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1 e coagulation assays, and reversibility with protamine sulfate.
2 onic detergents or the antimicrobial peptide protamine sulfate.
3 ionic strength buffer and buffers containing protamine sulfate.
4 tivate PKC in cells by the same mechanism as protamine sulfate.
5  known glycosaminoglycan binders, surfen and protamine sulfate.
6 % to 0.2% Reh cells), and in suspension with protamine sulfate (0.7% to 3.1% for Nalm-6 cells and 0%
7 before study agent (sample 1), 10 mins after protamine sulfate administration after cardiopulmonary b
8 ailed antagonism of the activation of PKC by protamine sulfate and did not involve competition with e
9             In a typical case, coassembly of protamine sulfate and perylene dye via electrostatic att
10                               The effects of protamine sulfate and vanadate on Nephrin phosphorylatio
11 and fluorescent dye permeability of control, protamine sulfate- and lipopolysaccharide-treated denude
12 sulated with pancreatic islet cells by using protamine sulfate as a clinical-grade alginate cross lin
13                                  Conversely, protamine sulfate, as a stronger competitor for heparin,
14                                              Protamine sulfate can be administered at the conclusion
15 s and other mammalian cells with ferumoxides-protamine sulfate complexes (FE-Pro), cellular toxicity,
16 ated SPIO used as an MRI contrast agent, and protamine sulfate, conventionally used to reverse hepari
17 ion of cellular PKC substrates that resemble protamine sulfate in their interactions with PKC may con
18 and high affinity SAPD binding and inhibited protamine sulfate-induced activity.
19 d chelation of extracellular calcium reduced protamine sulfate-induced damage, suggesting that calciu
20 eficient mice display impaired recovery from protamine sulfate-induced foot process effacement and li
21                             On the contrary, protamine sulfate-induced phosphorylation at Tyr-1176/11
22 npo(-/-) mice display impaired recovery from protamine sulfate-induced podocyte foot process (FP) eff
23 l facet cell QIRs with the cationic protein, protamine sulfate, led to epithelial exfoliation and era
24  the cathepsin L inhibitor E64 all inhibited protamine sulfate-mediated barrier changes, which sugges
25  was measured in the presence and absence of protamine sulfate on the cytoplasmic side of the channel
26 with wild-type littermates injured by either protamine sulfate or nephrotoxic serum (NTS).
27 n subjected to podocyte injury in vivo using protamine sulfate or nephrotoxic serum (NTS).
28 ted in GECs from puromycin aminonucleoside-, protamine sulfate-, or sialidase-treated rats, which sho
29         In a mouse model of podocyte injury, protamine sulfate perfusion of the Cfl1 mutant mouse ind
30 e podocyte foot process effacement following protamine sulfate perfusion.
31               Resveratrol potently inhibited protamine sulfate phosphorylation (IC(50) = 10 microM) b
32 ralized by heparin-binding proteins, such as protamine sulfate, platelet factor-4, and beta-thrombogl
33 ytoadherence, whereas the positively charged protamine sulfate promoted cytoadherence.
34 particles with various ratios of CaCO(3) and protamine sulfate (PS) were used to transfect pDNA encod
35 idance stress (WAS) and/or acute exposure to protamine sulfate (PS).
36                            Administration of protamine sulfate rapidly damaged the isolated glomeruli
37 ons in this model using high-dose heparin or protamine sulfate support the pathogenic role of surface
38  infusion of the positively charged protein, protamine sulfate, the reverse was observed with mPF4(+/
39 of heparin alone or in the administration of protamine sulfate to reverse heparin anticoagulation dur
40 medium supplemented with growth factors, and protamine sulfate was replaced 4 times over a 48-hour pe
41       AC133(+) cells labeled with ferumoxide-protamine sulfate were mixed with either rat glioma or h
42 ctions with native PKCalpha were enhanced by protamine sulfate, which activates the enzyme without re
43                                     Cationic protamine sulfate, which forms similar complexes with he
44 lation of the cofactor-independent substrate protamine sulfate, which is a polybasic protein that act