The α-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum (Q39175147)

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scientific article published on 26 March 2013

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English	The α-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum	scientific article published on 26 March 2013

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scholarly article

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Europe PubMed Central

PMC publication ID

9 September 2017

The α-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum (English)

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Europe PubMed Central

PMC publication ID

9 September 2017

endoplasmic reticulum

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Konstanze Winklhofer

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Konstanze F Winklhofer

8

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Nir Ben-Tal

5

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9

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Jörg Tatzelt

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Europe PubMed Central

9 September 2017

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2

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Ralf P Seidel

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Europe PubMed Central

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9 September 2017

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Daniela Dirndorfer

1

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Europe PubMed Central

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9 September 2017

Guy Nimrod

3

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9 September 2017

Margit Miesbauer

4

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PMC publication ID

9 September 2017

Martin Engelhard

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9 September 2017

Richard Zimmermann

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publication date

26 March 2013

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9 September 2017

Journal of Biological Chemistry

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9 September 2017

288

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9 September 2017

20

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Europe PubMed Central

PMC publication ID

9 September 2017

13961-13973

1 reference

Europe PubMed Central

PMC publication ID

9 September 2017

The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness

1 reference

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Fuzzy complexes: a more stochastic view of protein function

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The unfolded protein response: from stress pathway to homeostatic regulation

1 reference

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Protein quality control in the ER: balancing the ubiquitin checkbook

1 reference

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Fumarase: a paradigm of dual targeting and dual localized functions

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Protein folding and modification in the mammalian endoplasmic reticulum.

1 reference

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Protein translocation across the ER membrane

1 reference

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10 September 2017

Quality and quantity control at the endoplasmic reticulum

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Understanding protein non-folding.

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Function and structure of inherently disordered proteins

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Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

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Role of a pro-sequence in the secretory pathway of prothyrotropin-releasing hormone

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Neuronostatin encoded by the somatostatin gene regulates neuronal, cardiovascular, and metabolic functions

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The concept of translocational regulation

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Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome

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The Jpred 3 secondary structure prediction server

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The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum

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Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

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The role of p58IPK in protecting the stressed endoplasmic reticulum

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Predicting mostly disordered proteins by using structure-unknown protein data

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Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway

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Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload

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The surprising complexity of signal sequences

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ERAD: the long road to destruction

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IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content

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RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins

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Intrinsically unstructured proteins and their functions

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Comparing and combining predictors of mostly disordered proteins.

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Improved prediction of signal peptides: SignalP 3.0

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Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

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Quality control in the endoplasmic reticulum

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Jekyll-Hyde neurotrophins: the story of proNGF

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Different conformations of nascent polypeptides during translocation across the ER membrane

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Caspase activation: the induced-proximity model

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Protein secondary structure prediction based on position-specific scoring matrices

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alpha-Factor pro-peptide N-linked oligosaccharides facilitate secretion of the insulin precursor in Saccharomyces cerevisiae

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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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NMR structure of the mouse prion protein domain PrP(121-231)

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A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain

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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum

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Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor

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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

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Signal sequences. The limits of variation

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alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum

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1 reference

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The C-terminal Globular Domain of the Prion Protein Is Necessary and Sufficient for Import into the Endoplasmic Reticulum

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Signal sequences: more than just greasy peptides

1 reference

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based on heuristic

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Proteasomal Degradation and N-terminal Protease Resistance of the Codon 145 Mutant Prion Protein

1 reference

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based on heuristic

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Secondary structure formation of a transmembrane segment in Kv channels

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M112.430264

1 reference

Europe PubMed Central

PMC publication ID

9 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 September 2017

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