Reference health

A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors

https://doi.org/10.1016/0022-2836(74)90343-x
CiteStamped reference-health badge
30/30 checkable references clean · checked 2026-08-09

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

7 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 30 checked references that resolve
resolves10.1016/S0021-9258(18)85018-9
THE HEMOGLOBIN SYSTEM
resolves10.1038/237146a0
X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
resolves10.1016/0034-5687(70)90022-8
Reduction of the carbon dioxide affinity of human haemoglobin solutions by 2,3 diphosphoglycerate
resolves10.1021/bi00834a046
Oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration
resolves10.1016/S0021-9258(19)67978-0
The Relation between the Oxygen Equilibrium and Aggregation of Subunits in Lamprey Hemoglobin
resolves10.1172/JCI106324
The interaction of 2,3-diphosphoglycerate with various human hemoglobins
resolves10.1016/S0006-291X(71)80256-5
The effect of oxygen, carbon dioxide, pH and cyanate on the binding of 2,3-diphosphoglycerate to human hemoglobin
resolves10.1016/S0021-9258(19)63805-6
Functional Aspects of the Subunit Association-Dissociation Equilibria of Hemoglobin
resolves10.1016/S0021-9258(17)48178-6
Kinetic Evidence for a Tetrameric Functional Unit in Hemoglobin
resolves10.1016/S0006-291X(72)80051-2
A general model of cooperativity and its application to DPG inhibition of hemoglobin oxygenation
resolves10.1016/0006-291X(72)90428-7
31P-NMR studies of the release of diphospholygeric acid on carbon monoxide binding to hemoglobin
resolves10.1016/0006-291X(72)90616-X
19F-nmr studies of oxygen binding to hemoglobin
resolves10.1016/0006-291X(72)90506-2
The rate of carbon monoxide binding to hemoglobin Kansas
resolves10.1016/0022-2836(71)90307-X
Dissociation of hemoglobin into subunits
resolves10.1038/227921a0
Reactions of Haemoglobin Dimers after Ligand Dissociation
resolves10.1021/bi00865a047
Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits<sup>*</sup>
resolves10.1016/S0022-2836(65)80285-6
On the nature of allosteric transitions: A plausible model
resolves10.1021/bi00775a024
States of hemoglobin in solution
resolves10.1038/228726a0
Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
resolves10.1016/S0021-9258(19)44683-8
The Deoxygenation Kinetics of Hemoglobin Partially Saturated with Carbon Monoxide
resolves10.1016/0022-2836(72)90077-0
A mathematical model for structure-function relations in hemoglobin
resolves10.1016/0020-711X(71)90002-4
Oxygen equilibrium studies of the radular muscle myoglobins of the gastropod molluscs, buccinum undatum L. and Bustcon canaliculatum L.
resolves10.1016/S0021-9258(20)81781-5
Observation of the Dissociation of Unliganded Hemoglobin
resolves10.1002/bip.1968.360060806
Models for hemoglobin and allosteric enzymes
resolves10.1016/S0021-9258(18)62449-4
Studies of the Interaction of 2,3-Diphosphoglycerate and Carbon Dioxide with Hemoglobins from Mouse, Man, and Elephant
resolves10.1016/0006-291X(71)90770-4
Effect of 2,3-diphosphoglycerate on the cooperativity in oxygen binding of human adult hemoglobin
resolves10.1016/0079-6107(70)90028-3
The regulation of enzyme activity and allosteric transition
resolves10.1016/S0022-2836(65)80017-1
The binding potential, a neglected linkage concept
resolves10.1021/ja00985a037
Allosteric Linkage
resolves10.1017/S0033583500000457
Regulation in macromolecules as illustrated by haemoglobin
The 7 references without a DOI — listed, not checked
no DOI — not checked10.1016/0022-2836(74)90343-X_bib1
no DOI — not checked10.1016/0022-2836(74)90343-X_bib9
no DOI — not checked10.1016/0022-2836(74)90343-X_bib13
no DOI — not checked10.1016/0022-2836(74)90343-X_bib21
no DOI — not checked10.1016/0022-2836(74)90343-X_bib23
no DOI — not checked10.1016/0022-2836(74)90343-X_bib26
no DOI — not checked10.1016/0022-2836(74)90343-X_bib28
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-08-09 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

view as graph · paper page

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1016/0022-2836(74)90343-x"><img src="https://citestamp.com/citestamped/10.1016/0022-2836(74)90343-x/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1016/0022-2836(74)90343-x/badge.svg)](https://citestamp.com/citestamped/10.1016/0022-2836(74)90343-x)