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1 complex formed between streptococcal M1 and human fibrinogen.
2 s the RGD572-574 motif in the alpha chain of human fibrinogen.
3 ish between glycosylation of the porcine and human fibrinogens.
5 ers than their respective control rabbit and human fibrinogens; (2) the clot structure could be made
7 ructure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution
11 These results indicate that both bovine and human fibrinogen alpha C-domains consist of a compact gl
14 forms against several substrates, including human fibrinogen and beta-chain insulin, was the Ser-1-G
16 y inactivated preparation of highly purified human fibrinogen and human thrombin that includes aproti
21 ifically homotypic, because immobilized BSA, human fibrinogen, and fibronectin cannot substitute for
22 d over the course of thrombin reactions with human fibrinogen are only half of what would be expected
23 These results indicate that an RGD site in human fibrinogen at either position alpha252-254 or posi
27 ng the genomic sequence for one of the three human fibrinogen chains controlled by sheep whey protein
28 d by a crystal structure of the D-dimer from human fibrinogen cocrystallized with GHRPYam, the packin
29 iologic concentrations of 0.15 to 0.5 mg/mL, human fibrinogen dose-dependently enhanced by threefold
30 d to support human leukocyte adhesion, while human fibrinogen enhanced monocytic cell attachment to r
31 epidermidis that binds to the Bbeta chain of human fibrinogen (Fg) and is necessary and sufficient fo
32 e dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observe
34 ach at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and pre
35 Analysis of N-glycan mixtures derived from human fibrinogen further demonstrated that AP MALDI-FT I
39 se sequences are nearly identical to the two human fibrinogen glycopeptides, Val-Glu-Asn(CHO)-Lys (ga
42 ructure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 A resolu
43 n of the A alpha chain (residues 220-610) of human fibrinogen have been hampered by the difficulty of
44 tropicity, and many of these strains express human fibrinogen (hFg) binding Pattern A-C M-proteins, e
46 is a recently identified subclass of normal human fibrinogen in which two extended alpha chain isofo
49 ys measuring whole-cell S. aureus binding to human fibrinogen, MAb 12-9 inhibited S. aureus binding b
51 eek fetal liver were nicotinamide deaminase, human fibrinogen-related protein and alpha-acid glycopro
52 We hypothesized that the alpha C-domain of human fibrinogen (residues hA alpha 221-610) and of othe
53 he beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is esse
55 ure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to
56 founder animal demonstrated the presence of human fibrinogen subunits at concentrations of 2000 micr
60 Aalpha251 matrix and matrices generated from human fibrinogen variants lacking the alphaC regions sup
61 ystem organ microthrombi study in which 125I-human fibrinogen was injected 30 min prior to an endotox
62 the gamma or gamma' chains, respectively, of human fibrinogen were expressed in yeast (Pichia pastori
63 wild-type strain cleaved the alpha chain of human fibrinogen, whereas a cspA mutant, TOH121, was una
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