Results 181 to 190 of about 8,676 (203)

A comprehensive catalogue of receptor-binding domains in extracellular contractile injection systems. [PDF]

Nat Commun
Nachmias N, Wang Z, Feng X, Jiang F, Levy A.   +4 more
europepmc   +1 more source

Conflicting Kinesin-14s in a single chromosomal drive haplotype. [PDF]

Genetics
Brady MJ, Gupta A, Gent JI, Swentowsky KW, Unckless RL, Dawe RK.   +5 more
europepmc   +1 more source

A robust platform for recombinant production of animal venom toxin modulators of ion channels

Gonzalez-Prada JE, Haworth AS, Browne JI, Salvage SC, Secomandi N, Rush AM, Ritoux A, Dannawi M, Lee L, Mavridou V, Dong YY, Smith ES, Jackson AP, Stevens EB, Miller PS.   +14 more
europepmc   +1 more source

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Adjusting middleware knobs to suit CPS domains

Proceedings of the 31st Annual ACM Symposium on Applied Computing, 2016
The large scale and dynamic behavior of cyber-physical systems (CPS) require great effort at the middleware level. Middleware lies at the architectural point where low-level communication and execution meet the horizontal control and orchestration accross nodes and systems.
Marisol García-Valls, Cristian Calva-Urrego, Alejandro Alonso 0001, Juan Antonio de la Puente   +3 more
openaire   +1 more source

Retargeting Adenovirus Serotype 48 Fiber Knob Domain by Peptide Incorporation

Human Gene Therapy, 2014
Adenovirus type 5 (Ad5) is a commonly used vector for gene therapy, but its efficacy is limited by high seroprevalence and off-target hepatic and splenic sequestration. In order to circumvent these limitations, the use of vectors derived from rare species adenoviruses is appealing.
Lynda, Coughlan, Hanni, Uusi-Kerttula, Jiangtao, Ma, Bethany P, Degg, Alan L, Parker, Andrew H, Baker   +5 more
openaire   +2 more sources

A “Knob Switch” Model for the Phosphoregulatory Mechanism of KCC3 at the Carboxy-Terminal Domain

Biochemistry
Phosphorylation is a reversible post-translational modification that can modulate protein function. For example, phosphorylation modifications of solute carrier family 12 (SLC12) proteins function as molecular switches that precisely regulate cation-chloride ion transport.
Xiaoli Lu, Jing Xue, Qiang Zhou, Jing Huang   +3 more
openaire   +2 more sources

Two Distinct Domains Mediate Self-Assembly of Knob Protein in Plasmodium Falciparum-Infected Human Erythrocytes.

Blood, 2004
Abstract Plasmodium falciparum associated mortality is believed to originate from the adhesion of infected erythrocytes to the endothelial cells. The adhesion of mature parasite infected erythrocytes is mediated by the surface protrusions called knobs. A dominant constituent of knobs is the parasite derived knob-associated histidine-rich
Huiqing Chen, Xuerong Li, Steven S. Oh, Athar H. Chishti   +3 more
openaire   +1 more source

Fiber knob domain lacking the shaft sequence but fused to a coiled coil is a candidate subunit vaccine against egg-drop syndrome

Vaccine, 2016
Egg-drop syndrome (EDS) virus is an avian adenovirus that causes a sudden drop in egg production and in the quality of the eggs when it infects chickens, leading to substantial economic losses in the poultry industry. Inactivated EDS vaccines produced in embryonated duck eggs or cell culture systems are available for the prophylaxis of EDS.
Tetsuya, Harakuni, Kiyohiko, Andoh, Ryu-Ichi, Sakamoto, Yukihiro, Tamaki, Takeshi, Miyata, Hirotaka, Uefuji, Ken-Ichi, Yamazaki, Takeshi, Arakawa   +7 more
openaire   +2 more sources

A PHIST protein interacts with the intracellular ATS domain of PfEMP1 and localizes to knob structures in P. falciparum

2014
The most severe form of malaria is caused by the asexual development of the apicomplexan parasite Plasmodium falciparum within the red blood cell (RBC) and leads to almost one million deaths each year. In order to avoid splenic clearance the parasite transports adhesion molecules like PfEMP1 to the [for full text, please go to the a.m. URL]
Oberli, A, Slater, L, Cutts, E, Brand, F, Vakonakis, I, Beck, HP   +5 more
openaire   +2 more sources

Genetic polymorphism at the C-terminal domain (region III) of knob-associated histidine-rich protein (KAHRP) of Plasmodium falciparum in isolates from Iran

Parasitology Research, 2011
The knob-associated histidine-rich protein (KAHRP) plays a major role in the virulence of Plasmodium falciparum and is one of the targets for molecular therapy. The primary structure of KAHRP of P. falciparum consists of three domains (regions I-III), of which the C-terminal domain (region III) is the most polymorphic segment of this protein.
Ahmad, Mardani, Hossein, Keshavarz, Aliehsan, Heidari, Homa, Hajjaran, Ahmad, Raeisi, Mohammad Reza, Khorramizadeh   +5 more
openaire   +2 more sources