(Q74114981)

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The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes

scientific article published on 15 May 2002

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scholarly article

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9 November 2019

The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes (English)

1 reference

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9 November 2019

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Steven J Kolodziej

1

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9 November 2019

Terence Wagenknecht

2

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9 November 2019

Dudley K Strickland

3

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9 November 2019

James K Stoops

4

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9 November 2019

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15 May 2002

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9 November 2019

Journal of Biological Chemistry

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9 November 2019

277

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9 November 2019

28031-28037

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9 November 2019

31

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9 November 2019

Immunoglobulins and complement components in human aortic atherosclerotic intima

1 reference

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Distinct binding sites in the structure of alpha 2-macroglobulin mediate the interaction with beta-amyloid peptide and growth factors

1 reference

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The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin

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21 January 2018

Similar architectures of native and transformed human alpha2-macroglobulin suggest the transformation mechanism.

1 reference

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21 January 2018

Three-dimensional structures of the human α2-macroglobulin-methylamine and chymotrypsin complexes

1 reference

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21 January 2018

The novel three-dimensional structure of native human alpha 2-macroglobulin and comparisons with the structure of the methylamine derivative

1 reference

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21 January 2018

Low resolution X-ray structure of human methylamine-treated alpha 2-macroglobulin.

1 reference

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21 January 2018

The structure of the C949S mutant human alpha(2)-macroglobulin demonstrates the critical role of the internal thiol esters in its proteinase-entrapping structural transformation

1 reference

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21 January 2018

Thiol ester role in correct folding and conformation of human alpha 2-macroglobulin. Properties of recombinant C949S variant

1 reference

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21 January 2018

Structural details of proteinase entrapment by human alpha2-macroglobulin emerge from three-dimensional reconstructions of Fab labeled native, half-transformed, and transformed molecules

1 reference

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21 January 2018

Alpha 2-macroglobulin bait region variants. A role for the bait region in tetramer formation

1 reference

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21 January 2018

Ultrastructure of alpha 2-macroglobulins

1 reference

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21 January 2018

Evidence for active half-molecules of alpha 2-macroglobulin formed by dissociation in urea

1 reference

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21 January 2018

Structural studies of human alpha 2-macroglobulin: concordance between projected views obtained by negative-stain and cryoelectron microscopy

1 reference

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21 January 2018

Comparisons of the low-resolution structures of ornithine decarboxylase by electron microscopy and X-ray crystallography: the utility of methylamine tungstate stain and Butvar support film in the study of macromolecules by transmission electron micr

1 reference

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21 January 2018

Utility of Butvar support film and methylamine tungstate stain in three-dimensional electron microscopy: agreement between stain and frozen-hydrated reconstructions

1 reference

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21 January 2018

Localization of ribosomal proteins on the surface of ribosomal subunits from Escherichia coli using immunoelectron microscopy.

1 reference

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21 January 2018

EMAN: semiautomated software for high-resolution single-particle reconstructions

1 reference

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21 January 2018

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

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21 January 2018

Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids

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21 January 2018

The correlation averaging of a regularly arranged bacterial cell envelope protein

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21 January 2018

SUPRIM: easily modified image processing software.

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21 January 2018

The conformational state of human alpha 2-macroglobulin influences its dissociation into half-molecules by sodium thiocyanate.

1 reference

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21 January 2018

Electron microscope studies of human alpha 2-macroglobulin-chymotrypsin complex: demonstration that the two structures assigned to native and proteolyzed alpha 2-macroglobulin represent two views of the proteolyzed molecule

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202714200

21 January 2018

Separation and localization of the four cysteine-949 residues in human .alpha.2-macroglobulin using fluorescence energy transfer

1 reference

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21 January 2018

Proximity of thiol esters and bait region in human alpha 2-macroglobulin: paramagnetic mapping

1 reference

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21 January 2018

Immunoelectron microscopy studies with a monoclonal antibody directed against a receptor recognition site epitope in human ?2-macroglobulin*1

1 reference

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21 January 2018

The structure of α2-macroglobulin-methylamine after papain digestion as determined by electron microscopy

1 reference

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21 January 2018

On the structural changes of native human alpha2-macroglobulin upon proteinase entrapment. Three-dimensional structure of the half-transformed molecule

1 reference

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21 January 2018

The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature

1 reference

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21 January 2018

Bait region involvement in the dimer-dimer interface of human alpha 2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides

1 reference

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21 January 2018

Three-dimensional structure of the human plasmin alpha2-macroglobulin complex

1 reference

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21 January 2018

The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

1 reference

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21 January 2018

Protein binding of pancreatic proteolytic enzymes

1 reference

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21 January 2018

Polarization fluorescence studies on proteolytic activity of alpha 2-macroglobulin-trypsin complexes

1 reference

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21 January 2018

In support of the trap hypothesis. Chymotrypsin is not rigidly held in its complex with human alpha 2-macroglobulin

1 reference

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21 January 2018

Structure of alpha-chymotrypsin refined at 1.68 A resolution

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M202714200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12015318%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12015318%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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