Paper Citation Record · LEDGER

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate

As of 13 August 2026, this Paper Citation Record lists 33 of 33 outbound references and 0 inbound Pith citation observations for arXiv:2607.29639.

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pith.paper-citation-record.v1
2607.29639 v1

Coverage vector

measured 33 of 33 reference resolution

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Source: paper_references, paper_reference_links, observed 2026-08-03T03:00:11.484753Z

measured 33 of 33 standing notices

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Source: scholarly_work_events, retraction_status_cache, observed 2026-08-13T06:32:02.005865+00:00

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33 of 33 outbound references displayed

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Outbound references

Observation db56f4e4-6902-4e59-a430-92e31bac6ae9 · outbound

This paper cites 3(a)) exhibits a series of sharp peaks atr= 0.70, 0.90, 1.04, 1.36, and 1.70 nm, whose positions are strictly invariant with pressure across the full range studied.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate 3(a)) exhibits a series of sharp peaks atr= 0.70, 0.90, 1.04, 1.36, and 1.70 nm, whose positions are strictly invariant with pressure across the full range studied

Reference 1

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Observation fa8fe31d-a826-4038-9e08-b2e3d0ace02c · outbound

This paper cites 3(b)) displays peaks at r= 0.54, 0.70, 0.88, 1.02, and 1.36 nm, again with strictly invariant positions.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate 3(b)) displays peaks at r= 0.54, 0.70, 0.88, 1.02, and 1.36 nm, again with strictly invariant positions

Reference 2

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Observation 7c409b38-988f-427d-a4df-3f0ffa6f91b2 · outbound

This paper cites 3(c)) occupies a quali- tatively distinct category fromg P P(r) andg HH (r) be- cause, by construction, all P–H bead pairs are inter- chain.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate 3(c)) occupies a quali- tatively distinct category fromg P P(r) andg HH (r) be- cause, by construction, all P–H bead pairs are inter- chain

Reference 3

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Observation 38ebd8b5-cd6e-42fb-bc60-c375f12ca117 · outbound

This paper cites an unresolved cited work.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Unresolved cited work

Reference 4

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Observation e46a32b1-d5df-45b7-ab7c-35ce49359593 · outbound

This paper cites an unresolved cited work.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Unresolved cited work

Reference 5

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Observation 995a6361-1233-432e-800b-65459c326572 · outbound

This paper cites an unresolved cited work.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Unresolved cited work

Reference 6

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Observation 02569585-f95d-4df7-beaf-368c6369aead · outbound

This paper cites Why are ”natively unfolded” proteins unstructured under physiologic conditions?Proteins:Struct., Funct., Bioinf., 41(3):415–427, 2000.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Why are ”natively unfolded” proteins unstructured under physiologic conditions?Proteins:Struct., Funct., Bioinf., 41(3):415–427, 2000

Reference 7

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Observation 63d90a44-bc89-4114-ac02-c23b240a0cf2 · outbound

This paper cites Intrinsically disordered proteins and intrinsically disordered protein regions.Annu.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Intrinsically disordered proteins and intrinsically disordered protein regions.Annu

Reference 8

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Observation 8653ee3b-b2d9-48a2-87cc-e1f100a53c22 · outbound

This paper cites Rules of physical mathematics govern intrinsically disordered proteins.Annu.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Rules of physical mathematics govern intrinsically disordered proteins.Annu

Reference 9

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Observation 07e3ec60-8d23-4d1f-b65f-1584a94609fd · outbound

This paper cites https://mobidb.org/.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate https://mobidb.org/

Reference 10

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Observation 36562d3a-2f86-4fc9-8479-afce995790b2 · outbound

This paper cites Hamilton, Tanguy LeGall, Vladimir Vacic, Marc S.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Hamilton, Tanguy LeGall, Vladimir Vacic, Marc S

Reference 11

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Observation 6c8ad9a0-3acd-416b-b166-d3a66647b5a7 · outbound

This paper cites Extreme disorder in an ultrahigh-affinity protein complex.Nature, 555(7694):61– 66, 2018.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Extreme disorder in an ultrahigh-affinity protein complex.Nature, 555(7694):61– 66, 2018

Reference 12

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:08.175974Z

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Observation ea5c8141-b2d1-4a1a-bd10-84b3f829efc4 · outbound

This paper cites Driving forces of the com- plex formation between highly charged disordered pro- teins.Proceedings of the National Academy of Sciences, 120(41):e2304036120, 2023.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Driving forces of the com- plex formation between highly charged disordered pro- teins.Proceedings of the National Academy of Sciences, 120(41):e2304036120, 2023

Reference 13

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Observation 757b3282-2ee0-427e-8a65-e03f427c119f · outbound

This paper cites Behaviour of intrinsically disordered proteins in protein– protein complexes with an emphasis on fuzziness.Cellu- lar and Molecular Life Sciences, 74(17):3175–3183, 2017.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Behaviour of intrinsically disordered proteins in protein– protein complexes with an emphasis on fuzziness.Cellu- lar and Molecular Life Sciences, 74(17):3175–3183, 2017

Reference 14

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Observation c6b9b0e5-b9b0-4444-86be-7f3487317140 · outbound

This paper cites Charge interactions can dominate the dimensions of intrinsically disordered pro- teins.Proceedings of the National Academy of Sciences, 107(33):14609–14614, 2010.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Charge interactions can dominate the dimensions of intrinsically disordered pro- teins.Proceedings of the National Academy of Sciences, 107(33):14609–14614, 2010

Reference 15

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Observation eb2c6b68-b72b-4700-a430-54fc8c8b581d · outbound

This paper cites Sequence determi- nants of protein phase behavior from a coarse-grained model.PLoS Comput.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Sequence determi- nants of protein phase behavior from a coarse-grained model.PLoS Comput

Reference 16

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Observation 7205df24-a45b-4235-b024-dc7843c9040f · outbound

This paper cites Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties.Proc.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties.Proc

Reference 17

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Observation ae27bb37-9ae2-42ac-a70f-a933a76867d7 · outbound

This paper cites Theoretical studies of protein folding.An- nual review of biophysics and bioengineering, 12(1):183– 210, 1983.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Theoretical studies of protein folding.An- nual review of biophysics and bioengineering, 12(1):183– 210, 1983

Reference 18

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Observation 03812e12-af00-418e-b4f7-22d227560528 · outbound

This paper cites Muthukumar.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Muthukumar

Reference 19

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:09.455951Z

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Observation ebf486eb-08f1-41c5-ba9e-fc522d08e365 · outbound

This paper cites Muthukumar.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Muthukumar

Reference 20

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:09.584880Z

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Observation deca9190-0489-414c-a193-625a60b2f1cc · outbound

This paper cites Natively unfolded protein stability as a coil-to-globule transi- tion in charge/hydropathy space.J.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Natively unfolded protein stability as a coil-to-globule transi- tion in charge/hydropathy space.J

Reference 21

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:09.735550Z

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Observation 290f5a52-5a45-4990-bdc5-9338611f4d7c · outbound

This paper cites Academic press, 2011.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Academic press, 2011

Reference 22

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:09.854752Z

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Observation 6687ac48-d1ae-4a01-aa91-4745dab5f4c7 · outbound

This paper cites The dielectric constant of water at high temperatures and in equilibrium with its vapor.Journal of the American Chemical Society, 72(7):2844–2847, 1950.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate The dielectric constant of water at high temperatures and in equilibrium with its vapor.Journal of the American Chemical Society, 72(7):2844–2847, 1950

Reference 23

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Observation e591e99c-833f-4420-9a60-4a413b80658f · outbound

This paper cites Fine structures of intrinsically disordered pro- teins.J.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Fine structures of intrinsically disordered pro- teins.J

Reference 24

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:10.155046Z

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Observation dfc1ed96-01a8-4504-ab2e-80c78e978a8d · outbound

This paper cites Vmd: visual molecular dynamics.Journal of molecular graphics, 14(1):33–38, 1996.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Vmd: visual molecular dynamics.Journal of molecular graphics, 14(1):33–38, 1996

Reference 25

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Observation 152b8dd7-0e7c-41d1-9de1-9c58fcfab3ef · outbound

This paper cites Oxford university press, 2003.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Oxford university press, 2003

Reference 26

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Observation 1274fc27-bcf3-487b-a9ca-63f7ff7e158d · outbound

This paper cites Diffusion of intrinsically disordered proteins within protein condensates.Physical Review Research, 7(4):043117, 2025.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Diffusion of intrinsically disordered proteins within protein condensates.Physical Review Research, 7(4):043117, 2025

Reference 27

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Observation 61b24593-2c40-4b6d-876e-8fe53878fc96 · outbound

This paper cites an unresolved cited work.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Unresolved cited work

Reference 28

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Observation f88f12b1-0a89-423e-900e-1cd6ef7c7798 · outbound

This paper cites Protein condensates as aging maxwell fluids.Science, 370:1317–1323, 2020.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Protein condensates as aging maxwell fluids.Science, 370:1317–1323, 2020

Reference 29

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Observation d0c3532c-1de6-421a-a979-8dfede6fcfe5 · outbound

This paper cites Heterogeneous slowdown of dynamics in the condensate of an intrinsically disordered protein.J.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Heterogeneous slowdown of dynamics in the condensate of an intrinsically disordered protein.J

Reference 30

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:11.024910Z

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Observation 8e30dc4b-bdd5-4845-9483-0d6af8d7834b · outbound

This paper cites Burke, Abigail M.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Burke, Abigail M

Reference 31

Resolution: unresolved; no resolver link, observed 2026-08-03T03:00:11.204751Z

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Observation a96f2967-835f-41cb-a576-b8972b36e337 · outbound

This paper cites Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically dis- ordered proteins.Annu.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically dis- ordered proteins.Annu

Reference 32

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Observation ffb5beed-ccd4-42f6-a805-22ad181f4762 · outbound

This paper cites Limiting laws and counterion con- densation in polyelectrolyte solutions i.

Structure, Diffusion, and Relaxation in a Charge-Neutral ProTalpha-Histone H1 Condensate Limiting laws and counterion con- densation in polyelectrolyte solutions i

Reference 33

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