Zippers parts

Antifriction parts, bearings, bushings, rods, zippers. .. 

Unfortunately, the exact nature of the intermediate species detected by the ring electrode is not clear, and whether these are from different stages in the zipper process, or why they should have left the disc electrode part way through the fluorination, is not explained. 

The observation of large amounts of polyfluorinated compounds dissolved in the HF-phase was claimed not to be peculiar to these reactions but was said to be a normal part of all ECF reactions, and as such, said to contradict the zipper mechanism production of perfluorinated compounds, a pathway regarded as a support of the ECbECN process [62,172]. 

The cadherins are calcium-dependent adhesion proteins that mediate direct cell-cell interactions.295 296 The external parts of the cadherins also have repeated structural domains with the Ig fold.297 298b They have high affinity for each other, allowing cadherins from two different cells to interact and tie the cells together with a zipper-like interaction that is stabilized by the bound Ca2+ ions,297 300 and may be relatively long-lived. The gene for cadherin E is often mutated in breast cancers and may be an important tumor suppressor gene (Box 11-D).301... 

Jun is actually a multigene family whose encoded proteins bind to DNA as complexes formed with the 62 kDa phosphoprotein Fos, the product of the c-fos gene.460 The heterodimeric Fos/Jun complex is held together, at least in part, by interactions between leucine side chains lying along a pair of parallel a-helices in a "leucine zipper" (Fig. 5-36 Fig. 2-21).461 462... 

Diagrammatic sketch of a leucine zipper dimer. The protein monomers are held together by interaction between leucine side chains (green knobs in the upper part of the structure). The part of the protein monomers that interacts with the major groove of the DNA is shown (in red). (Adapted from C. R. Vinson et al Science 246 911, 1989.)... 

FIGURE 2—38. How early genes activate late genes, part 3. Once Fos and Jun proteins are synthesized, they can collaborate as partners and produce a Fos-Jun combination protein, which now acts as a transcription factor for late genes. Sometimes the Fos-Jun transcription factor is called a leucine zipper. 

Stahl, S.M. (2000) Molecular neurobiology for practicing psychiatrists, part 5 how a leucine zipper can turn on genes immediate early genes activate late gene expression in the brain. Journal of Clinical Psychiatry 61(1), 7—8. 

Studies using knockout mice implicate the basic leucine zipper Nrf2 as part of the transcriptional complex directly involved in mediating ARE-dependent transcriptional... 

The second class of eukaryotic DNA-binding unit is the basic-leucine zipper, or bZip, proteins (Figure 31.6). This DNA-binding unit consists of a pair of long a helices. The first part of each a helix is a basic region that lies in the major groove of the DNA and makes contacts responsible for DNA-site recognition. The second part of each a helix forms a coiled-coil structure with its partner. Because these units are often stabilized by appropriately spaced leucine residues, these structures are often referred to as leucine zippers (p. 45). 

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