct4 proteins are produced via a sugar starvation-inducible αAmy3/RAmy3D promoter–signal peptide-based rice recombinant protein expression system. Oct4 mRNAs accumulate in the transgenic rice susp

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Riggs, Paul. "Expression and Purification of Recombinant Proteins by Fusion to Maltose-Binding Protein." Molecular Biotechnology 15, no. 1 (2000): 51–63. http://dx.doi.org/10.1385/mb:15:1:51.

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Wong, Henry, and Anthony B. Schryvers. "Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe." Microbiology 149, no. 7 (2003): 1729–37. http://dx.doi.org/10.1099/mic.0.26281-0.

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Pathogenic bacteria in the family Neisseriaceae express surface receptors to acquire iron from the mammalian iron-binding proteins. Transferrins and lactoferrins constitute a family of iron-binding proteins highly related in both sequence and structure, yet the bacterial receptors are able to distinguish between these proteins and uphold a strict binding specificity. In order to understand the molecular basis for this specificity, the interaction between human lactoferrin (hLf) and the lactoferrin-binding protein A (LbpA) from Moraxella catarrhalis was studied. A periplasmic expression system

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Chan, K. W., M. N. Langan, J. L. Sui, et al. "A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins." Journal of General Physiology 107, no. 3 (1996): 381–97. http://dx.doi.org/10.1085/jgp.107.3.381.

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GTP-binding (G) proteins have been shown to mediate activation of inwardly rectifying potassium (K+) channels in cardiac, neuronal and neuroendocrine cells. Here, we report functional expression of a recombinant inwardly rectifying channel which we call KGP (or hpKir3.4), to signify that it is K+ selective, G-protein-gated and isolated from human pancreas. KGP expression in Xenopus oocytes resulted in sizeable basal (or agonist-independent) currents while coexpression with a G-protein-linked receptor, yielded additional agonist-induced currents. Coexpression of KGP and hGIRK1 (a human brain ho

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Kim, Y. W., G. A. Otterson, R. A. Kratzke, A. B. Coxon, and F. J. Kaye. "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein." Molecular and Cellular Biology 14, no. 11 (1994): 7256–64. http://dx.doi.org/10.1128/mcb.14.11.7256.

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The growth suppressor activities of the RB and p107 products are believed to be mediated by the reversible binding of a heterogeneous family of cellular proteins to a conserved T/E1A pocket domain that is present within both proteins. To study the functional role of these interactions, we examined the properties of cellular retinoblastoma binding protein 2 (RBP2) binding to RB, p107, and the related TATA-binding protein (TBP) product. We observed that although RBP2 bound exclusively to the T/E1A pocket of p107, it could interact with RB through independent T/E1A and non-T/E1A domains and with

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Kim, Y. W., G. A. Otterson, R. A. Kratzke, A. B. Coxon, and F. J. Kaye. "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein." Molecular and Cellular Biology 14, no. 11 (1994): 7256–64. http://dx.doi.org/10.1128/mcb.14.11.7256-7264.1994.

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The growth suppressor activities of the RB and p107 products are believed to be mediated by the reversible binding of a heterogeneous family of cellular proteins to a conserved T/E1A pocket domain that is present within both proteins. To study the functional role of these interactions, we examined the properties of cellular retinoblastoma binding protein 2 (RBP2) binding to RB, p107, and the related TATA-binding protein (TBP) product. We observed that although RBP2 bound exclusively to the T/E1A pocket of p107, it could interact with RB through independent T/E1A and non-T/E1A domains and with

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33

Hailman, E., H. S. Lichenstein, M. M. Wurfel, et al. "Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14." Journal of Experimental Medicine 179, no. 1 (1994): 269–77. http://dx.doi.org/10.1084/jem.179.1.269.

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CD14 is a 55-kD protein found as a glycosylphosphatidylinositol (GPI)-anchored protein on the surface of monocytes, macrophages, and polymorphonuclear leukocytes, and as a soluble protein in the blood. Both forms of CD14 participate in the serum-dependent responses of cells to bacterial lipopolysaccharide (LPS). While CD14 has been described as a receptor for complexes of LPS with LPS-binding protein (LBP), there has been no direct evidence showing whether a ternary complex of LPS, LBP, and CD14 is formed, or whether CD14 binds LPS directly. Using nondenaturing polyacrylamide gel electrophores

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Kannan, T. R., D. Provenzano, J. R. Wright, and J. B. Baseman. "Identification and Characterization of Human Surfactant Protein A Binding Protein of Mycoplasma pneumoniae." Infection and Immunity 73, no. 5 (2005): 2828–34. http://dx.doi.org/10.1128/iai.73.5.2828-2834.2005.

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ABSTRACT Mycoplasma pneumoniae infections represent a major primary cause of human respiratory diseases, exacerbate other respiratory disorders, and are associated with extrapulmonary pathologies. Cytadherence is a critical step in mycoplasma colonization, aided by a network of mycoplasma adhesins and cytadherence accessory proteins which mediate binding to host cell receptors. Furthermore, the respiratory mucosa is enriched with extracellular matrix components, including surfactant proteins, fibronectin, and mucin, which provide additional in vivo targets for mycoplasma parasitism. In this st

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Parker, F., F. Maurier, I. Delumeau, et al. "A Ras-GTPase-activating protein SH3-domain-binding protein." Molecular and Cellular Biology 16, no. 6 (1996): 2561–69. http://dx.doi.org/10.1128/mcb.16.6.2561.

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We report the purification of a Ras-GTPase-activating protein (GAP)-binding protein, G3BP, a ubiquitously expressed cytosolic 68-kDa protein that coimmunoprecipitates with GAP. G3BP physically associates with the SH3 domain of GAP, which previously had been shown to be essential for Ras signaling. The G3BP cDNA revealed that G3BP is a novel 466-amino-acid protein that shares several features with heterogeneous nuclear RNA-binding proteins, including ribonucleoprotein (RNP) motifs RNP1 and RNP2, an RG-rich domain, and acidic sequences. Recombinant G3BP binds effectively to the GAP SH3 domain G3

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EVANS, Gareth J. O., and Alan MORGAN. "Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I." Biochemical Journal 364, no. 2 (2002): 343–47. http://dx.doi.org/10.1042/bj20020123.

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The secretory vesicle cysteine string proteins (CSPs) are members of the DnaJ family of chaperones, and function at late stages of Ca2+-regulated exocytosis by an unknown mechanism. To determine novel binding partners of CSPs, we employed a pull-down strategy from purified rat brain membrane or cytosolic proteins using recombinant hexahistidine-tagged (His6-)CSP. Western blotting of the CSP-binding proteins identified synaptotagmin I to be a putative binding partner. Furthermore, pull-down assays using cAMP-dependent protein kinase (PKA)-phosphorylated CSP recovered significantly less synaptot

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Jin, Yu Fen, Yan Lei Li, Yan Hua, Xiao Gang Zhang, and Ting Yu. "Expression of Recombinant Human Cytomegalovirus Fusion Proteins pp150-pp65 Fragments and its Application." Advanced Materials Research 634-638 (January 2013): 1313–18. http://dx.doi.org/10.4028/www.scientific.net/amr.634-638.1313.

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Objective To evaluate the effectiveness of prokaryotic expression of fusion proteins pp150-pp65 of human cytomegalovirus (hCMV) for its application as antigen, the fusion protein of pp150-pp65 were expressed in prokaryotic expression system and purified by Ni-NTA affinity chromatography column for preparing the colloidal gold kit. Methods Using DNA from HCMV strain as template, the genes encoding pp150 and pp65 protein fragment were amplified by PCR technique, respectively. After confirmed by DNA sequence analysis, the recombinant plasmid pET28a-pp150-pp65 was transformed into E.Coil.BL21(DE3)

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Ro, Hyeon-Su, Sun Ok Jung, Byung Hoon Kho, et al. "Surface Plasmon Resonance Imaging-Based Protein Array Chip System for Monitoring a Hexahistidine-Tagged Protein during Expression and Purification." Applied and Environmental Microbiology 71, no. 2 (2005): 1089–92. http://dx.doi.org/10.1128/aem.71.2.1089-1092.2005.

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ABSTRACT A surface plasmon resonance imaging-based Ni2+-iminodiacetic acid-coated gold chip system was developed to enable specific detection of a hexahistidine-tagged recombinant protein in crude extracts or in column chromatography fractions. This system is especially advantageous for high-throughput analysis of multiple proteins.

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Tarcha, Eric J., Venkatesha Basrur, Chiung-Yu Hung, Malcolm J. Gardner, and Garry T. Cole. "Multivalent Recombinant Protein Vaccine against Coccidioidomycosis." Infection and Immunity 74, no. 10 (2006): 5802–13. http://dx.doi.org/10.1128/iai.00961-06.

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ABSTRACT Coccidioidomycosis is a human respiratory disease that is endemic to the southwestern United States and is caused by inhalation of the spores of a desert soilborne fungus. Efforts to develop a vaccine against this disease have focused on identification of T-cell-reactive antigens derived from the parasitic cell wall which can stimulate protective immunity against Coccidioides posadasii infection in mice. We previously described a productive immunoproteomic/bioinformatic approach to the discovery of vaccine candidates which makes use of the translated genome of C. posadasii and a compu

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Chang, Glenn T. G., Bart H. A. Maas, Hans K. Ploos van Amstel, Pieter H. Reitsma, Rogier M. Bertina, and Bonno N. Bouma. "Studies of the Interaction between Human Protein S and Human C4b-Binding Protein Using Deletion Variants of Recombinant Human Protein S." Thrombosis and Haemostasis 71, no. 04 (1994): 461–67. http://dx.doi.org/10.1055/s-0038-1642461.

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SummaryHuman protein S interacts noncovalently with human C4b-binding protein (C4BP). We have studied this interaction using deletion variants of recombinant human protein S. Two deletion variants were constructed by restriction enzyme digestion and in vitro site-specific mutagenesis of the human protein S cDNA. The variants were stably expressed in Cl27 cells. Recombinant proteins were purified using Fast Flow Q anion-exchange chromatography. The activated protein C (APC) cofactor activity, C4BP binding properties and reactivity to different monoclonal antibodies against human protein S were

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Lai, Meng-Yee, and Yee-Ling Lau. "Measurement of binding strength between prey proteins interacting with Toxoplasma gondii SAG1 and SAG2 using isothermal titration calorimetry (ITC)." Acta Parasitologica 63, no. 1 (2018): 106–13. http://dx.doi.org/10.1515/ap-2018-0012.

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Abstract Following the outcome from a previously performed yeast two-hybrid experiment, the binding strength between T. gondii SAG1 and SAG2 and their respective prey proteins were further confirmed in this study. The sag1, sag2 and their prey genes were amplified and cloned into a pGEMT vector. To express the recombinant proteins, the fragments were then subcloned into a pRSETA vector and transformed into E. coli BL21 (DE3) cells. The recombinant proteins were expressed optimally at 37°C and 1mM of IPTG. The 6X His-tag fusion proteins were purified, dialyzed and concentrated. To confirm the e

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Meesaragandla, Brahmaiah, Isabel García, Doreen Biedenweg, et al. "H-Bonding-mediated binding and charge reorganization of proteins on gold nanoparticles." Physical Chemistry Chemical Physics 22, no. 8 (2020): 4490–500. http://dx.doi.org/10.1039/c9cp06371d.

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Gold nanoparticles with various functionalities interact with the human serum albumin (HSA) leading to protein structural changes. HSA-nanoparticles bioconjugates display lower toxicity and slower cell uptake rates, compared to nanoparticles in the absence of protein.

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Cameron, Caroline E. "Identification of a Treponema pallidum Laminin-Binding Protein." Infection and Immunity 71, no. 5 (2003): 2525–33. http://dx.doi.org/10.1128/iai.71.5.2525-2533.2003.

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ABSTRACT Host extracellular matrix (ECM) components represent ideal microbial adhesion targets that many pathogens use for colonization of tissues and initiation of infection. This study investigated the interaction of the spirochete Treponema pallidum with the ECM component laminin. To identify candidate laminin-binding adhesins, the T. pallidum genome was analyzed to predict open reading frames that encode putative outer membrane proteins, as these proteins interact directly with host ECM components. Subsequent recombinant expression of these proteins and analysis of their laminin-binding po

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Masri, Heather P., and Cynthia Nau Cornelissen. "Specific Ligand Binding Attributable to Individual Epitopes of Gonococcal Transferrin Binding Protein A." Infection and Immunity 70, no. 2 (2002): 732–40. http://dx.doi.org/10.1128/iai.70.2.732-740.2002.

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ABSTRACT The gonococcal transferrin receptor complex comprises two iron-regulated proteins, TbpA and TbpB. TbpA is essential for transferrin-iron uptake and is a TonB-dependent integral outer membrane protein. TbpB is thought to increase the efficiency of iron uptake from transferrin and is lipid modified and surface exposed. To evaluate the structure-function relationships in one of the components of the receptor, TbpA, we created constructs that fused individual putative loops of TbpA with amino-terminal affinity tags. The recombinant proteins were then overexpressed in Escherichia coli, and

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KITAMURA, Yukari, Tadahiro KITAMURA, Hiroshi SAKAUE, et al. "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac." Biochemical Journal 322, no. 3 (1997): 873–78. http://dx.doi.org/10.1042/bj3220873.

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Bacterially expressed glutathione S-transferase fusion proteins containing Rac1 were used to identify binding proteins of this Rho family GTPase present in a bovine brain extract. Five proteins of 85, 110, 125, 140 and 170 kDa were detected, all of which were associated exclusively with guanosine 5´-[γ-thio]triphosphate-bound Rac1, not with GDP-bound Rac1. The 85 and 110 kDa proteins were identified as the regulatory and catalytic subunits respectively of phosphatidylinositol 3-kinase. Several lines of evidence suggested that the 125 kDa protein is identical with Nck-associated protein 1 (Nap1

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Liang, Hong, David L. Narum, Steven R. Fuhrmann, Tin Luu, and B. Kim Lee Sim. "A Recombinant Baculovirus-ExpressedPlasmodium falciparum Receptor-Binding Domain of Erythrocyte Binding Protein EBA-175 Biologically Mimics Native Protein." Infection and Immunity 68, no. 6 (2000): 3564–68. http://dx.doi.org/10.1128/iai.68.6.3564-3568.2000.

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ABSTRACT EBA-175 of Plasmodium falciparum is a merozoite ligand that binds its receptor glycophorin A on erythrocytes during invasion. The ligand-receptor interaction is dependent on sialic acids as well as the protein backbone of glycophorin A. Region II (RII) of EBA-175 has been defined as the receptor-binding domain. RII is divided into regions F1 and F2, which contain duplicated cysteine motifs. We expressed RII in a baculovirus and show that RII binds erythrocytes with a specificity identical to that of the native protein. We found that, consistent with the binding of erythrocytes to COS

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Liu, Hui, Yan-Li Ding, Wei Han, et al. "Recombinant scFv Antibodies against E Protein and N Protein of Severe Acute Respiratory Syndrome Virus." Acta Biochimica et Biophysica Sinica 36, no. 8 (2004): 541–47. http://dx.doi.org/10.1093/abbs/36.8.541.

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Abstract Three single chain antibodies (scFv) against the proteins of severe acute respiratory syndrome coronavirus (SARS-CoV) were isolated by phage display from an scFv antibody library. Bio-panning was carried out against immobilized purified envelope (E) and nucleocapsid (N) proteins of SARS-CoV. Their binding activity and specificity to E or N protein of SARS-CoV were characterized by phage-ELISA. Two of them, B10 and C20, could recognize non-overlapping epitopes of the E protein according to the two-site binding test result. Clone A17 could recognize N protein. The sequence of the epitop

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West, David, Karen Reddin, Mary Matheson, et al. "Recombinant Neisseria meningitidis Transferrin Binding Protein A Protects against Experimental Meningococcal Infection." Infection and Immunity 69, no. 3 (2001): 1561–67. http://dx.doi.org/10.1128/iai.69.3.1561-1567.2001.

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ABSTRACT To better characterize the vaccine potential of Neisseria meningitidis transferrin binding proteins (Tbps), we have overexpressed TbpA and TbpB from Neisseria meningitidisisolate K454 in Escherichia coli. The ability to bind human transferrin was retained by both recombinant proteins, enabling purification by affinity chromotography. The recombinant Tbps were evaluated individually and in combination in a mouse intraperitoneal-infection model to determine their ability to protect against meningococcal infection and to induce cross-reactive and bactericidal antibodies. For the first ti

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LIN, Wey-Jinq, Yaun-Fu CHANG, Wei-Li WANG та Chi-Ying F. HUANG. "Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Cα-binding protein rPICK1". Biochemical Journal 354, № 3 (2001): 635–43. http://dx.doi.org/10.1042/bj3540635.

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TIS21 is induced transiently by PMA and a number of extracellular stimuli. Yeast two-hybrid screening has identified three TIS21 interacting clones from a rat cDNA library [Lin, Gary, Yang, Clarke and Herschman (1996) J. Biol. Chem 271, 15034–15044]. The amino acid sequence deduced from clone 5A shows 96.9% identity with the murine PICK1, a protein kinase Cα (PKCα)-binding protein postulated to act as an intracellular receptor for PKC. A fusion protein of glutathione S-transferase and rPICK1 associates with the TIS21 translated in vitro, suggesting a direct physical interaction between these t

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Al Atalah, Bassam, Dieter Vanderschaeghe, Yehudi Bloch, et al. "Characterization of a type D1A EUL-related lectin from rice expressed in Pichia pastoris." Biological Chemistry 395, no. 4 (2014): 413–24. http://dx.doi.org/10.1515/hsz-2013-0267.

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Abstract OrysaEULD1A is one of the five EUL genes in rice (Oryza sativa) encoding a putative carbohydrate-binding protein belonging to the family of Euonymus related lectins (EUL). The OrysaEULD1A sequence comprises two highly similar EUL domains (91% sequence similarity and 72% sequence identity) separated by a 23 amino acid linker sequence and preceded by a 19 amino acid N-terminal sequence. In the present study, the full-length protein OrysaEULD1A as well as its individual domains OrysaEULD1A domain 1 and 2 were expressed in Pichiapastoris. After purification of the recombinant proteins, th

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