Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Biochemistry and Biotechnology  (2)
  • Life and Medical Sciences  (1)
  • 1
    Electronic Resource
    Electronic Resource
    A model of the platelet factor 4 complex with heparin (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 14 (1992), S. 277-287 
    Details
    ISSN: 0887-3585
    Keywords: α-helix ; lysine residues ; disaccharide units ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A model of heparin bound to bovine platelet factor 4 (BPF4) was completed using a graphically designed heparin molecule and the crystallographic coordinates of the native bovine platelet factor 4 tetramer. The oligosaccharides had a chain length of at least eight disaccharide units with the major repeating disaccharide unit consisting of (I→4)-O-(α-L-idopyranosyluronic acid 2-sulfate)-(l→4)-(2-deoxy-2-sulfamino-2-D-glucopyra-nosyl 6-sulfate). Each disaccharide unit carried a -4.0 charge. The structure of BPF4 was solved to 2.6 Å resolution with R = 0.237. Each monomer of BPF4 contains an α-helix lying across 3 strands of antiparallel β-sheet. Each helix has four lysines, which have been implicated in heparin binding. These lysine residues are predominantly on one side of the helix and are solvent accessible. Electrostatic calculations performed on the BPF4 tetramer show a ring of strong, positive charge which runs perpendicularly across the helices. Included in this ring of density is His-38, which has been shown by NMR to have a large pKa shift when heparin binds to BPF4. Our model of heparin bound to PF4 has the anionic polysaccharide perpendicular to the α-helices, wrapped about the tetramer along the ring of positive charge, and salt linked to all four lysines on the helix of each monomer. © 1992 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340140213
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Crystal structure of the complex of human α-thrombin and nonhydrolyzable bifunctional inhibitors, hirutonin - 2 and hirutonin - 6 (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 17 (1993), S. 252-265 
    Details
    ISSN: 0887-3585
    Keywords: thrombin ; bifunctional inhibitor ; crystal structure ; hirutonis ; drugdesing ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The crystal structure of the complexes of hirutonin-2 and hirutonin-6 with human α-thrombin have been solved and refined to R-factors of 0.169 (2.0 Å resolution) and 0.162 (201Å), respectively. Hirutonins belong to a family of bifunctional inhibitors bearing a noncleavable moiety mimicking the scissile bond. Hirutonin-2 is an analog of (D)Phe-Pro-Arg-Gly-hirudin49-65; hirutonin-6 has the same N-terminal tripeptide connected to a shortened fibrinogen exosite-binding part by a short, non-peptidyl linker. The hirutonin-6 molecule is well defined in the electron density with the exception of the C-terminal Leu-h61. The linker follows near the bottom of the canyon connecting the active site with the exosite, forms a short antiparallel β-sheet-like arrangement with Leu-40-Leu41 and makes van der Waals contacts with Glu39-Leu40-Leu41 of thrombin. In the thrombin-hirutonin-2 complex, the N- and C-terminal parts of the inhibitor are well or dered (except the C-terminal Gln-h65) while the central portion of the linker is partially disordered. The glycine analog in the P1′ position of hirutonin-2 assumes a conformation similar to that of the canonical form (Bode and Huber (1992) Eur. J. Biochem. 204 : 433-451) and supports the identification of the S1′ site as restricted by His57, Trp60D, Lys60F, and the Cys42-Cys58 disulfide bridge. The carbonyl oxygen of the P1 arginine residue is located in the oxyanion hole formed by the NH groups of Gly193 and Ser195, while the carbonyl carbon is positioned within a short distance, 2.8 Å, from the Oγ of Ser195. This resembles the conformation of the substrate-like inhibitors bound to other serine proteases. The N-terminal (D)Phe-pro-Arg fragment common to both inhibitors binds to thrombin in a fashion very similar to that of other inhibitors having this motif. The binding of the C-terminus of hirutonins to the fibrinogen-binding exosite is similar to that observed in hirudin and hirulog complexes. © 1993 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340170304
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Cobalt, chromium, and nickel concentrations in body fluids of patients with porous-coated knee or hip prostheses (1989)
    Hoboken, NJ [u.a.] : Wiley-Blackwell
    Journal of Orthopaedic Research 7 (1989), S. 307-315 
    Details
    ISSN: 0736-0266
    Keywords: Cobalt ; Chromium ; Nickel ; Total knee arthroplasty ; Total hip arthroplasty ; Prostheses, porous-coated ; Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Co, Cr, and Ni concentrations were determined by electrothermal atomic absorption spectrophotometry in serum and urine specimens collected from a group of 28 patients at intervals of from 1 day to 2.5 years after total knee or hip arthroplasty with porous-coated prostheses fabricated of Co-Cr alloy (ASTM F-75-82). Two control groups were also tested: (a) 42 healthy adults and (b) 16 orthopaedic patients after total knee or hip arthroplasty with porous-coated prostheses fabricated predominantly of Ti-Al-V alloy (ASTM F-136-84). All prostheses contained polyethylene components to avoid metal-to-metal contact. Mean Co concentrations in serum and urine were slightly increased in patients with Co-Cr knee implants at 6-120 weeks after surgery, compared with (a) preoperative values, (b) corresponding values in patients with Co-Cr hip implants, and (c) corresponding values in control patients with Ti-Al-V knee and hip prostheses. Substantially increased Co levels were observed in serum and urine of two patients at 7 weeks and 22 months postarthroplasty, associated with loosening of the prostheses; one of the patients also had elevated Cr levels in serum and urine. Although ASTM F-75-82 and F-136-84 alloys contain very little Ni (〈1.0 and 〈0.2% Ni, respectively, by wt), mean Ni concentrations in serum and urine were greatly increased at 1-2 days after implantation of Ti-Al-V and Co-Cr prostheses, diminishing by 2 weeks. The postoperative hypernickelemia and nickeluresis may reflect contamination of the operative field with Ni-containing particles from the drills, cutting jigs, and drilling jigs, or it may represent a previously unrecognized pathophysiological response to surgery.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jor.1100070302
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...