Skip to content
VuFind
    • English
    • Deutsch
    • Español
    • Français
    • Italiano
    • 日本語
    • Nederlands
    • Português
    • Português (Brasil)
    • 中文(简体)
    • 中文(繁體)
    • Türkçe
    • עברית
    • Gaeilge
    • Cymraeg
    • Ελληνικά
    • Català
    • Euskara
    • Русский
    • Čeština
    • Suomi
    • Svenska
    • polski
    • Dansk
    • slovenščina
    • اللغة العربية
    • বাংলা
    • Galego
    • Tiếng Việt
    • Hrvatski
    • हिंदी
    • Հայերէն
    • Українська
    • Sámegiella
    • Монгол
Advanced
  • Structural and functional anat...
  • Cite this
  • Text this
  • Email this
  • Print
  • Export Record
    • Export to RefWorks
    • Export to EndNoteWeb
    • Export to EndNote
  • Permanent link
Structural and functional anatomy of the globular domain of complement protein C1q (vol 95, pg 113, 2004)

Structural and functional anatomy of the globular domain of complement protein C1q (vol 95, pg 113, 2004)

Bibliographic Details
Main Authors: Kishore, U, Ghai, R, Greenhough, T, Shrive, A, Bonifati, D, Gadjeva, MG, Waters, P, Kojouharova, MS, Chakraborty, T, Agrawal, A
Format: Journal article
Published: 2005
  • Holdings
  • Description
  • Similar Items
  • Staff View

Similar Items

  • Erratum: Structural and functional anatomy of the globular domain of complement protein C1q (Immunology Letters (2004) 95:2 (113-128) DOI: 10.1016/j.imlet.2004.06.015)
    by: Kishore, U, et al.
    Published: (2005)
  • Structural and functional anatomy of the globular domain of complement protein C1q.
    by: Kishore, U, et al.
    Published: (2004)
  • Role of Ca2+ in the electrostatic stability and the functional activity of the globular domain of human C1q.
    by: Roumenina, LT, et al.
    Published: (2005)
  • Recombinant forms of monomeric and homotrimeric globular regions of human C1q as inhibitors of complement and microglia activation induced by beta-amyloid and familial dementia peptides
    by: Nayak, A, et al.
    Published: (2010)
  • Mutational analyses of the recombinant globular regions of human C1q A, B, and C chains suggest an essential role for arginine and histidine residues in the C1q-IgG interaction.
    by: Kojouharova, MS, et al.
    Published: (2004)

Search Options

  • Search History
  • Advanced Search

Find More

  • Browse the Catalog
  • Browse Alphabetically
  • Explore Channels
  • Course Reserves
  • New Items

Need Help?

  • Search Tips
  • Ask a Librarian
  • FAQs