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| - artículu científicu espublizáu en 2003 (ast)
- vědecký článek publikovaný v roce 2003 (cs)
- 2003 թվականի ապրիլին հրատարակված գիտական հոդված (hy)
- наукова стаття, опублікована у квітні 2003 (uk)
- 2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw)
- مقالة علمية (نشرت في أبريل 2003) (ar)
- научни чланак (објављен 2003-04) (sr)
- article scientifique (publié 2003-04) (fr)
- articolo scientifico (pubblicato il 2003-04) (it)
- artigo científico (publicado na 2003-04) (pt)
- vedecký článok (publikovaný 2003-04) (sk)
- videnskabelig artikel (udgivet 2003-04) (da)
- wetenschappelijk artikel (gepubliceerd op 2003-04) (nl)
- scientific article (publication date: April 2003) (en)
- im April 2003 veröffentlichter wissenschaftlicher Artikel (de)
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| - James A Irving
- Lisa D Cabrita
- Robert N Pike
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| rdfs:label
| - The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (en)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (nl)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (ast)
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| skos:prefLabel
| - The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (en)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (nl)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (ast)
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| name
| - The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (en)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (nl)
- The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (ast)
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| author
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| author
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| title
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| title
| - The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment (en)
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| DOI
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| DOI
| - 10.1016/S0969-2126(03)00057-1
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| is about
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| is cites work
of | - Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions
- An overview of the serpin superfamily
- Serpins in plants and green algae
- The N terminus of the serpin, tengpin, functions to trap the metastable native state
- A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome
- Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function
- Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop
- Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution
- How do proteins avoid becoming too stable? Biophysical studies into metastable proteins
- Local and global effects of a cavity filling mutation in a metastable serpin
- Siropins, novel serine protease inhibitors from gut microbiota acting on human proteases involved in inflammatory bowel diseases.
- The serpin gene family in Anopheles gambiae.
- Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides
- Serpins in rice: protein sequence analysis, phylogeny and gene expression during development.
- Structure-function relationship of SW-AT-1, a serpin-type protease inhibitor in silkworm
- Serine protease inhibitors and human wellbeing interplay: new insights for old friends
- Pnserpin: A Novel Serine Protease Inhibitor from Extremophile Pyrobaculum neutrophilum
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