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Serpin: History, Biological function and localization & Conformational change and inhibitory mechanism

Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors). They are notable for their…

Language: English [EN]
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Serpin topic overview

The analysis highlights History, Biological function and localization and Conformational change and inhibitory mechanism as prominent areas in the source structure around Serpin.

Related topics
192
Source areas
10
Connected nodes
202
Extracted relationships
245
Concept neighborhoods
41
Bridge connections
202

What this topic covers Research coverage

Source areas are shown by the number of related topics found in each part of the analysis. Use smaller areas too: they can reveal specialized angles and content gaps.

Overview · 47 topics
Biological function and localization · 31 topics
Distribution · 28 topics
Conformational change and inhibitory mechanism · 25 topics
Disease and serpinopathies · 20 topics
Activity · 14 topics
History · 11 topics
Structure · 6 topics
Degradation · 5 topics
Evolution · 5 topics

Smaller areas are not necessarily less important. They contain fewer connections in this analysis and can be useful for finding specialized angles or coverage gaps.

Key facts & relationships

High-confidence facts extracted from structured source data. Use them as anchors for further research.

AlphaFold
IPR000215 · PF00079
Available protein structures:
IPR000215 · PF00079
CDD
cd00172
InterPro
IPR000215
PDB
1m37A:1-378 1hleB:349-379 1jrrA:1-415 1by7A:1-415 1ovaA:1-385 1uhgA:1-385 1jtiB:1-385 1attB:77-433 1nq9L:76-461 1oyhI:76-461 1e03L:76-461 1e05I:76-461 1br8L:76-461 1r1lL:76-461…
Pfam
PF00079

Explore all related topics Closing gaps

Browse the complete topic structure, not only the most central items. Less prominent entities and concepts can reveal missing angles, specialized context and useful research gaps. Each item opens a new analysis centered on that subject.

Overview

History

Activity

Biological function and localization

Structure

Conformational change and inhibitory mechanism

Degradation

Disease and serpinopathies

Evolution

Distribution

Advanced semantic analysis

Deeper signals for content research, entity SEO and topical coverage. The plain-language headings explain what each technical view is useful for.

How Serpin connects Entity context

The extracted context around Serpin shows recurring relationship patterns in the source. For example, Serpin → Archived, CambridgeFrank Church, Chapel HillPaul Declerck, ChicagoOverview, December, Family I4, Human Alpha-1-antitrypsin, Illinois, James Whisstock, Katholieke Universiteit LeuvenTom Roberts, Medicine Medical Subject Headings, MeSH, Monash UniversityJim Huntington, Month SerpinMerops, National Library, North Carolina, October, P01009, PDB, PDB Molecule Another extracted example is Serpin → After, Fondaparinux, For, Furthermore, Heparin, II, In, MENT, P1, RCL, The, The X-ray, This, Understanding, Upon, Xa. Use these groups to spot repeated connection types before inspecting the individual relationships.

Serpin

Top relations

related to External links · 28
Serpin → Archived, CambridgeFrank Church, Chapel HillPaul Declerck, ChicagoOverview, December, Family I4, Human Alpha-1-antitrypsin, Illinois, James Whisstock, Katholieke Universiteit LeuvenTom Roberts, Medicine Medical Subject Headings, MeSH, Monash UniversityJim Huntington, Month SerpinMerops, National Library, North Carolina, October, P01009, PDB, PDB Molecule
related to Allosteric activation · 16
Serpin → After, Fondaparinux, For, Furthermore, Heparin, II, In, MENT, P1, RCL, The, The X-ray, This, Understanding, Upon, Xa
related to Insect · 16
Serpin → Accordingly, Amino, As, Drosophila, Easter, Gastrulation Defective, In Tenebrio, Nudel, Serpin-27A, Snake, SPN93, Spätzle, Studies, The, The Drosophila, Thirteen
related to Latent conformation · 15
Serpin → Although PAI-1, C-sheet, Certain, Disruption, Finally, Latent, N-terminal, N-terminus, PAI-1, RCL, Regulation, Similarly, Since, The, Thermoanaerobacter
related to Polymerisation and aggregation · 15
Serpin → A-sheet, C1-inhibitor, Each, FENIB, First, HAE, However, In, RCL, Second, Serpinopathies, Serpins, The, Well-characterised, Within
related to Conformational change and inhibitory mechanism · 12
Serpin → C-terminus, For, However, Inhibitory, Initially, Instead, Kunitz-type, N-terminus, RCL, Serine, The, This
related to Plant · 11
Serpin → Although, Arabidopsis, BSZx, CmPS-1, However, In, It, Plant, The, The RCL, Zx
related to Protease inhibition · 10
Serpin → Approximately, By, C1-inhibitor, For, Further, In, Nevertheless, PAI-1, Serpin B9, The
related to Activity · 9
Serpin → B4, Examples, MENT, Most, Nonetheless, SCCA-1, Serpins, Some, These
related to Degradation · 9
Serpin → Drosophila, For, LDL, Lipophorin Receptor-1, LRP, One, PAI-1, Similarly, When

Important terminology

Use these terms to understand the vocabulary surrounding the topic, not as a checklist for keyword stuffing.

Important terminology

serpins protease proteases inhibitors also conformational change mechanism antithrombin protein structure rcl inhibitory function proteins active human plant cysteine serine

Serpin relationships Subject–Predicate–Object triples

TTTA extracted 245 structured relationships around Serpin. Examples in this analysis include Serpin → AlphaFold → IPR000215 and Serpin → AlphaFold → PF00079. The table shows each extracted connection, where it came from and its confidence.

SubjectPredicateObjectConfidenceSrc
SerpinAlphaFoldIPR0002151.00infobox
SerpinAlphaFoldPF000791.00infobox
SerpinAvailable protein structures:IPR0002151.00infobox
SerpinAvailable protein structures:PF000791.00infobox
SerpinCDDcd001721.00infobox
SerpinInterProIPR0002151.00infobox
SerpinPDB1m37A:1-378 1hleB:349-379 1jrrA:1-415 1by7A:1-415 1ovaA:1-385 1uhgA:1-385 1jtiB:1-385 1attB:77-433 1nq9L:76-461 1oyhI:76-461 1e03L:76-461 1e05I:76-461 1br8L:76-461 1r1lL:76-461…1.00infobox
SerpinPfamPF000791.00infobox
SerpinPROSITEPDOC002561.00infobox
SerpinSCOP21hle / SCOPe / SUPFAM1.00infobox
SerpinSymbolSerpin, SERPIN (root symbol of family)1.00infobox
protein misfoldinginstance ofserpins are vulnerable to mutations that can result in serpinopathies0.80text

Related concept clusters Concept neighborhoods

The concept neighborhoods around Serpin bring nearby vocabulary together. In this analysis, examples include Serpins, Protein and Inhibitory. Use the clusters to find adjacent concepts and terminology that may deserve separate research.

  • Serpin
    • Serpins
    • Protein
    • Inhibitory
    • Conformational
    • Change
    • Cell
    • Human
    • Function
    • Non-inhibitory
    • Transition
    • Cause
    • Mutations
  • serpin
    • Serpins
    • Protein
    • Inhibitory
    • Conformational
    • Change
    • Cell
    • Human
    • Function
    • Non-inhibitory
    • Transition
    • Cause
    • Mutations
  • proteins
    • Inhibition
    • Human
    • Non-inhibitory
    • Serpins
    • Also
    • Inhibitors
    • Protease
    • Activity
    • First
    • Inhibit
    • May
    • Plant
  • protease inhibition
    • Serpins
    • Inhibitors
    • Target
    • Serpin
    • Proteins
    • Inhibition
    • Protease
    • Change
    • Activity
    • Conformational
    • Cysteine
    • Transition
  • serine proteases
    • Proteases
    • Serine
    • Inhibit
    • Cysteine
    • Inhibitors
    • Serpins
    • Active
    • May
    • Plant
    • Therefore
    • Function
    • Also
  • protease
    • Serpins
    • Inhibitors
    • Target
    • Serpin
    • Inhibition
    • Change
    • Conformational
    • Activity
    • Cysteine
    • Transition
    • Mechanism
    • Inhibitory
  • conformational change
    • Change
    • Conformational
    • Structure
    • Protease
    • Mechanism
    • Inhibition
    • Latent
    • Rcl
    • Target
    • Mutations
    • Also
    • Serpin
  • active site
    • Serine
    • Mutations
    • Antithrombin
    • Mechanism
    • Proteases
    • Activity
    • First
    • Inhibition
    • Latent
    • Polymers
    • Protease
    • Antitrypsin

Connections between topic areas Semantic bridges

For Serpin, one of the stronger structural bridges in this analysis connects Serpin with Overview. Bridges highlight paths between different parts of the map and can reveal research angles that are easy to miss in a flat list.

Min side: 3
SerpinOverview · splits 155 ⟂ 48
SerpinBiological function and localization · splits 171 ⟂ 32
SerpinDistribution · splits 174 ⟂ 29
SerpinConformational change and inhibitory mechanism · splits 177 ⟂ 26
SerpinDisease and serpinopathies · splits 182 ⟂ 21
SerpinActivity · splits 188 ⟂ 15
SerpinHistory · splits 191 ⟂ 12
SerpinStructure · splits 196 ⟂ 7
SerpinDegradation · splits 197 ⟂ 6
SerpinEvolution · splits 197 ⟂ 6

Map overview Semantic statistics

Serpin

Nodes203
Edges202
Triples245
Avg. degree1.99
Density0.009852
Components1

Source & methodology

TTTA analyzes the structure around Serpin to surface related topics, entities, relationships, concept neighborhoods and bridge connections. Use the map to explore areas such as History, Biological function and localization & Conformational change and inhibitory mechanism, including less central topics that may reveal useful research gaps. Automatically extracted connections are research leads rather than rewritten encyclopedia content.

Source: Wikipedia — Serpin · EN edition · Analysis: TopicsToTalkAbout

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