Same transporter, new scale: a 2026 whole-enterocyte model operationalizes the SGLT1 kinetics the 2011 structure paper pinned down — with zero shared authors

Asked (summary):

How do the concepts and authors of DOI 10.64898/2026.01.28.702213 (“The biophysical basis of enterocyte homeostasis”, 2026 preprint) link to those of DOI 10.1152/ajpcell.00397.2011 (“Bridging the gap between structure and kinetics of human SGLT1”, 2011/2012)?

Five evidence rows from five independent hosts — one row per host — cover the two papers’ concepts, metadata and authors plus two intellectual-lineage links. Both works center on human SGLT1 as an electrogenic 2 Na⁺:1 glucose cotransporter; the connection is strong conceptually but indirect bibliographically, and no direct citation from the 2026 preprint to the 2011 article was verified in the fetched preprint text.

Concept flow: structure and kinetics → bond-graph modelling → whole-cell homeostasis

2011 structure & kinetics (Wright/Loo lab)intervening SGLT1 literature & bond-graph modelling2026 thermodynamic enterocyte model (Auckland)

Hover a node or ribbon to isolate one pathway. Ribbons are conceptual carriers, not verified citations; widths are illustrative of the strength described in the evidence rows.

The two papers, side by side

2011 · Am J Physiol-Cell Physiol 302(9): C1293–305

Bridging the gap between structure and kinetics of human SGLT1

Molecular and experimental: homology models, mutagenesis, Xenopus-oocyte assays, ligand affinity (K_0.5), external gates, glucose and phlorizin binding, and how Na⁺ opens the external vestibule. Mutating sugar-binding residues raises glucose K_0.5 by up to three orders of magnitude; mutating external-gate residues raises the Na⁺:sugar stoichiometry.

Monica Sala-Rabanal, Bruce A. Hirayama, Donald D. F. Loo, Vincent Chaptal, Jeff Abramson, Ernest M. Wright · journals.physiology.org · wikidata.org

2026 · bioRxiv preprint

The biophysical basis of enterocyte homeostasis

Transporter-to-whole-cell scale: SGLT1 embedded in a thermodynamically constrained bond-graph enterocyte model with NKA, GLUT2, Kir, glycolysis, ATP, ions, water and membrane potential. SGLT1 is modelled under Briggs–Haldane steady-state cycling with no slippage, 2:1 Na⁺:glucose stoichiometry and an explicit reversal potential — kinetics turned into conservation-law-constrained homeostasis.

Peter Hunter, Jarrah Dowrick, Weiwei Ai, David Nickerson, Mohammad Hossein Shafieizadegan, Finbar Argus (Auckland Bioengineering Institute) · biorxiv.org

Authors: zero overlap, one lineage

No author appears on both papers. The connection runs through literature: bond-graph modelling of SGLT1 (Gawthrop 2020) cites and validates against the Wright/Loo lab’s experimental SGLT1 work; Hunter, Nickerson and Ai then developed the enterocyte and energy-based SLC modelling line culminating in the 2026 preprint.

Findings

Mutating sugar-binding residues raises glucose K_0.5 by up to three orders of magnitude, and mutating external-gate residues increases the Na⁺:sugar stoichiometry — the 2011 paper’s core structure-to-kinetics result. journals.physiology.org

The 2026 preprint’s SGLT1 equations point to their own bond-graph source and to parameters fitted to Lowe and Walmsley — not to the 2011 article — so the relationship is conceptual lineage, not a verified direct citation. biorxiv.org

Gawthrop’s bond-graph paper builds and validates an SGLT1 model against, and cites, the Wright/Loo lab’s experimental SGLT1 work — the bibliographic bridge between the two author teams. ar5iv.labs.arxiv.org

Peter Hunter’s record ties the 2026 preprint to earlier Physiome enterocyte models of glucose uptake by SGLT1 and GLUT2 and to energy-based bond-graph SLC transporter models, with David Nickerson and colleagues. orcid.org

Evidence rows

Item	Authors	Linkage	Source

Method: 5 evidence rows from 5 independent hosts (one row per host) gathered with Keenable AI, covering two papers’ concepts, metadata and authors plus two intellectual-lineage links; K_0.5 is a half-saturation concentration and 2:1 is the Na⁺:glucose cotransport stoichiometry. Linkage text is truncated in the table for space; ribbon widths in the diagram are illustrative, not citation counts.

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