Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex (Q24677661)

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Language	Label	Description	Also known as
English	Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex	scientific article

Statements

instance of

scholarly article

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title

Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex (English)

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main subject

structural biology

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author name string

Rhiannon R Penkert

series ordinal

1

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Heather M DiVittorio

series ordinal

2

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Kenneth E Prehoda

series ordinal

3

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language of work or name

English

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publication date

November 2004

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published in

Nature Structural & Molecular Biology

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volume

11

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issue

11

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page(s)

1122-7

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cites work

CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells

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PubMed Central

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Direct interaction of two polarity complexes implicated in epithelial tight junction assembly

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7 April 2017

The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost

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PubMed Central

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Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins

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7 April 2017

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex

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7 April 2017

Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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7 April 2017

Implementation of molecular replacement in AMoRe

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7 April 2017

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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PubMed Central

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

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PubMed Central

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Assembly of Cell Regulatory Systems Through Protein Interaction Domains

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7 April 2017

Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1)

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7 April 2017

Mechanism and role of PDZ domains in signaling complex assembly

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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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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis

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Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition

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28 September 2017

PDZ domains-glue and guide.

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PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain

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Cyclic peptides as non-carboxyl-terminal ligands of syntrophin PDZ domains

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PubMed Central

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Role of electrostatic interactions in PDZ domain ligand recognition

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21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

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21 January 2018

Identifiers

DOI

10.1038/NSMB839

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

40424

Dimensions Publication ID

1035415318

0 references

OpenCitations bibliographic resource ID

40424

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

40424

PMC publication ID

2140275

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

40424

PubMed publication ID

15475968

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

40424

ResearchGate publication ID

8239892

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