Proteins reviewed

Nijdam, D. Rood, T. Westhoek, H. The price of protein review of land use and carbon footprints from life cycle assessments of animal food products and their substitutes. Food Pol. 2012, 37, 760-770. 

Poulos T, Finzel B (1984) In Hearn MTW (ed) Peptide and Protein Reviews, Marcel Dekker, Inc, New York, p 115... 

Testotoxicosis is a form of male precocious puberty. The disorder results from a constitutive activation of the G a protein (reviewed in Chapter 6). This results in LH receptor activation that is analogous to the LH receptor mutant phenotypes. The disorder often presents alongside paradoxical pseudohypoparathyroidism type la (PHP-Ia), a condition that is marked by resistance to hormones acting through cAMP (PTH and TSH) (91). 

The regulation of the TFR and ferritin concentrations occurs at the mRNA level for both proteins (review Klausner et al., 1993 Hentze and Kiihn, 1996). The key element for the regulation of the TFR concentration is a region at the 3 - non-translated end of... 

PDZ domains were first identified in proteins of postsynaptic cells and their designation comes from their occurrence in the proteins PSD-95, DlgA and ZO-1 (see Saras and Heldin, 1996). In the meantime, PDZ domains have been found in many other proteins, particularly in proteins that form structures in the cell membrane (e.g. in ion channels) and in signal proteins (review Craven and Brett, 1997). PDZ domains recognize short peptide sequences with a C-terminal hydrophobic residue and a free carboxyl group, such as the E(S/T)DV motif at the C terminus of certain subunits of ion channels. 

The protein PSD-95 is an example of a PDZ-containing protein (review Craven and Bredt, 1998). PSD-95 is found in postsynaptic cells where, via its PDZ domains, it mediates interactions with intracellular domains of receptors such as the NMDA receptor (see 16.4.2.1). The InaD protein which is composed solely of PDZ domains has an adaptor function in the vision process in Drosophila (see 8.2.5). 

The two-component system is a signaling pathway of great importance in bacteria. Similar proteins and signaling pathways can also be identified in plant cells and in yeast, based on sequence homology with the bacterial proteins (review Swanson et al., 1994). It is expected that signaling pathways using the principle of the two-component system will also be foimd in mammals. 

The following central functions may be assigned to the p53 protein (review Ko and Prives, 1996, Agarwal et al., 1998). 

Indeed, the observation that different agonists can affect which G proteins are activated by a given receptor supports a model where specific receptor conformations may be more or less favorable for coupling to specific G proteins (reviewed in Kenakin, 2003 Perez and Karnik, 2005). In one... 

Dolnik V (2006), Capillary electrophoresis of proteins (Review 2003-2005), Electrophoresis 27 126-141. 

Hybridization-Independent Toxicides Many, if not most, of the toxicities that have been observed with PS ODN and other oligonucleotide classes are related to the hybridization-independent effects. These class effects are related to the chemistry, and many are known to be related to the interaction of oligonucleotides with proteins (reviewed in [17,30,31] [1]). Toxicities such as the prolongation of aPTT, the activation of complement, and immunostimulation are all examples of oligonucleotide protein interactions that are independent of hybridization. Thus reducing protein binding also reduces the likelihood of some of these toxicities, but that comes at a cost. Reduced protein binding... 

It may no longer matter what hypothesis has led to the identification of angiostatin and endostatin. Of more concern for us are the questions of how angiostatin and endostatin relate to cytokines and growth factors, and how their actions can be explained in molecular terms. It appears that, of all the proteins reviewed in this chapter, angiostatin and endostatin... 

Fig. 6. Repacking of the influenza HA2 hydrophobic core. Left. A ribbon trace of HA2 residues 38 to 127, including the helices that make up the core of the stalk in the native HA structure (see Fig. 3). Middle A hypothetical structure obtained by fusing the base of the coiled coil from the native HA structure with the top of the extended coiled coil from the low pH-converted HA structure. This panel helps distinguish the two major components of the HA conformational change on low pH treatment the existence of such an intermediate structure has not been shovm experimentally for influenza and may exist only transiently if at all. This extended structure, known as a prehairpin intermediate, has been detected indirectly in other virus envelope proteins (reviewed in Chan and Kim, 1998). Right Residues 38 to 127 from low pH-converted HA2 (Bullough et al, 1994). Hydrophobic residues that stabilize the jackknifed structure are indicated in one protomer as gray space-filling atoms. The amino (N) and carboxy (C) termini of a protomer within each trimer structure are indicated.

Uversky VN, Fink AL. Protein Misfolding, Aggregation and Conformational Diseases Part A Protein Aggregation and Conformational Diseases Series Protein Reviews. Volume 4. 2006. Springer, New York. 

Massey V. Activation of molecular oxygen by flavins and flavo-proteins review. J. Biol. Chem. 1994 269 22459-22462. 

Not only do these studies support the presence in blood platelets of receptors with two distinct binding affinities but s concept is also supported by earlier functional evidence that thrombin-induced platelet activation is mediated by two distinct pathways which differ in their sensitivity to proteolysis, their requirement for sodium ions, in the need for receptor occupancy and in the role of G proteins (reviewed in ). Furthermore, kinetic studies demonstrated that both ligand-receptor and proteolytic interactions occur in thrombin-induced platelet activation. Thus, foe preponderance of evidence supports foe view that two different types of receptor are involved in foe interaction of thrombin with platelets. The major question is, however, what is foe nature of these two receptors ... 

The ability to bind actin is an intrinsic capacity of coronin proteins (reviewed in refs. 1, 2). In some family members, it is ofren hard to define the bona fide actin binding domain because most parts of the molecule possess actin binding properties. There is at least one family member, however, which until to date has not been shown to physically interact or colocalizc with actin. Although it is quite possible that future research will reveal specific conditions, processes or cell types where mammalian coronin 7 (CRN7 current official symbol C0R07) associates with actin cytoskeleton, the current data surest that this family member is unique in that its function is irrelevant to the regulation of the cytoskeleton. 

Klein I, Sarkadi B, Varadi A. An inventory of the human ABC proteins (review). Biochim Biophys Acta 1999 1461 237-262. 

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