Paper Citation Record · LEDGER

Inferring protein folding mechanisms from natural sequence diversity

As of 24 August 2026, this Paper Citation Record lists 43 of 43 outbound references and 1 inbound Pith citation observation for arXiv:2412.14341.

A citation records a reference. It does not transfer a finding from one paper to another.

pith.paper-citation-record.v1
2412.14341 v3

Coverage vector

measured 43 of 43 reference resolution

Typed states for the displayed outbound observations.

Source: paper_references, paper_reference_links, observed 2026-08-11T12:25:39.128427Z

measured 44 of 44 standing notices

One-hop event checks from named stored sources.

Source: scholarly_work_events, retraction_status_cache, observed 2026-08-23T06:30:58.430688+00:00

measured 1 of 1 inbound itemization

Pith citing papers itemized under the disclosed page cap.

Source: paper_references, paper_reference_links, observed 2026-08-07T14:54:02.021611Z

measured 1 of 1 external citation measurements

A source-named dated measurement, never combined with another source.

Source: pith, observed 2026-08-10T05:30:23.456663Z

Reference resolution

43 of 43 outbound references displayed

verified exact33
verified fuzzy1
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External citation measurements

0
pith, observed 2026-08-10T05:30:23.456663Z

Outbound references

Observation d8bb77b8-5934-47aa-8fc4-818e1d850c18 · outbound

This paper cites Chemical physics of protein folding,.

Inferring protein folding mechanisms from natural sequence diversity Chemical physics of protein folding,

Reference 1

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.583128Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation c268d386-c679-4fa2-9e56-127394548f0a · outbound

This paper cites Protein folding funnels: a kinetic approach to the sequence-structure relationship.,.

Inferring protein folding mechanisms from natural sequence diversity Protein folding funnels: a kinetic approach to the sequence-structure relationship.,

Reference 2

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:38.974904Z

Source-reported events for the cited work

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Observation 1e16bf9f-0355-44f2-98f7-65005bceee14 · outbound

This paper cites Spin glasses and the statistical mechanics of protein folding,.

Inferring protein folding mechanisms from natural sequence diversity Spin glasses and the statistical mechanics of protein folding,

Reference 3

Resolution: verified fuzzy; raw_fallback, observed 2026-08-11T12:25:39.659614Z

Source-reported events for the cited work

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Observation 8c9dfc88-cb45-48fc-8e56-45520b2199c9 · outbound

This paper cites Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space,.

Inferring protein folding mechanisms from natural sequence diversity Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space,

Reference 4

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.563812Z

Source-reported events for the cited work

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Observation 46aa9e74-612d-401d-a236-327aab550940 · outbound

This paper cites Statistical mechanics of simple models of protein folding and design,.

Inferring protein folding mechanisms from natural sequence diversity Statistical mechanics of simple models of protein folding and design,

Reference 5

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.552877Z

Source-reported events for the cited work

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Observation 580a8339-4b09-4503-9d9d-6a040ffbe96e · outbound

This paper cites Frustration in biomolecules,.

Inferring protein folding mechanisms from natural sequence diversity Frustration in biomolecules,

Reference 6

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.541699Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation bbd15a3b-8af8-41ea-958d-c5157c7c8b91 · outbound

This paper cites Molecular Information Theory Meets Protein Folding,.

Inferring protein folding mechanisms from natural sequence diversity Molecular Information Theory Meets Protein Folding,

Reference 7

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.530129Z

Source-reported events for the cited work

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Observation a78eaf68-7ead-4001-8a68-6168d040dd9c · outbound

This paper cites Machine learning in protein structure prediction,.

Inferring protein folding mechanisms from natural sequence diversity Machine learning in protein structure prediction,

Reference 9

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.506544Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 54c12ce3-cb23-4b92-85a3-b93722286968 · outbound

This paper cites Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright,.

Inferring protein folding mechanisms from natural sequence diversity Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright,

Reference 10

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.008407Z

Source-reported events for the cited work

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Observation 8f20b366-1ab3-4ac4-ae6e-f6e3b5eab480 · outbound

This paper cites Coarse-grained models of protein folding: toy models or predictive tools?,.

Inferring protein folding mechanisms from natural sequence diversity Coarse-grained models of protein folding: toy models or predictive tools?,

Reference 11

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.495997Z

Source-reported events for the cited work

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Observation f59314fa-e3b0-496b-933f-31747e0844b8 · outbound

This paper cites Frustration, function and folding,.

Inferring protein folding mechanisms from natural sequence diversity Frustration, function and folding,

Reference 12

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.485029Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation f01d0532-fcd0-47c6-bf0f-f241415f671b · outbound

This paper cites Conserved residues and the mechanism of protein folding,.

Inferring protein folding mechanisms from natural sequence diversity Conserved residues and the mechanism of protein folding,

Reference 13

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.474064Z

Source-reported events for the cited work

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Observation 4fb17ec3-912c-4f13-832b-00daff039f7d · outbound

This paper cites Identification of direct residue contacts in protein-protein interaction by message passing,.

Inferring protein folding mechanisms from natural sequence diversity Identification of direct residue contacts in protein-protein interaction by message passing,

Reference 14

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.463839Z

Source-reported events for the cited work

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Observation fdbe44c8-cce5-4eae-8b61-b2f28c72b532 · outbound

This paper cites Direct-coupling analysis of residue coevolution captures native contacts across many protein families,.

Inferring protein folding mechanisms from natural sequence diversity Direct-coupling analysis of residue coevolution captures native contacts across many protein families,

Reference 15

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.026031Z

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Observation 6696e94a-93d4-4b3a-a109-828660bc8497 · outbound

This paper cites Inverse statistical physics of protein sequences: A key issues review,.

Inferring protein folding mechanisms from natural sequence diversity Inverse statistical physics of protein sequences: A key issues review,

Reference 16

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.447063Z

Source-reported events for the cited work

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Observation d360ff8a-a176-426b-8f01-5e31c904ecfb · outbound

This paper cites Direct Coupling Analysis for Protein Contact Prediction,.

Inferring protein folding mechanisms from natural sequence diversity Direct Coupling Analysis for Protein Contact Prediction,

Reference 17

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.436320Z

Source-reported events for the cited work

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Observation 046bef68-c704-43ea-be19-a3b8af0fcb21 · outbound

This paper cites Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1,.

Inferring protein folding mechanisms from natural sequence diversity Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1,

Reference 18

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.035298Z

Source-reported events for the cited work

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Observation f37af4cd-c8c0-402c-a180-fd86f8dd66f5 · outbound

This paper cites Inferring repeat-protein energetics from evolutionary information,.

Inferring protein folding mechanisms from natural sequence diversity Inferring repeat-protein energetics from evolutionary information,

Reference 19

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.418316Z

Source-reported events for the cited work

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Observation 833d1844-61b2-498e-92e0-1dc874c3f615 · outbound

This paper cites Size and structure of the sequence space of repeat proteins,.

Inferring protein folding mechanisms from natural sequence diversity Size and structure of the sequence space of repeat proteins,

Reference 20

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.407475Z

Source-reported events for the cited work

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Observation 26a6043f-96b5-4829-9372-de60b67de7dc · outbound

This paper cites Epistatic contributions promote the unification of incompatible models of neutral molecular evolution,.

Inferring protein folding mechanisms from natural sequence diversity Epistatic contributions promote the unification of incompatible models of neutral molecular evolution,

Reference 21

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.396309Z

Source-reported events for the cited work

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Observation f3f27078-38a6-441c-9da1-adde71289538 · outbound

This paper cites Emergent time scales of epistasis in protein evolution,.

Inferring protein folding mechanisms from natural sequence diversity Emergent time scales of epistasis in protein evolution,

Reference 22

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.048697Z

Source-reported events for the cited work

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Observation 386f045a-c0e9-4d53-a722-5327d8ec2984 · outbound

This paper cites Kinetic coevolutionary models predict the temporal emergence of HIV-1 resistance mutations under drug selection pressure,.

Inferring protein folding mechanisms from natural sequence diversity Kinetic coevolutionary models predict the temporal emergence of HIV-1 resistance mutations under drug selection pressure,

Reference 23

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.379518Z

Source-reported events for the cited work

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Observation 57475a1f-4fd0-495c-a766-9c04240d43d1 · outbound

This paper cites Foldons, protein structural modules, and exons.,.

Inferring protein folding mechanisms from natural sequence diversity Foldons, protein structural modules, and exons.,

Reference 24

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.055958Z

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Observation f9f5a4db-0eac-406c-91dd-fc34b9957c17 · outbound

This paper cites Reassessing the exon–foldon correspondence using frustration analysis,.

Inferring protein folding mechanisms from natural sequence diversity Reassessing the exon–foldon correspondence using frustration analysis,

Reference 25

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.362249Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 69268aff-563f-4080-911c-ae9049b5acc5 · outbound

This paper cites Evolution and folding of repeat proteins,.

Inferring protein folding mechanisms from natural sequence diversity Evolution and folding of repeat proteins,

Reference 26

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.350465Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 2685523f-a2f3-4621-bd90-026d69b61fb5 · outbound

This paper cites The energy landscapes of repeat-containing proteins: Topology, cooperativity, and the folding funnels of one-dimensional architectures,.

Inferring protein folding mechanisms from natural sequence diversity The energy landscapes of repeat-containing proteins: Topology, cooperativity, and the folding funnels of one-dimensional architectures,

Reference 27

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.338792Z

Source-reported events for the cited work

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Observation edaf0a07-57af-4aba-a7a5-9145471d555d · outbound

This paper cites Learning protein constitutive motifs from sequence data,.

Inferring protein folding mechanisms from natural sequence diversity Learning protein constitutive motifs from sequence data,

Reference 28

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.327765Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 75baeb2f-c7a4-4ae2-8bf3-339ccebdab2e · outbound

This paper cites Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection,.

Inferring protein folding mechanisms from natural sequence diversity Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection,

Reference 29

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.518202Z

Source-reported events for the cited work

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Observation 2987cf4e-5a7a-443a-9ae0-d543029bd762 · outbound

This paper cites Selection originating from protein stability/foldability: Relationships between protein folding free energy, sequence ensemble, and fitness,.

Inferring protein folding mechanisms from natural sequence diversity Selection originating from protein stability/foldability: Relationships between protein folding free energy, sequence ensemble, and fitness,

Reference 30

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.317500Z

Source-reported events for the cited work

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Observation dd2b62eb-5ad8-4288-bfa5-a13d944c4771 · outbound

This paper cites Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.,.

Inferring protein folding mechanisms from natural sequence diversity Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.,

Reference 31

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.307352Z

Source-reported events for the cited work

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Observation cedfc19c-4879-4b5e-8d7e-001747ecc6ae · outbound

This paper cites Folding of dihydrofolate reductase from Escherichia coli,.

Inferring protein folding mechanisms from natural sequence diversity Folding of dihydrofolate reductase from Escherichia coli,

Reference 32

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.297500Z

Source-reported events for the cited work

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Observation b40ee040-4f30-4bb3-97dc-a213cf458e78 · outbound

This paper cites Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway,.

Inferring protein folding mechanisms from natural sequence diversity Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway,

Reference 33

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.286277Z

Source-reported events for the cited work

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Observation 02deb424-7b31-4fff-b5ca-a56fdd093c41 · outbound

This paper cites Microsecond Subdomain Folding in Dihydrofolate Reductase,.

Inferring protein folding mechanisms from natural sequence diversity Microsecond Subdomain Folding in Dihydrofolate Reductase,

Reference 34

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.274568Z

Source-reported events for the cited work

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Observation 80607c89-7dd4-4c72-8cb8-cf6365f62634 · outbound

This paper cites Structure of a partially unfolded form of E scherichia coli dihydrofolate reductase provides insight into its folding pathway,.

Inferring protein folding mechanisms from natural sequence diversity Structure of a partially unfolded form of E scherichia coli dihydrofolate reductase provides insight into its folding pathway,

Reference 35

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.263653Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 8c117f1e-722f-4961-94fe-bdff66edca17 · outbound

This paper cites Co-Evolutionary Fitness Landscapes for Sequence Design,.

Inferring protein folding mechanisms from natural sequence diversity Co-Evolutionary Fitness Landscapes for Sequence Design,

Reference 36

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.252346Z

Source-reported events for the cited work

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Observation bfb20caf-1b10-4ed5-adf1-9c02463d76fe · outbound

This paper cites Solvent constraints for biopolymer folding and evolution in extraterrestrial environments,.

Inferring protein folding mechanisms from natural sequence diversity Solvent constraints for biopolymer folding and evolution in extraterrestrial environments,

Reference 37

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.240428Z

Source-reported events for the cited work

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Observation 849e6503-3fa7-459b-ab44-b075435623a2 · outbound

This paper cites Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kinetics,.

Inferring protein folding mechanisms from natural sequence diversity Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kinetics,

Reference 38

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.229251Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation bb940dfd-d738-4ee2-8c41-01c16dfe0586 · outbound

This paper cites Start2Fold: A database of hydrogen/deuterium exchange data on protein folding and stability,.

Inferring protein folding mechanisms from natural sequence diversity Start2Fold: A database of hydrogen/deuterium exchange data on protein folding and stability,

Reference 39

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.218231Z

Source-reported events for the cited work

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Observation cf8cc249-11f0-4d43-8ce6-e835087d52e1 · outbound

This paper cites Local energetic frustration conservation in protein families and superfamilies,.

Inferring protein folding mechanisms from natural sequence diversity Local energetic frustration conservation in protein families and superfamilies,

Reference 40

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.206677Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.

Observation 86cf9e30-bad3-42fe-be71-00c8fc03323c · outbound

This paper cites The Pfam protein families database: towards a more sustainable future,.

Inferring protein folding mechanisms from natural sequence diversity The Pfam protein families database: towards a more sustainable future,

Reference 41

Resolution: verified exact; doi, observed 2026-08-11T12:25:39.194797Z

Source-reported events for the cited work

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Observation 3204c102-b082-4b53-bbea-b3a6bb22eb9c · outbound

This paper cites InterPro in 2022,.

Inferring protein folding mechanisms from natural sequence diversity InterPro in 2022,

Reference 42

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.120759Z

Source-reported events for the cited work

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Observation e00c4a87-2280-45f6-ba77-f03c4968d9d4 · outbound

This paper cites Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences,.

Inferring protein folding mechanisms from natural sequence diversity Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences,

Reference 43

Resolution: unresolved; no resolver link, observed 2026-08-11T12:25:39.124579Z

Source-reported events for the cited work

Unavailable: canonical work link unavailable.

Observation f8fcc2b1-bd83-40b8-abf0-c0320299e96b · outbound

This paper cites Frustration, dynamics and catalysis.

Inferring protein folding mechanisms from natural sequence diversity Frustration, dynamics and catalysis

Reference 44

Resolution: metadata mismatch; local_arxiv, observed 2026-08-11T12:25:39.167739Z

Source-reported events for the cited work

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Pith citing papers

Observation d84dadb0-1277-41df-9b18-4601c1f7e83c · inbound

Predicting protein folding dynamics using sequence information cites this paper.

Predicting protein folding dynamics using sequence information Inferring protein folding mechanisms from natural sequence diversity

Reference 18

Resolution: verified exact; local_arxiv, observed 2026-08-07T14:54:02.409660Z

Source-reported events for the cited work

No event found in the named queried sources as of 2026-08-23T06:30:58.430688+00:00.