منابع مشابه
Using Recombinant Chlamydia Major Outer Membrane Protein (MOMP) in ELISA Diagnostic Kit
Chlamydia trachomatis is one of the main causes of Sexually Transmitted Diseases (STDs) such as prostatitis and epididymitis in men and cervicitis, endometriosis, vaginitis and ureogenital tract infections in women. Serological tests with sensitivities related to specific antigens are commonly used as routine laboratory tests for diagnosis of Chlamydia. In this research the Chlamydia Major O...
متن کاملCloning and expression of Brucella outer membrane protein 36kDa (OMP2b) in E. coli
Background & Objective: Brucellosis is an important zoonotic disease of economic significance. Brucella species are gram-negative, facultative intracellular bacteria, and are capable of replicating in the phagosomes of macrophages. They cause infection in several animal species and humans. Prevention of new diseases and diagnosis of cases infected with the organism are both essential for eradic...
متن کاملHelicobacter pylori Outer Membrane Protein-Related Pathogenesis
Helicobacter pylori colonizes the human stomach and induces inflammation, and in some cases persistent infection can result in gastric cancer. Attachment to the gastric mucosa is the first step in establishing bacterial colonization, and outer membrane proteins (OMPs) play a pivotal role in binding to human cells. Some OMP interaction molecules are known in H. pylori, and their associated host ...
متن کاملThe Outer Mitochondrial Membrane Protein mitoNEET
Received for publication, May 31, 2007, and in revised form, June 20, 2007 Published, JBC Papers in Press, June 21, 2007, DOI 10.1074/jbc.C700107200 Sandra E. Wiley, Mark L. Paddock, Edward C. Abresch, Larry Gross, Peter van der Geer , Rachel Nechushtai**, Anne N. Murphy, Patricia A. Jennings, and Jack E. Dixon From the Departments of Pharmacology, Physics, Chemistry and Biochemistry, and Cellu...
متن کاملMembrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consiste...
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ژورنال
عنوان ژورنال: Current Opinion in Structural Biology
سال: 2021
ISSN: 0959-440X
DOI: 10.1016/j.sbi.2021.01.002