Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase (Q28610913)

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English	Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase	scientific journal article

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scholarly article

1 reference

3 February 2017

Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase (English)

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3 February 2017

author name string

Karthe Ponnuraj

1

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3 February 2017

Yuanyuan Xu

2

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3 February 2017

Kevin Macon

3

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3 February 2017

Dwight Moore

4

1 reference

3 February 2017

John E. Volanakis

5

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3 February 2017

Sthanam V. L. Narayana

6

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3 February 2017

publication date

9 April 2004

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3 February 2017

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3 February 2017

14

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3 February 2017

1

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3 February 2017

17–28

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3 February 2017

Nickel and cobalt activate complement factor C3 faster than magnesium

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Structural basis of collagen recognition by integrin alpha2beta1

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New synthetic inhibitors of C1r̄, C1 esterase, thrombin, plasmin, kallikrein and trypsin

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Metal-dependent conformational changes in a recombinant vWF-A domain from human factor B: a solution study by circular dichroism, fourier transform infrared and (1)H NMR spectroscopy.

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Searching protein structure databases has come of age.

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Studies on esterolytic activity of alternative complement component factor B

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Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity

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New structural motifs on the chymotrypsin fold and their potential roles in complement factor B

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Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

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Crystal structure of a complement factor D mutant expressing enhanced catalytic activity

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Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)

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An isolated, surface-expressed I domain of the integrin alphaLbeta2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond.

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Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl)trypsin

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Solvent content of protein crystals

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Structure of human factor D. A complement system protein at 2.0 A resolution

1 reference

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AMoRe: an automated package for molecular replacement

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Processing of X-ray diffraction data collected in oscillation mode

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The C3 convertase of the alternative pathway of human complement. Enzymic properties of the bimolecular proteinase

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Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold

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Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo

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Stabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds.

1 reference

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Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation

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MHC Class III products: an electron microscopic study of the C3 convertases of human complement

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C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1

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Induced fit activation mechanism of the exceptionally specific serine protease, complement factor D

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Surface Loops Adjacent to the Cation-Binding Site of the Complement Factor B von Willebrand Factor Type A Module Determine C3b Binding Specificity†

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Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding

1 reference

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Structural biology of the alternative pathway convertase

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Identifiers

10.1016/S1097-2765(04)00160-1

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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