On the public citation graph

Face traverses and a volume algorithm for polyhedra

https://doi.org/10.1007/bfb0038197
0 signed · 18 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1080/00029890.1986.11971863openalex-snapshot
A Mnemonic for Areas of Polygons
inferredcites →https://doi.org/10.1112/jlms/s1-21.2.98openalex-snapshot
On Hamiltonian Circuits

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1007/978-3-031-05914-8_2openalex-snapshot
Explaining Small Molecule Binding Specificity with Volumetric Representations of Protein Binding Sites
inferred← citeshttps://doi.org/10.1007/bfb0038178openalex-snapshot
New Results and New Trends in Computer Science
inferred← citeshttps://doi.org/10.1089/cmb.2015.0117openalex-snapshot
Conformational Sampling Reveals Amino Acids with a Steric Influence on Specificity
inferred← citeshttps://doi.org/10.1109/bibm.2011.33openalex-snapshot
VASP-S: A Volumetric Analysis and Statistical Model for Predicting Steric Influences on Protein-Ligand Binding Specificity
inferred← citeshttps://doi.org/10.1109/bibm.2015.7359658openalex-snapshot
Superposition of protein structures using electrostatic isopotentials
inferred← citeshttps://doi.org/10.1109/bibm.2015.7359859openalex-snapshot
A statistical model of electrostatic isopotential variation in serine protease binding cavities
inferred← citeshttps://doi.org/10.1109/bibmw.2011.6112409openalex-snapshot
A statistical model of overlapping volume in ligand binding cavities
inferred← citeshttps://doi.org/10.1142/s0219720012420048openalex-snapshot
A REGIONALIZABLE STATISTICAL MODEL OF INTERSECTING REGIONS IN PROTEIN–LIGAND BINDING CAVITIES
inferred← citeshttps://doi.org/10.1145/2649387.2649428openalex-snapshot
A flexible volumetric comparison of protein cavities can reveal patterns in ligand binding specificity
inferred← citeshttps://doi.org/10.1145/2649387.2660837openalex-snapshot
Variational Bayesian clustering on protein cavity conformations for detecting influential amino acids
inferred← citeshttps://doi.org/10.1145/3233547.3233710openalex-snapshot
MAPS
inferred← citeshttps://doi.org/10.1186/1472-6807-13-s1-s10openalex-snapshot
An aggregate analysis of many predicted structures to reduce errors in protein structure comparison caused by conformational flexibility
inferred← citeshttps://doi.org/10.1186/1477-5956-10-s1-s6openalex-snapshot
Modeling regionalized volumetric differences in protein-ligand binding cavities
inferred← citeshttps://doi.org/10.1186/s13015-020-00168-zopenalex-snapshot
Precise parallel volumetric comparison of molecular surfaces and electrostatic isopotentials
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1000881openalex-snapshot
VASP: A Volumetric Analysis of Surface Properties Yields Insights into Protein-Ligand Binding Specificity
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1003792openalex-snapshot
VASP-E: Specificity Annotation with a Volumetric Analysis of Electrostatic Isopotentials
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.