(Q43843392)

English

6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis

scientific article published on 28 December 2001

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

2

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

author name string

Ravi Mahadeva

1

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Robin W Carrell

3

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

David A Lomas

4

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

language of work or name

0 references

publication date

28 December 2001

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

277

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

9

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

6771-6774

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

An atlas of serpin conformations.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

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

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Major proteinase movement upon stable serpin-proteinase complex formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Structure of a serpin-protease complex shows inhibition by deformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

What do dysfunctional serpins tell us about molecular mobility and disease?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

The mechanism of Z alpha 1-antitrypsin accumulation in the liver

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Heteropolymerization of S, I, and Z alpha1-antitrypsin and liver cirrhosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Probing serpin reactive-loop conformations by proteolytic cleavage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Cleaved antitrypsin polymers at atomic resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

A 2.6 A structure of a serpin polymer and implications for conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

A Kinetic Mechanism for the Polymerization of α1-Antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

The structure of a serpin-protease complex revealed by intramolecular distance measurements using donor-donor energy migration and mapping of interaction sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Structural explanation for the deficiency of S alpha 1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Risk of cirrhosis and primary liver cancer in alpha 1-antitrypsin deficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Prevention of polymerization of M and Z alpha1-Antitrypsin (alpha1-AT) with trimethylamine N-oxide. Implications for the treatment of alpha1-at deficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Preparation and characterization of latent alpha 1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C100722200

21 January 2018

Identifiers

10.1074/JBC.C100722200

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

ResearchGate publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q43843392&oldid=2103813615"