Reference health

Modifying Caspase-3 Activity by Altering Allosteric Networks

39/39 checkable references clean · checked 2026-07-22

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.

The 39 checked references that resolve

resolves10.1016/j.ceb.2003.10.009

Mechanisms of caspase activation

resolves10.1007/978-1-4614-3229-6_4

Death by Caspase Dimerization

resolves10.1074/jbc.273.5.2926

An Induced Proximity Model for Caspase-8 Activation

resolves10.1021/bi0110387

Dimeric Procaspase-3 Unfolds via a Four-State Equilibrium Process

resolves10.1074/jbc.M109.095083

Inducible Dimerization and Inducible Cleavage Reveal a Requirement for Both Processes in Caspase-8 Activation

resolves10.1073/pnas.0404781101

Discovery of an allosteric site in the caspases

resolves10.1016/j.devcel.2008.12.012

The Jekyll and Hyde Functions of Caspases

resolves10.1182/blood-2002-06-1778

Specific involvement of caspases in the differentiation of monocytes into macrophages

resolves10.1038/nn.2709

Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease

resolves10.1016/j.tins.2011.09.001

Caspase-6 and neurodegeneration

resolves10.1038/cdd.2011.30

Caspases and cancer

resolves10.1101/cshperspect.a008656

Caspase Functions in Cell Death and Disease

resolves10.1016/j.jmb.2008.06.040

An Allosteric Circuit in Caspase-1

resolves10.1021/bi400115n

Slow Folding and Assembly of a Procaspase-3 Interface Variant

resolves10.1021/bi034999p

Mutations in the Procaspase-3 Dimer Interface Affect the Activity of the Zymogen

resolves10.1042/BSR20120037

Allosteric modulation of caspase 3 through mutagenesis

resolves10.1021/bi0611964

Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of (Pro)caspase-3

resolves10.1021/bi400793s

Lengthening the Intersubunit Linker of Procaspase 3 Leads to Constitutive Activation

resolves10.1042/BJ20090825

A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis

resolves10.1021/bi011037e

Removal of the Pro-Domain Does Not Affect the Conformation of the Procaspase-3 Dimer

resolves10.1016/j.abb.2011.01.011

Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3

resolves10.1021/bi034998x

An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3

resolves10.1093/nar/gkh398

MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes

resolves10.1042/BJ20040693

Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3

resolves10.1021/ct700301q

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

resolves10.1002/1096-987X(200009)21:12<1049::AID-JCC3>3.0.CO;2-F

How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?

resolves10.1063/1.445869

Comparison of simple potential functions for simulating liquid water

resolves10.1007/s10495-008-0259-9

Structural basis for executioner caspase recognition of P5 position in substrates

resolves10.1038/370270a0

Structure and mechanism of interleukin-lβ converting enzyme

resolves10.1016/j.str.2008.12.019

Structural and Biochemical Studies on Procaspase-8: New Insights on Initiator Caspase Activation

resolves10.1016/j.febslet.2012.08.032

Structural insights into the calcium‐dependent interaction between calbindin‐D28K and caspase‐3

resolves10.1073/pnas.1306759110

Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation

resolves10.1074/jbc.M112.397752

Zinc-mediated Allosteric Inhibition of Caspase-6

resolves10.1084/jem.20031771

p38-MAPK Signals Survival by Phosphorylation of Caspase-8 and Caspase-3 in Human Neutrophils

resolves10.1101/cshperspect.a008672

Cellular Mechanisms Controlling Caspase Activation and Function

resolves10.1074/jbc.M112.351213

Inhibitory Mechanism of Caspase-6 Phosphorylation Revealed by Crystal Structures, Molecular Dynamics Simulations, and Biochemical Assays

resolves10.1016/j.str.2012.02.003

Phosphorylation Regulates Assembly of the Caspase-6 Substrate-Binding Groove

resolves10.1038/sj.cdd.4402034

Caspase inhibitors: viral, cellular and chemical

resolves10.1021/jm0601405

Design, Synthesis, and Evaluation of Aza-Peptide Michael Acceptors as Selective and Potent Inhibitors of Caspases-2, -3, -6, -7, -8, -9, and -10

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 2026-07-22 — 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/10.1021/bi500874k"><img src="https://citestamp.com/citestamped/10.1021/bi500874k/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>

[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1021/bi500874k/badge.svg)](https://citestamp.com/citestamped/10.1021/bi500874k)