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1

Letek, Michal, María Fiuza, Almudena F. Villadangos, Luís M. Mateos, and José A. Gil. "Cytoskeletal Proteins ofActinobacteria." International Journal of Cell Biology 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/905832.

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Although bacteria are considered the simplest life forms, we are now slowly unraveling their cellular complexity. Surprisingly, not only do bacterial cells have a cytoskeleton but also the building blocks are not very different from the cytoskeleton that our own cells use to grow and divide. Nonetheless, despite important advances in our understanding of the basic physiology of certain bacterial models, little is known aboutActinobacteria, an ancient group of Eubacteria. Here we review current knowledge on the cytoskeletal elements required for bacterial cell growth and cell division, focusing
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Chakroun, Maissa, Núria Banyuls, Yolanda Bel, Baltasar Escriche, and Juan Ferré. "Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria." Microbiology and Molecular Biology Reviews 80, no. 2 (2016): 329–50. http://dx.doi.org/10.1128/mmbr.00060-15.

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SUMMARYEntomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it di
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3

Kormanec, Jan. "Bacterial Regulatory Proteins." International Journal of Molecular Sciences 23, no. 12 (2022): 6854. http://dx.doi.org/10.3390/ijms23126854.

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4

Płaczkiewicz, Jagoda. "BACTERIAL MOONLIGHTING PROTEINS." Postępy Mikrobiologii - Advancements of Microbiology 56, no. 2 (2019): 226–32. http://dx.doi.org/10.21307/pm-2017.56.2.226.

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5

Henderson, Brian. "An overview of protein moonlighting in bacterial infection." Biochemical Society Transactions 42, no. 6 (2014): 1720–27. http://dx.doi.org/10.1042/bst20140236.

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We are rapidly returning to a world in which bacterial infections are a major health issue. Pathogenic bacteria are able to colonize and cause pathology due to the possession of virulence factors such as adhesins, invasins, evasins and toxins. These are generally specifically evolved proteins with selective actions. It is, therefore, surprising that most human bacterial pathogens employ moonlighting proteins as virulence factors. Currently, >90 bacterial species employ one or more moonlighting protein families to aid colonization and induce disease. These organisms employ 90 moonlighting ba
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6

Grigorov, A. S., and T. L. Azhikina. "Bacterial Cold Shock Proteins as a Factor of Adaptation to Stresses." Биоорганическая химия 49, no. 1 (2023): 23–31. http://dx.doi.org/10.31857/s0132342323010104.

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Bacteria have evolved a number of mechanisms to cope with stresses and adapt to changing environmental conditions. A family of bacterial proteins containing a functional cold shock domain are highly conserved nucleic acid-binding proteins that modulate transcription and post-transcriptional events in bacteria. For many bacteria, these proteins have been shown to regulate the expression of various genes involved in virulence and resistance of bacteria to stresses. The review discusses the new data on the mechanisms of action and the roles of cold shock proteins in the regulation of expression i
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7

Sánchez, Borja, María C. Urdaci, and Abelardo Margolles. "Extracellular proteins secreted by probiotic bacteria as mediators of effects that promote mucosa–bacteria interactions." Microbiology 156, no. 11 (2010): 3232–42. http://dx.doi.org/10.1099/mic.0.044057-0.

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During the last few years, a substantial body of scientific evidence has accumulated suggesting that certain surface-associated and extracellular components produced by probiotic bacteria could be responsible for some of their mechanisms of action. These bacterial components would be able to directly interact with the host mucosal cells; they include exopolysaccharides, bacteriocins, lipoteichoic acids and surface-associated and extracellular proteins. Extracellular proteins include proteins that are actively transported to the bacterial surroundings through the cytoplasmic membrane, as well a
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8

Beatty, Wandy L., and David G. Russell. "Identification of Mycobacterial Surface Proteins Released into Subcellular Compartments of Infected Macrophages." Infection and Immunity 68, no. 12 (2000): 6997–7002. http://dx.doi.org/10.1128/iai.68.12.6997-7002.2000.

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ABSTRACT Considerable effort has focused on the identification of proteins secreted from Mycobacterium spp. that contribute to the development of protective immunity. Little is known, however, about the release of mycobacterial proteins from the bacterial phagosome and the potential role of these molecules in chronically infected macrophages. In the present study, the release of mycobacterial surface proteins from the bacterial phagosome into subcellular compartments of infected macrophages was analyzed. Mycobacterium bovis BCG was surface labeled with fluorescein-tagged succinimidyl ester, an
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9

Lim, Sooa. "A Review of the Bacterial Phosphoproteomes of Beneficial Microbes." Microorganisms 11, no. 4 (2023): 931. http://dx.doi.org/10.3390/microorganisms11040931.

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The number and variety of protein post-translational modifications (PTMs) found and characterized in bacteria over the past ten years have increased dramatically. Compared to eukaryotic proteins, most post-translational protein changes in bacteria affect relatively few proteins because the majority of modified proteins exhibit substoichiometric modification levels, which makes structural and functional analyses challenging. In addition, the number of modified enzymes in bacterial species differs widely, and degrees of proteome modification depend on environmental conditions. Nevertheless, evid
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10

Culbertson, Edward M., and Tera C. Levin. "Eukaryotic CD-NTase, STING, and viperin proteins evolved via domain shuffling, horizontal transfer, and ancient inheritance from prokaryotes." PLOS Biology 21, no. 12 (2023): e3002436. http://dx.doi.org/10.1371/journal.pbio.3002436.

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Animals use a variety of cell-autonomous innate immune proteins to detect viral infections and prevent replication. Recent studies have discovered that a subset of mammalian antiviral proteins have homology to antiphage defense proteins in bacteria, implying that there are aspects of innate immunity that are shared across the Tree of Life. While the majority of these studies have focused on characterizing the diversity and biochemical functions of the bacterial proteins, the evolutionary relationships between animal and bacterial proteins are less clear. This ambiguity is partly due to the lon
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Covacci, Antonello, and Rino Rappuoli. "Tyrosine-Phosphorylated Bacterial Proteins." Journal of Experimental Medicine 191, no. 4 (2000): 587–92. http://dx.doi.org/10.1084/jem.191.4.587.

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12

Ermolenko, D. N., and G. I. Makhatadze. "Bacterial cold-shock proteins." Cellular and Molecular Life Sciences 59, no. 11 (2002): 1902–13. http://dx.doi.org/10.1007/pl00012513.

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Dennison, Christopher, Sholto David, and Jaeick Lee. "Bacterial copper storage proteins." Journal of Biological Chemistry 293, no. 13 (2018): 4616–27. http://dx.doi.org/10.1074/jbc.tm117.000180.

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14

SOMEYA, Yuichi, and Akihito YAMAGUCHI. "Bacterial Drug Efflux Proteins." Nippon Saikingaku Zasshi 50, no. 2 (1995): 403–21. http://dx.doi.org/10.3412/jsb.50.403.

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15

Monnet, V. "Bacterial oligopeptide-binding proteins." Cellular and Molecular Life Sciences (CMLS) 60, no. 10 (2003): 2100–2114. http://dx.doi.org/10.1007/s00018-003-3054-3.

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16

Rosen, Ran, Dörte Becher, Knut Büttner, Dvora Biran, Michael Hecker, and Eliora Z. Ron. "Highly phosphorylated bacterial proteins." PROTEOMICS 4, no. 10 (2004): 3068–77. http://dx.doi.org/10.1002/pmic.200400890.

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17

Plüddemann, Annette, Subhankar Mukhopadhyay, and Siamon Gordon. "The interaction of macrophage receptors with bacterial ligands." Expert Reviews in Molecular Medicine 8, no. 28 (2006): 1–25. http://dx.doi.org/10.1017/s1462399406000159.

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Innate immune receptors play a key role in the early recognition of invading bacterial pathogens and initiate the crucial innate immune response. The diverse macrophage receptors recognise Gram-positive and Gram-negative bacteria via conserved structures on the bacterial surface and facilitate phagocytosis and/or signalling, providing the trigger for the adaptive immune response. These receptors include scavenger receptors, C-type lectins, integrins, Toll-like receptors and siglecs. The bacterial ligands generally recognised by these receptors range from lipopolysaccharides on Gram-negative ba
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18

Alshammari, Askar K., Meshach Maina, Adam M. Blanchard, Janet M. Daly, and Stephen P. Dunham. "Understanding the Molecular Interactions Between Influenza A Virus and Streptococcus Proteins in Co-Infection: A Scoping Review." Pathogens 14, no. 2 (2025): 114. https://doi.org/10.3390/pathogens14020114.

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Influenza A virus infections are known to predispose infected individuals to bacterial infections of the respiratory tract that result in co-infection with severe disease outcomes. Co-infections involving influenza A viruses and streptococcus bacteria result in protein–protein interactions that can alter disease outcomes, promoting bacterial colonisation, immune evasion, and tissue damage. Focusing on the synergistic effects of proteins from different pathogens during co-infection, this scoping review evaluated evidence for protein–protein interactions between influenza A virus proteins and st
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19

Shih, Yu-Ling, and Lawrence Rothfield. "The Bacterial Cytoskeleton." Microbiology and Molecular Biology Reviews 70, no. 3 (2006): 729–54. http://dx.doi.org/10.1128/mmbr.00017-06.

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SUMMARY In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA group, that appears to be unique to bacteria. The cytoskeletal structures play important roles in cell division, cell polarity, cell shape regulation, plasmid partition, and other functions. The proteins self-assemble into filamentous structures in vitro and form intracellular ordered structures in
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20

Kaeser, Gero, Norbert Krauß, Clare Roughan, Luisa Sauthof, Patrick Scheerer, and Tilman Lamparter. "Phytochrome-Interacting Proteins." Biomolecules 14, no. 1 (2023): 9. http://dx.doi.org/10.3390/biom14010009.

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Phytochromes are photoreceptors of plants, fungi, slime molds bacteria and heterokonts. These biliproteins sense red and far-red light and undergo light-induced changes between the two spectral forms, Pr and Pfr. Photoconversion triggered by light induces conformational changes in the bilin chromophore around the ring C-D-connecting methine bridge and is followed by conformational changes in the protein. For plant phytochromes, multiple phytochrome interacting proteins that mediate signal transduction, nuclear translocation or protein degradation have been identified. Few interacting proteins
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21

Boichenko, M. N., E. O. Kravtsova, and V. V. Zverev. "Mechanism of intracellular bacterial parasitism." Journal of microbiology, epidemiology and immunobiology, no. 5 (November 21, 2019): 61–72. http://dx.doi.org/10.36233/0372-9311-2019-5-61-72.

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Algorithm of intracellular bacterial parasitism does not depend on if bacterium is obligate or facultative intracellular parasite. Depending on replicative niche’s localization intracellular bacterial parasites are divided onto cellular and vacuolated. Rickettsia spp., Shigella spp., Chlamydia spp. and Listeria monocytogenes use cell’s machinery of actin polymerization during process of their intracellular parasitism. These bacteria possess some of effector’s proteins which contain domains identical to effector proteins from the host cell. Shigella spp. T3SS and autotransporter protein IscA pr
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22

Kleba, Betsy, and Richard S. Stephens. "Chlamydial Effector Proteins Localized to the Host Cell Cytoplasmic Compartment." Infection and Immunity 76, no. 11 (2008): 4842–50. http://dx.doi.org/10.1128/iai.00715-08.

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ABSTRACT Disease-causing microbes utilize various strategies to modify their environment in order to create a favorable location for growth and survival. Gram-negative bacterial pathogens often use specialized secretion systems to translocate effector proteins directly into the cytosol of the eukaryotic cells they infect. These bacterial proteins are responsible for modulating eukaryotic cell functions. Identification of the bacterial effectors has been a critical step toward understanding the molecular basis for the pathogenesis of the bacteria that use them. Chlamydiae are obligate intracell
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23

Shapiro, L., H. H. McAdams, and R. Losick. "Why and How Bacteria Localize Proteins." Science 326, no. 5957 (2009): 1225–28. http://dx.doi.org/10.1126/science.1175685.

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Despite their small size, bacteria have a remarkably intricate internal organization. Bacteria deploy proteins and protein complexes to particular locations and do so in a dynamic manner in lockstep with the organized deployment of their chromosome. The dynamic subcellular localization of protein complexes is an integral feature of regulatory processes of bacterial cells.
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24

Van Amersfoort, Edwin S., Theo J. C. Van Berkel, and Johan Kuiper. "Receptors, Mediators, and Mechanisms Involved in Bacterial Sepsis and Septic Shock." Clinical Microbiology Reviews 16, no. 3 (2003): 379–414. http://dx.doi.org/10.1128/cmr.16.3.379-414.2003.

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SUMMARY Bacterial sepsis and septic shock result from the overproduction of inflammatory mediators as a consequence of the interaction of the immune system with bacteria and bacterial wall constituents in the body. Bacterial cell wall constituents such as lipopolysaccharide, peptidoglycans, and lipoteichoic acid are particularly responsible for the deleterious effects of bacteria. These constituents interact in the body with a large number of proteins and receptors, and this interaction determines the eventual inflammatory effect of the compounds. Within the circulation bacterial constituents
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Anjaini, Jefri, Tohap Simangunsong, and Hery Irawan. "Quorum Sensing Inhibition pada Pembetukan Biofilm Salmonella typhi dengan Ekstrak Daun Cincau Hijau (Cyclea barbata Miers)." Jurnal Biologi Tropis 24, no. 2 (2024): 993–98. http://dx.doi.org/10.29303/jbt.v24i2.7232.

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Salmonella is one example of bacteria that can contaminate fishery products. It is one of the bacteria that most commonly infects people through contaminated food and drink. One management to reduce Salmonella in fishery products is using Biofilm. The biofilm mechanism formed from Salmonella typhi type bacteria can be inhibited from several intervention strategies that are able to disrupt and prevent biofilm formation. Green grass jelly leaf extract has antibacterial activity against S. typhi which is indicated by the formation of an inhibition zone due to the activity of flavonoid compounds.
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26

Nordenfelt, Pontus, Sofia Waldemarson, Adam Linder, et al. "Antibody orientation at bacterial surfaces is related to invasive infection." Journal of Experimental Medicine 209, no. 13 (2012): 2367–81. http://dx.doi.org/10.1084/jem.20120325.

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Several of the most significant bacterial pathogens in humans, including Streptococcus pyogenes, express surface proteins that bind IgG antibodies via their fragment crystallizable (Fc) region, and the dogma is that this protects the bacteria against phagocytic killing in blood. However, analysis of samples from a patient with invasive S. pyogenes infection revealed dramatic differences in the presence and orientation of IgG antibodies at the surface of bacteria from different sites. In the throat, IgG was mostly bound to the bacterial surface via Fc, whereas in the blood IgG was mostly bound
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Lorv, Janet S. H., David R. Rose, and Bernard R. Glick. "Bacterial Ice Crystal Controlling Proteins." Scientifica 2014 (2014): 1–20. http://dx.doi.org/10.1155/2014/976895.

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Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice
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28

Ellefson, D., D. Parker, and F. Heffron. "Identification of MHC-I Accessible Proteins from Salmonella Typhimurium." Microscopy and Microanalysis 7, S2 (2001): 616–17. http://dx.doi.org/10.1017/s1431927600029159.

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Intracellular bacterial pathogens such as Salmonella typhimurium secrete proteins into the host cell after infection. These proteins alter the normal structural and metabolic machinery of the host cell and benefit the bacterium by facilitating replication and avoidance of host immune surveillance. Since the host cytoplasmic localization of these proteins infers access to the class-I MHC antigen processing and presentation machinery of the host cell, we collectively refer to these proteins as Class- I Accessible Proteins (CAPs).The design of vaccines for new and emerging bacterial pathogens is
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29

Kivisaar, Maia. "Mutation and Recombination Rates Vary Across Bacterial Chromosome." Microorganisms 8, no. 1 (2019): 25. http://dx.doi.org/10.3390/microorganisms8010025.

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Bacteria evolve as a result of mutations and acquisition of foreign DNA by recombination processes. A growing body of evidence suggests that mutation and recombination rates are not constant across the bacterial chromosome. Bacterial chromosomal DNA is organized into a compact nucleoid structure which is established by binding of the nucleoid-associated proteins (NAPs) and other proteins. This review gives an overview of recent findings indicating that the mutagenic and recombination processes in bacteria vary at different chromosomal positions. Involvement of NAPs and other possible mechanism
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30

Mattoo, Seema, Yvonne M. Lee, and Jack E. Dixon. "Interactions of bacterial effector proteins with host proteins." Current Opinion in Immunology 19, no. 4 (2007): 392–401. http://dx.doi.org/10.1016/j.coi.2007.06.005.

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31

Vázquez-Laslop, Nora, Hyunwoo Lee, Rong Hu, and Alex A. Neyfakh. "Molecular Sieve Mechanism of Selective Release of Cytoplasmic Proteins by Osmotically Shocked Escherichia coli." Journal of Bacteriology 183, no. 8 (2001): 2399–404. http://dx.doi.org/10.1128/jb.183.8.2399-2404.2001.

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ABSTRACT Escherichia coli cells, the outer membrane of which is permeabilized with EDTA, release a specific subset of cytoplasmic proteins upon a sudden drop in osmolarity in the surrounding medium. This subset includes EF-Tu, thioredoxin, and DnaK among other proteins, and comprises ∼10% of the total bacterial protein content. As we demonstrate here, the same proteins are released from electroporatedE. coli cells pretreated with EDTA. Although known for several decades, the phenomenon of selective release of proteins has received no satisfactory explanation. Here we show that the subset of re
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32

Bartosik, Aneta A., and Grazyna Jagura-Burdzy. "Bacterial chromosome segregation." Acta Biochimica Polonica 52, no. 1 (2005): 1–34. http://dx.doi.org/10.18388/abp.2005_3481.

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In most bacteria two vital processes of the cell cycle: DNA replication and chromosome segregation overlap temporally. The action of replication machinery in a fixed location in the cell leads to the duplication of oriC regions, their rapid separation to the opposite halves of the cell and the duplicated chromosomes gradually moving to the same locations prior to cell division. Numerous proteins are implicated in co-replicational DNA segregation and they will be characterized in this review. The proteins SeqA, SMC/MukB, MinCDE, MreB/Mbl, RacA, FtsK/SpoIIIE playing different roles in bacterial
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Cahoon, Laty A., and Nancy E. Freitag. "Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone." Infection and Immunity 83, no. 10 (2015): 4028–41. http://dx.doi.org/10.1128/iai.00504-15.

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The Gram-positive bacteriumListeria monocytogenesis a facultative intracellular pathogen that relies on the regulated secretion and activity of a variety of proteins that sustain life within diverse environments. PrsA2 has recently been identified as a secreted peptidyl-prolylcis/transisomerase and chaperone that is dispensable for bacterial growth in broth culture but essential forL. monocytogenesvirulence. Following host infection, PrsA2 contributes to the proper folding and activity of secreted proteins that are required for bacterial replication within the host cytosol and for bacterial sp
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34

Aseev, Leonid V., Ludmila S. Koledinskaya, and Irina V. Boni. "Extraribosomal Functions of Bacterial Ribosomal Proteins—An Update, 2023." International Journal of Molecular Sciences 25, no. 5 (2024): 2957. http://dx.doi.org/10.3390/ijms25052957.

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Ribosomal proteins (r-proteins) are abundant, highly conserved, and multifaceted cellular proteins in all domains of life. Most r-proteins have RNA-binding properties and can form protein–protein contacts. Bacterial r-proteins govern the co-transcriptional rRNA folding during ribosome assembly and participate in the formation of the ribosome functional sites, such as the mRNA-binding site, tRNA-binding sites, the peptidyl transferase center, and the protein exit tunnel. In addition to their primary role in a cell as integral components of the protein synthesis machinery, many r-proteins can fu
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35

Minniti, Giusi, Simen Rød Sandve, János Tamás Padra, et al. "The Farmed Atlantic Salmon (Salmo salar) Skin–Mucus Proteome and Its Nutrient Potential for the Resident Bacterial Community." Genes 10, no. 7 (2019): 515. http://dx.doi.org/10.3390/genes10070515.

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Norway is the largest producer and exporter of farmed Atlantic salmon (Salmo salar) worldwide. Skin disorders correlated with bacterial infections represent an important challenge for fish farmers due to the economic losses caused. Little is known about this topic, thus studying the skin–mucus of Salmo salar and its bacterial community depict a step forward in understanding fish welfare in aquaculture. In this study, we used label free quantitative mass spectrometry to investigate the skin–mucus proteins associated with both Atlantic salmon and bacteria. In particular, the microbial temporal p
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36

Adamu, Zainab, Humphery Chukwuemeka Nzelibe, Hajiya Mairo Inuwa, Yunusa Pala Yahaya, and AbdulRahman Umar Abubakar. "Purification of antibacterial proteins from Coffee senna (Senna occidentalis) seeds." GSC Biological and Pharmaceutical Sciences 7, no. 2 (2019): 118–26. https://doi.org/10.5281/zenodo.4294630.

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<em>Senna occidentalis</em>&nbsp;(L.) Link formally known as&nbsp;<em>Cassia occidentalis</em>&nbsp;is a popular herb in folk medicine for the treatment of a wide range of microbial infections. Crude, ammonium sulphate precipitated and dialyzed proteins of&nbsp;<em>S. occidentalis</em>&nbsp;seeds were evaluated for their antibacterial potential by agar well diffusion and broth dilution techniques, against ten bacterial isolates made up of five Gram positive bacteria;&nbsp;<em>Staphylococcus aureus</em>,&nbsp;<em>Streptococcus pyogenes</em>, Enterococcus Sp,&nbsp;<em>Listeria monocytogene</em>&
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37

Gursoy, Ulvi Kahraman. "Periodontal Bacteria and Epithelial Cell Interactions: Role of Bacterial Proteins." European Journal of Dentistry 02, no. 04 (2008): 231–32. http://dx.doi.org/10.1055/s-0039-1697385.

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Shen, Xi, Zixiang Yang, Zihan Li, et al. "Identification of atypical T4SS effector proteins mediating bacterial defense." mLife 2, no. 3 (2023): 295–307. http://dx.doi.org/10.1002/mlf2.12084.

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AbstractTo remain competitive, proteobacteria use various contact‐dependent weapon systems to defend against microbial competitors. The bacterial‐killing type IV secretion system (T4SS) is one such powerful weapon. It commonly controls the killing/competition between species by secreting the lethal T4SS effector (T4E) proteins carrying conserved XVIPCD domains into competing cells. In this study, we sought knowledge to understand whether the bacterial‐killing T4SS‐producing bacteria encode T4E‐like proteins and further explore their biological functions. To achieve this, we designed a T4E‐guid
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39

Heras, Begoña, Stephen R. Shouldice, Makrina Totsika, Martin J. Scanlon, Mark A. Schembri, and Jennifer L. Martin. "DSB proteins and bacterial pathogenicity." Nature Reviews Microbiology 7, no. 3 (2009): 215–25. http://dx.doi.org/10.1038/nrmicro2087.

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40

Lencer, Wayne I. "Signal Transduction by Bacterial Proteins." Journal of Pediatric Gastroenterology and Nutrition 40, Supplement 1 (2005): S33—S34. http://dx.doi.org/10.1097/00005176-200504001-00020.

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41

Philpott, Dana. "NOD Proteins and Bacterial Detection." Inflammatory Bowel Diseases 12 (April 2006): S3. http://dx.doi.org/10.1097/00054725-200604002-00009.

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42

Mota, Luís Jaime, and David W. Holden. "FlAsHlights on bacterial virulence proteins." Nature Methods 2, no. 12 (2005): 898–99. http://dx.doi.org/10.1038/nmeth1205-898.

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43

O'Kane, D. J., B. Woodward, J. Lee, and D. C. Prasher. "Borrowed proteins in bacterial bioluminescence." Proceedings of the National Academy of Sciences 88, no. 4 (1991): 1100–1104. http://dx.doi.org/10.1073/pnas.88.4.1100.

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44

Hellman, J., and H. S. Warren. "Antibodies against bacterial membrane proteins." Journal of Endotoxin Research 5, no. 4 (1999): 213–15. http://dx.doi.org/10.1179/096805199101531787.

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45

Choi, Charles Q. "Bacterial proteins on the move." Genome Biology 5 (2004): spotlight—20050705–01. http://dx.doi.org/10.1186/gb-spotlight-20050705-01.

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46

Hellman, Judith, and H. Shaw Warren. "Antibodies against bacterial membrane proteins." Journal of Endotoxin Research 5, no. 4 (1999): 213–15. http://dx.doi.org/10.1177/09680519990050040901.

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47

Petermann, Mary L. "PLASMA PROTEINS IN BACTERIAL INFECTIONS." Annals of the New York Academy of Sciences 94, no. 1 (2006): 144–48. http://dx.doi.org/10.1111/j.1749-6632.1961.tb35538.x.

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48

Pallen, Mark J., and Christopher P. Ponting. "PDZ domains in bacterial proteins." Molecular Microbiology 26, no. 2 (1997): 411–13. http://dx.doi.org/10.1046/j.1365-2958.1997.5591911.x.

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Celia Henry Arnaud. "Floppy linkers direct bacterial proteins." C&EN Global Enterprise 99, no. 29 (2021): 13. http://dx.doi.org/10.1021/cen-09929-scicon6.

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Ceri, Howard, and Yolande Westra. "Host binding proteins and bacterial adhesion: ecology and binding model." Biochemistry and Cell Biology 66, no. 6 (1988): 541–48. http://dx.doi.org/10.1139/o88-064.

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Abstract:
Defining the involvement of specific recognition and (or) adhesion molecules in the precise association formed between cells of an organism during development or between bacteria and specific host tissues has become a focus of extensive research. The possibility that the same molecules responsible for cellular adhesion in the host may also play a major role in determining host–bacterial interactions is now becoming more evident. The following review looks at the interaction of a group of host binding proteins, including lectins, fibronectin, and laminin, with respect to their specific associat
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