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The Design of Repeat Proteins: Stability Conflicts with Functionality
(Insight Medical Publishing, 2017-03)
Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces ...
Intrinsically disordered linkers impart processivity on enzymes by spatial confinement of binding domains
(Multidisciplinary Digital Publishing Institute, 2019-05)
(1) Background: Processivity is common among enzymes and mechanochemical motors that synthesize, degrade, modify or move along polymeric substrates, such as DNA, RNA, polysaccharides or proteins. Processive enzymes can ...
CHARACTERISTICS OF ZINC-BINDING TO HUMAN RED-BLOOD-CELL MEMBRANES
(Wiley-Blackwell, 2014)
Zinc transport in mammalian cells
(American Physiological Society, 1996)
The importance of zinc in cell physiology is related mainly to its intracellular involvement in enzyme catalysis, protein structure, protein- protein interactions, and protein-oligonucleotide interactions. The mechanisms ...
An interaction between two RNA binding proteins, Nab2 and Pub1, links mRNA Processing/Export and mRNA stability
(Amer Soc Microbiology, 2014)
Polycystin-2 (TRPP2) regulation by Ca2+ is effected and diversified by actin-binding proteins
(Cell Press, 2015-05)
Calcium regulation of Ca2+-permeable ion channels is an important mechanism in the control of cell function. Polycystin-2 (PC2, TRPP2), a member of the transient receptor potential superfamily, is a nonselective cation ...
Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface
(2007-08-01)
The orphan receptor nerve growth factor-induced B (NGFI-B) is a member of the nuclear receptor's subfamily 4A (Nr4a). NGFI-B was shown to be capable of binding both as a monomer to an extended half-site containing a single ...
Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface
(2007-08-01)
The orphan receptor nerve growth factor-induced B (NGFI-B) is a member of the nuclear receptor's subfamily 4A (Nr4a). NGFI-B was shown to be capable of binding both as a monomer to an extended half-site containing a single ...