(Q44639262)

English

α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition

scientific article published on October 30, 2003

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scholarly article

1 reference

Europe PubMed Central

4 December 2017

alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibition (English)

1 reference

Europe PubMed Central

4 December 2017

α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition (English)

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

author name string

József Dobó

1

1 reference

Europe PubMed Central

4 December 2017

Peter G. W. Gettins

2

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14593107

27 March 2024

language of work or name

0 references

publication date

30 October 2003

1 reference

Europe PubMed Central

4 December 2017

full work available at URL

http://www.jbc.org/content/279/10/9264.full.pdf

Portable Document Format

online access status

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14593107

27 March 2024

https://api.elsevier.com/content/article/PII:S0021925817478343?httpAccept=text/xml

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

https://api.elsevier.com/content/article/PII:S0021925817478343?httpAccept=text/plain

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

https://syndication.highwire.org/content/doi/10.1074/jbc.M311731200

1 reference

10.1074/JBC.M311731200

https://api.crossref.org/works/10.1074/JBC.M311731200

27 March 2024

Journal of Biological Chemistry

1 reference

Europe PubMed Central

4 December 2017

279

1 reference

Europe PubMed Central

4 December 2017

10

1 reference

Europe PubMed Central

4 December 2017

9264-9269

1 reference

Europe PubMed Central

4 December 2017

Serpin structure, mechanism, and function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Structural basis for serpin inhibitor activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

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.M311731200

21 January 2018

Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Major proteinase movement upon stable serpin-proteinase complex formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Structure of a serpin-protease complex shows inhibition by deformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

The structure of a Michaelis serpin-protease complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

The reaction of serpins with proteinases involves important enthalpy changes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Structural similarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use of site-specific fluorescent probes of local environment

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Insight into the mechanism of serpin-proteinase inhibition from 2D [1H-15N] NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Formation of the covalent chymotrypsin.antichymotrypsin complex involves no large-scale movement of the enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Mechanism of action of naturally occurring proteinase inhibitors. Studies with anhydrotrypsin and anhydrochymotrypsin purified by affinity chromatography.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Serpin-protease complexes are trapped as stable acyl-enzyme intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

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.M311731200

21 January 2018

Formation of a noncovalent serpin-proteinase complex involves no conformational change in the serpin. Use of 1H-15N HSQC NMR as a sensitive nonperturbing monitor of conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Evidence that translocation of the proteinase precedes its acylation in the serpin inhibition pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Metastability in the inhibitory mechanism of human alpha1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

The preparation of anhydro-trypsin and its reactivity with naturally occurring proteinase inhibitors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin-proteinase complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311731200

21 January 2018

Identifiers

10.1074/JBC.M311731200

1 reference

Europe PubMed Central

4 December 2017

release_ahadqpznirexxnge762nfx5mpy

1 reference

https://api.fatcat.wiki/v0/release/ahadqpznirexxnge762nfx5mpy

24 November 2022

based on heuristic

mapped directly with Wikidata item

1 reference

Europe PubMed Central

4 December 2017

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