When a swingarm is present on only one side of the motorcycle, this is known as a single-sided swingarm. In 1981 BMW introduced the single sided swingarm (mono lever) to motorcycles on their R 80 GS model. Notable examples include the Honda VFR800 and the BMW R- and K-series. Single-sided swingarms make rear-wheel removal easier, though they generally increase the unsprung weight of the rear suspension. This is due to the additional material required to give identical torsional rigidity to a conventional (two-sided) swingarm setup.[citation needed] For this reason sports bikes are rarely seen using the setup. Notable exclusions are the Ducati 916 which was intended to be taken endurance racing, the MV Agusta f4 which has a hollow interior for reduced weight (a magnesium version is also available), and the Ducati 1098, which was given a single sided swingarm purely for styling reasons.[citation needed]
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One such target, first described by Cohen et al. over four decades ago, is the epidermal growth factor receptor (EGFR). It is a membrane-bound tyrosine kinase receptor (TKR) that plays a key role in mediating signal transduction from growth factors to the interior of the cell, where downstream effectors mediate a host of cellular functions [2] . It also plays an important role in the growth and survival of many tumors. Furthermore, it has favorable characteristics as a target for drugs. Two classes of agents have emerged designed to abrogate the function of this receptor. There are the 'small molecules', low-molecular-weight compounds that inhibit the receptor's tyrosine kinase region on the intracellular domain in an ATP-competitive manner (beyond the scope of this review). The second class includes monoclonal antibodies (mAbs) that target the extracellular domain of EGFR, which will be discussed in this review.
The EGFR belongs to the human epidermal growth factor receptor family comprised of four members; EGFR (HER1 or ErbB1), ErbB2 (HER2/neu), ErbB3 (HER3) and ErbB4 (HER4) [3] . ErbB receptors are glycoproteins composed of an extracellular ligand-binding domain, a transmembrane region and an intracellular protein tyrosine kinase domain with a regulatory carboxyl terminal segment. Despite moderate sequence homology, not all ErbB members are autonomous; HER2/neu lacks the capacity to interact with ligand, whereas HER3 is kinase defective [4] . Regardless, by complexing with other monomeric receptors (ErbB or otherwise) to form homo- or heterodimers, all family members are capable of generating and propagating cellular signals. 2ff7e9595c
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