Identification and functional characterization of a type�I signal peptidase gene of Bacillus megaterium DSM319

2004 ◽  
Vol 64 (2) ◽  
pp. 243-249 ◽  
Author(s):  
H. Nahrstedt ◽  
K.- D. Wittchen ◽  
M. A. Rachman ◽  
F. Meinhardt
Keyword(s):  
Bacillus Megaterium ◽  
Functional Characterization ◽  
Signal Peptidase ◽  
Type I

scholarly journals Functional Characterization of a Redundant Plasmodium TRAP Family Invasin, TRAP-Like Protein, by Aldolase Binding and a Genetic Complementation Test

2008 ◽  
Vol 7 (6) ◽  
pp. 1062-1070 ◽  
Author(s):  
Kirsten Heiss ◽  
Hui Nie ◽  
Sumit Kumar ◽  
Thomas M. Daly ◽  
Lawrence W. Bergman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Cell Entry ◽  
Host Cells ◽  
Complementation Test ◽  
Type I ◽  
Cycle Progression ◽  
Targeted Gene Disruption ◽  
Specific Host ◽  
Host Cell Entry

ABSTRACT Efficient and specific host cell entry is of exquisite importance for intracellular pathogens. Parasites of the phylum Apicomplexa are highly motile and actively enter host cells. These functions are mediated by type I transmembrane invasins of the TRAP family that link an extracellular recognition event to the parasite actin-myosin motor machinery. We systematically tested potential parasite invasins for binding to the actin bridging molecule aldolase and complementation of the vital cytoplasmic domain of the sporozoite invasin TRAP. We show that the ookinete invasin CTRP and a novel, structurally related protein, termed TRAP-like protein (TLP), are functional members of the TRAP family. Although TLP is expressed in invasive stages, targeted gene disruption revealed a nonvital role during life cycle progression. This is the first genetic analysis of TLP, encoding a redundant TRAP family invasin, in the malaria parasite.

Evaluation of an enzyme immunoassay kit for estrogen receptor measurement--report II.

1988 ◽  
Vol 34 (10) ◽  
pp. 2053-2057 ◽  
Author(s):  
S Raam ◽  
D M Vrabel
Keyword(s):  
Enzyme Immunoassay ◽  
Binding Sites ◽  
Solid Phase ◽  
Functional Characterization ◽  
Quantitative Agreement ◽  
Type I ◽  
Type Ii ◽  
Immunoreactive Protein ◽  
Estrogen Binding

Abstract We present evidence to show that monoclonal antibodies to estrogen receptors (ER) in solid phase recognize the secondary estrogen binding sites with moderate to low affinity for estradiol (E2). An excellent quantitative agreement was found in five cytosols between the ER values obtained by the enzyme immunoassay (ER-EIA) and the amount of secondary estrogen binding sites measured by the assay involving dextran-coated charcoal (Clin Chem 1986;32:1496). The immunoreactive protein recognized by the antibody-coated beads, when allowed to react with ER(+) cytosols, is shown to bind [3H]estradiol only when the ligand concentration exceeds 8 nmol/L. Further biochemical and functional characterization of the immunoreactive protein is required to establish similarities/dissimilarities between this protein, high-affinity Type I ER sites, and the secondary sites such as Type II sites.

scholarly journals Isolation and Characterization of Type I Signal Peptidase of Different Malaria Parasites

2005 ◽  
Vol 2005 (4) ◽  
pp. 301-309 ◽  
Author(s):  
Sutikshan Sharma ◽  
Arun Pradhan ◽  
Virander S. Chauhan ◽  
Renu Tuteja
Keyword(s):  
Signal Peptidase ◽  
Type I ◽  
Malaria Parasites ◽  
Isolation And Characterization

Expression and biochemical characterization of a novel type I pullulanase from Bacillus megaterium

2016 ◽  
Vol 39 (3) ◽  
pp. 397-405 ◽  
Author(s):  
Shaoqing Yang ◽  
Qiaojuan Yan ◽  
Qingdan Bao ◽  
Jingjing Liu ◽  
Zhengqiang Jiang
Keyword(s):  
Bacillus Megaterium ◽  
Biochemical Characterization ◽  
Type I

Molecular cloning and functional characterization of two duplicated two-cysteine containing type I interferon genes in rock bream Oplegnathus fasciatus

2012 ◽  
Vol 33 (4) ◽  
pp. 886-898 ◽  
Author(s):  
Qiang Wan ◽  
W.D. Niroshana Wicramaarachchi ◽  
Ilson Whang ◽  
Bong-Soo Lim ◽  
Myung-Joo Oh ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Type I Interferon ◽  
Functional Characterization ◽  
Type I ◽  
Oplegnathus Fasciatus ◽  
Rock Bream

scholarly journals THE FUNCTIONAL E1–E2 HETERODIMER HCV GLYCOPROTEINS

2018 ◽  
Vol 21 (05) ◽  
pp. 829-840
Author(s):  
Hamid Mahmood ◽  
Nasir Zulfiqar ◽  
Ghazia Irfan ◽  
Hashim Riaz ◽  
Ammara Waqar ◽  
...  
Keyword(s):  
Culture System ◽  
Viral Particle ◽  
Particle Production ◽  
Signal Peptidase ◽  
Envelope Glycoproteins ◽  
Type I ◽  
Cell Culture System ◽  
Viral Particle Production ◽  
Long Time

Introduction: The two HCV envelope glycoproteins E1 and E2 are released fromHCV polyprotein by signal peptidase cleavages. These glycoproteins are type I transmembraneproteins with a highly glycosylated N-terminal ectodomain and a C-terminal hydrophobicanchor. Methods and pathways: After their synthesis, HCV glycoproteins E1 and E2 associateas a non covalent heterodimer. The transmembrane domains of HCV envelope glycoproteinsplay a major role in E1–E2 heterodimer assembly and subcellular localization. The envelopeglycoprotein complex E1–E2 has been proposed to be essential for HCV entry. Results andconclusions: However, for a long time, HCV entry studies have been limited by the lack of arobust cell culture system for HCV replication and viral particle production. Recently, a modelmimicking the entry process of HCV lifecycle has been developed by pseudo typing retroviralparticles with native HCV envelope glycoproteins, allowing the characterization of functionalE1–E2 envelope glycoproteins., we review our understanding to date on the assembly of thefunctional HCV glycoprotein heterodimer.

scholarly journals Characterization of Functional Human Skeletal Myotubes and Neuromuscular Junction Derived—From the Same Induced Pluripotent Stem Cell Source

2020 ◽  
Vol 7 (4) ◽  
pp. 133
Author(s):  
Xiufang Guo ◽  
Agnes Badu-Mensah ◽  
Michael C. Thomas ◽  
Christopher W. McAleer ◽  
James J. Hickman
Keyword(s):  
Stem Cell ◽  
Pluripotent Stem Cell ◽  
Disease Modeling ◽  
Neuromuscular Junctions ◽  
Functional Characterization ◽  
Induced Pluripotent Stem Cell ◽  
Patient Specific ◽  
Type I ◽  
Induced Pluripotent

In vitro generation of functional neuromuscular junctions (NMJs) utilizing the same induced pluripotent stem cell (iPSC) source for muscle and motoneurons would be of great value for disease modeling and tissue engineering. Although, differentiation and characterization of iPSC-derived motoneurons are well established, and iPSC-derived skeletal muscle (iPSC-SKM) has been reported, there is a general lack of systemic and functional characterization of the iPSC-SKM. This study performed a systematic characterization of iPSC-SKM differentiated using a serum-free, small molecule-directed protocol. Morphologically, the iPSC-SKM demonstrated the expression and appropriate distribution of acetylcholine, ryanodine and dihydropyridine receptors. Fiber type analysis revealed a mixture of human fast (Type IIX, IIA) and slow (Type I) muscle types and the absence of animal Type IIB fibers. Functionally, the iPSC-SKMs contracted synchronously upon electrical stimulation, with the contraction force comparable to myofibers derived from primary myoblasts. Most importantly, when co-cultured with human iPSC-derived motoneurons from the same iPSC source, the myofibers contracted in response to motoneuron stimulation indicating the formation of functional NMJs. By demonstrating comparable structural and functional capacity to primary myoblast-derived myofibers, this defined, iPSC-SKM system, as well as the personal NMJ system, has applications for patient-specific drug testing and investigation of muscle physiology and disease.

scholarly journals Functional Characterization of a WWP1/Tiul1 Tumor-derived Mutant Reveals a Paradigm of Its Constitutive Activation in Human Cancer

2015 ◽  
Vol 290 (34) ◽  
pp. 21007-21018 ◽  
Author(s):  
Thomas Courivaud ◽  
Nathalie Ferrand ◽  
Abdelouahid Elkhattouti ◽  
Santosh Kumar ◽  
Laurence Levy ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Cell Function ◽  
Regulatory Mechanism ◽  
Human Cancer ◽  
Functional Characterization ◽  
Type I ◽  
Inhibitory Effects ◽  
Cancer Pathogenesis ◽  
Ubiquitin Ligase Activity

Although E3 ubiquitin ligases are deemed to play key roles in normal cell function and homeostasis, whether their alterations contribute to cancer pathogenesis remains unclear. In this study, we sought to investigate potential mechanisms that govern WWP1/Tiul1 (WWP1) ubiquitin ligase activity, focusing on its ability to trigger degradation of TGFβ type I receptor (TβRI) in conjunction with Smad7. Our data reveal that the WWP1 protein is very stable at steady states because its autopolyubiquitination activity is silenced due to an intra-interaction between the C2 and/or WW and Hect domains that favors WWP1 monoubiquitination at the expense of its polyubiquitination or polyubiquitination of TβRI. Upon binding of WWP1 to Smad7, this functional interplay is disabled, switching its monoubiquitination activity toward a polyubiquitination activity, thereby driving its own degradation and that of TβRI as well. Intriguingly, a WWP1 point mutation found in human prostate cancer disrupts this regulatory mechanism by relieving the inhibitory effects of C2 and WW on Hect and thereby causing WWP1 hyperactivation. That cancer-driven alteration of WWP1 culminates in excessive TβRI degradation and attenuated TGFβ cytostatic signaling, a consequence that could conceivably confer tumorigenic properties to WWP1.

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