Results 271 to 280 of about 4,630,754 (316)
Some of the next articles are maybe not open access.
DSC study of the thermal stability of S-protein and S-peptide/S-protein.
Biochemistry, 1996The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The process is reversible and can be assimilated to a two-state transition. The low values of denaturation temperature and enthalpy, between 38.5 and 40.0 °C and 165 and 180 kJ mol-1, respectively, demonstrate that the loss of S-peptide strongly decreases the ...
G. GRAZIANO +3 more
openaire +2 more sources
Protein S deficiency: a clinical perspective
Haemophilia, 2008Summary. Protein S (PS) is an extensively studied protein with an important function in the down‐regulation of thrombin generation. Because of the presence of a pseudogene and two different forms of PS in plasma, a bound and a free form, it is one of the most difficult thrombophilias to study.
Ten Kate, M. K., Van der Meer, J.
openaire +2 more sources
Regulation of coagulation by protein S
Current Opinion in Hematology, 2008Protein S has been one of the least mechanistically understood amongst the vitamin K-dependent coagulation proteins, and diagnosis of protein S deficiency and quantification of the associated thrombotic risk are not straightforward. In this review, the regulation of thrombin generation by protein S and the pathophysiological implications of protein S ...
Elisabetta, Castoldi, Tilman M, Hackeng
openaire +2 more sources
Conformation of ribonuclease S-protein
Experientia, 1979Ribonuclease S-protein exhibits a pH-dependent conformational transition between folded and unfolded states, and some unfolded S-protein persists up to pH 8. The histidine C2 proton resonance of the unfolded species was erroneously assigned by Bradbury et al. to histidine residue 119 of the folded species.
H, Shindo, S, Matsuura, J S, Cohen
openaire +2 more sources
Reassembly of S-layer proteins
Nanotechnology, 2014Crystalline bacterial cell surface layers (S-layers) represent the outermost cell envelope component in a broad range of bacteria and archaea. They are monomolecular arrays composed of a single protein or glycoprotein species and represent the simplest biological membranes developed during evolution.
Dietmar, Pum, Uwe B, Sleytr
openaire +2 more sources
Protein S and the Nephrotic Syndrome
Annals of Internal Medicine, 1988Excerpt To the editor: Vigano-D'Angelo and associates (1) present interesting hypotheses on protein S in nephrotic syndrome, but I do not believe their data support their conclusions.
openaire +2 more sources
The Role of S—S Groups in Proteins
1974The disulfide group is the most widespread of the covalent bonds in proteins that can link different parts of a polypeptide chain or different chains, and can thus play a part in maintaining the secondary, tertiary, and quaternary structures of proteins.
openaire +1 more source
The Clinical Investigator, 1992
Hereditary deficiencies of coagulation inhibitors like antithrombin III, protein C and protein S lead to an enhanced incidence of thromboembolic complications. Recently, acquired deficiencies of protein S were described in several disease states in which thromboembolic complications frequently occur. These acquired protein S deficiencies reach--in part-
openaire +2 more sources
Hereditary deficiencies of coagulation inhibitors like antithrombin III, protein C and protein S lead to an enhanced incidence of thromboembolic complications. Recently, acquired deficiencies of protein S were described in several disease states in which thromboembolic complications frequently occur. These acquired protein S deficiencies reach--in part-
openaire +2 more sources
S-Thiolation of Protein Sulfhydryls
1991Many cellular proteins have highly reactive sulfhydryls that are especially prone to modification during oxidative stress. Proteins with at least one “reactive” sulfhydryl are prevelant in cytoplasm, membranes, and nuclei, and the concentration of these reactive sites is impressive, reaching or exceeding the concentration of glutathione in many cells ...
J A, Thomas +5 more
openaire +2 more sources
Protein S-nitrosylation and cancer
Cancer Letters, 2012Protein S-nitrosylation is a covalent post-translational modification through coupling of a nitric oxide (NO) moiety with the reactive thiol group of a protein cysteine residue to form an S-nitrosothiol (SNO). S-nitrosylation is a key mechanism in the transmission of NO-based cellular signals in the vital cellular processes, including transcription ...
openaire +2 more sources