Results 51 to 60 of about 852,815 (296)

Single domain antibodies as a powerful tool for high quality surface plasmon resonance studies.

PLoS ONE, 2015
Single domain antibodies are recombinantly expressed functional antibodies devoid of light chains. These binding elements are derived from heavy chain antibodies found in camelids and offer several distinctive properties for applications in biotechnology
Eduardo Antonio Della Pia, Karen L Martinez   +1 more
doaj   +1 more source

The BAH domain of Rsc2 is a histone H3 binding domain [PDF]

, 2013
Bromo-adjacent homology (BAH) domains are commonly found in chromatin-associated proteins and fall into two classes; Remodels the Structure of Chromatin (RSC)-like or Sir3-like. Although Sir3-like BAH domains bind nucleosomes, the binding partners of RSC-
Adams, Angus-Hill, Anna L. Chambers, Antony W. Oliver, Armache, Badis, Bamford, Bochar, Burrows, Cairns, Cairns, Callebaut, CCP4, Chambers, Chen, Corpet, Davis, DeMase, Desai, Downs, Duncker, Emsley, Ericsson, Faucher, Foster, Gartenberg, Gartenberg, Goodwin, Hickman, Hsu, Huang, Jessica A. Downs, Jones, Kabsch, Kasten, Kent, Kuo, Lacoste, Langst, Laurence H. Pearl, Lee, Leslie, Livingstone, Longtine, McCoy, Mohrmann, Muller, Ng, Noguchi, Norris, Norris, Oliver, Onishi, Park, Peng, Ralhan, Shim, Strahl-Bolsinger, Tanny, Varela, Weissman, Xia   +61 more
core   +1 more source

Mapping the evolution of mitochondrial complex I through structural variation

FEBS Letters, EarlyView.
Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin, Tingting Chen, James A. Letts   +2 more
wiley   +1 more source

A novel tri-functional antibody fusion protein with improved pharmacokinetic properties generated by fusing a bispecific single-chain diabody with an albumin-binding domain from streptococcal protein G [PDF]

Protein Engineering Design and Selection, 2007
The therapeutic application of small recombinant antibody molecules is often limited by a short serum half-life. In order to improve the pharmacokinetic properties, we have investigated a strategy utilizing fusion with an albumin-binding domain (ABD) from streptococcal protein G.
Roland, Stork, Dafne, Müller, Roland E, Kontermann   +2 more
openaire   +2 more sources

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

FEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho, Shin Morioka, Junko Sasaki, Takehiko Sasaki   +3 more
wiley   +1 more source

Retargeted oncolytic adenovirus displaying a single variable domain of camelid heavy-chain-only antibody in a fiber protein

Molecular Therapy: Oncolytics, 2015
Conditionally replicative adenoviruses are promising agents for oncolytic virotherapy. Various approaches have been attempted to retarget adenoviruses to tumor-specific antigens to circumvent deficiency of receptor for adenoviral binding and to provide ...
Elisabeth A van Erp, Lyudmila N Kaliberova, Sergey A Kaliberov, David T Curiel   +3 more
doaj   +1 more source

Hsc70-induced changes in clathrin-auxilin cage structure suggest a role for clathrin light chains in cage disassembly [PDF]

, 2013
The molecular chaperone, Hsc70, together with its co-factor, auxilin, facilitates the ATP-dependent removal of clathrin during clathrin-mediated endocytosis in cells.
Brodsky, Frances M., Harvey-Smith, Phillip, Kent, Helen, Pearse, Barbara M. F., Ranson, Neil, Roseman, Alan, Rothnie, Alice, Smith, Corinne J., Stoilova-McPhie, Svetla, Vallis, Yvonne, Young, Anna   +10 more
core   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Production and characterization of anti-human interferon γ receptor antibody fragments that inhibit cytokine binding to the receptor [PDF]

, 2017
Three single-chain antibody fragments that recognize the extracellular human interferon γ receptor α-chain (IFNγR), and inhibit the binding of human IFNγ, have been produced in Escherichia coli.
Birch, Ashley, Bridges, Angela, Henke, Christoph, Lang, Stefan, Robinson, John A., Späth, Julia, Stuart, Fiona   +6 more
core  

The lysine residue in the membrane-spanning domain of the beta chain is necessary for cell surface expression of the T cell antigen receptor. [PDF]

, 1988
The TCR is a complex receptor composed of seven polypeptide chains consisting of a ligand-binding subunit, Ti, and a putative signal-transducing subunit, CD3.
Chin, KN, Morley, BJ, Newton, ME, Weiss, A   +3 more
core   +1 more source