Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes (Q27660268)

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English	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes	scientific article

Statements

instance of

scholarly article

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title

Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes (English)

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main subject

vitamin

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vitamin B

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author

Tina Storm

object named as

Tina Storm

series ordinal

3

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Gregers R. Andersen

object named as

Gregers R Andersen

series ordinal

5

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Søren Kragh Moestrup

object named as

Søren K Moestrup

series ordinal

4

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author name string

Christian Brix Folsted Andersen

series ordinal

1

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Mette Madsen

series ordinal

2

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language of work or name

English

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publication date

18 March 2010

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published in

Nature

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volume

464

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issue

7287

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page(s)

445-8

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cites work

Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins

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X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement

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Assembly of the Intrinsic Factor Domains and Oligomerization of the Protein in the Presence of Cobalamin†

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The protein and the gene encoding the receptor for the cellular uptake of transcobalamin-bound cobalamin

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Phasercrystallographic software

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reference URL

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The human intrinsic factor-vitamin B12 receptor, cubilin: molecular characterization and chromosomal mapping of the gene to 10p within the autosomal recessive megaloblastic anemia (MGA1) region

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Receptor-mediated endocytosis in renal proximal tubule

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Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding

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Identification of the haemoglobin scavenger receptor.

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Identification of the C1q-binding Sites of Human C1r and C1s: a refined three-dimensional model of the C1 complex of complement

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Molecular Dissection of the Intrinsic Factor-Vitamin B12Receptor, Cubilin, Discloses Regions Important for Membrane Association and Ligand Binding

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Improved methods for building protein models in electron density maps and the location of errors in these models

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The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin

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Versatility in ligand recognition by LDL receptor family proteins: advances and frontiers

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Hereditary juvenile cobalamin deficiency caused by mutations in the intrinsic factor gene

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The intrinsic factor-vitamin B12 receptor, cubilin, is assembled into trimers via a coiled-coil alpha-helix

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Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors

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Mutations in CUBN, encoding the intrinsic factor-vitamin B12 receptor, cubilin, cause hereditary megaloblastic anaemia 1

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ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments

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Glycosylation is not required for ligand or receptor binding by expressed rat intrinsic factor

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Characterization of an epithelial approximately 460-kDa protein that facilitates endocytosis of intrinsic factor-vitamin B12 and binds receptor-associated protein

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Genetically heterogeneous selective intestinal malabsorption of vitamin B12: founder effects, consanguinity, and high clinical awareness explain aggregations in Scandinavia and the Middle East

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PHENIX: building new software for automated crystallographic structure determination

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PubMed

reference URL

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Crystal structure of human intrinsic factor: cobalamin complex at 2.6-A resolution

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20237569

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Cubilin P1297L mutation associated with hereditary megaloblastic anemia 1 causes impaired recognition of intrinsic factor-vitamin B(12) by cubilin

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20237569

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Inference of macromolecular assemblies from crystalline state

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20237569

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.

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PubMed

reference URL

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based on heuristic

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xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20237569

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The functional cobalamin (vitamin B12)-intrinsic factor receptor is a novel complex of cubilin and amnionless

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20237569

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2FNATURE08874

retrieved

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based on heuristic

inferred from DOI database lookup

PROCHECK: a program to check the stereochemical quality of protein structures

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2FNATURE08874

retrieved

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based on heuristic

inferred from DOI database lookup

Identifiers

DOI

10.1038/NATURE08874

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4558204

Dimensions Publication ID

1033660561

0 references

OpenCitations bibliographic resource ID

4558204

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4558204

PubMed publication ID

20237569

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4558204

 

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