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
  • 1995-1999  (2)
  • 1985-1989  (1)
  • 1970-1974
  • Chemistry  (2)
  • retinol binding protein  (2)
  • Clivus length  (1)
Source
Material
Years
  • 1995-1999  (2)
  • 1985-1989  (1)
  • 1970-1974
  • 1990-1994  (4)
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Skull radiograph measurements of normals and patients with basilar impression; use of Landzert's angle (1987)
    Springer
    Surgical and radiologic anatomy 9 (1987), S. 225-229 
    Details
    ISSN: 1279-8517
    Keywords: Basilar impression ; Landzert's basal angle ; Clivus length ; Cervical canal
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé Cent crânes normaux ont été étudiés sur des radiographies de profil ainsi que dix crânes pathologiques présentant des impressions basilaires chez des patients traités à l'HÔpital Kenyatta de Nairobi. La plus courte distance moyenne entre le sommet de l'odontoÏde et la ligne basale de McGregor a été de 1,2±2,28 mm au-dessous de la ligne basale (extrÊmes étendues de 6 mm au-dessous à 3 mm au-dessus de la ligne basale), chez les sujets normaux et de 9±2,7 mm (6–14 mm) au-dessus de la ligne basale chez les sujets pathologiques. L'angle basai moyen était de 113
    Notes: Summary One hundred normal lateral skull radiographs were studied and those of ten patients with basilar impression attending Kenyatta Hospital, Nairobi. The mean shortest distance of the odontoid tip to McGregor's basal line was 1.2±2.28 mm below the basal line (range 6 mm below to 3 mm above basal line), in normals and 9±2.7 mm (6–14 mm) above basal line in patients. The mean basal angle was 113
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02109633
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Dissection of multi-protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol-binding protein complexes (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 33 (1998), S. 3-11 
    Details
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Dissection of multi-protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol-binding protein complexes (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 33 (1998), S. 3-11 
    Details
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...