MediaWiki API result
This is the HTML representation of the JSON format. HTML is good for debugging, but is unsuitable for application use.
Specify the format parameter to change the output format. To see the non-HTML representation of the JSON format, set format=json.
See the complete documentation, or the API help for more information.
{
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{
"logid": 3618,
"ns": 0,
"title": "2022Vilas Emerging",
"pageid": 3117,
"logpage": 3117,
"revid": 5173,
"params": {},
"type": "create",
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"user": "WikiSysop",
"timestamp": "2026-03-24T10:44:34Z",
"comment": "Created page with \"== Citation == Vilas, J.L., Carazo, J.M. and Sorzano, C.O.S. 2022. Emerging themes in CryoEM\u2500 Single particle analysis image processing. Chemical Reviews. 122, 17 (2022), 13915\u201313951. == Abstract == Cryo-electron microscopy (CryoEM) has become a vital technique in structural biology. It is an interdisciplinary field that takes advantage of advances in biochemistry, physics, and image processing, among other disciplines. Innovations in these three basic pillars hav...\""
},
{
"logid": 3617,
"ns": 0,
"title": "2026Xu MarkerFree",
"pageid": 3116,
"logpage": 3116,
"revid": 5171,
"params": {},
"type": "create",
"action": "create",
"user": "Vilas",
"timestamp": "2026-03-04T10:39:59Z",
"comment": "Created page with \"== Citation == Z. Xu, Z. Liu, T. Niu, B. He, F. Zhang, X. Li, R. Han, Markerfree: GPU-accelerated marker-free alignment for improved cryo-ET reconstruction, Structure, 0969-2126, (2026) == Abstract == Tilt series alignment is pivotal for cryo-electron tomography (cryo-ET). However, the increasing diversity of cryo-ET datasets, combined with challenges such as low signal-to-noise ratios and complex cellular structures, has significantly raised the demands for tilt se...\""
},
{
"logid": 3616,
"ns": 0,
"title": "2026Liu nextPYP",
"pageid": 3115,
"logpage": 3115,
"revid": 5169,
"params": {},
"type": "create",
"action": "create",
"user": "Vilas",
"timestamp": "2026-02-20T13:17:08Z",
"comment": "Created page with \"== Citation == HF. Liu, Y. Zhou, Q. Huang, et al. In situ structure determination of conformationally flexible targets using nextPYP. Nat Protoc 21, 851\u2013871 (2026). == Abstract == Single-particle cryoelectron tomography (SP-CET) is an imaging technique capable of determining the structure of proteins in their cellular environment at high-resolution. nextPYP is a web-based application designed to streamline the SP-CET structure determination process and facilitate t...\""
},
{
"logid": 3615,
"ns": 0,
"title": "2026Schreiber Turonova TANGO",
"pageid": 3114,
"logpage": 3114,
"revid": 5167,
"params": {},
"type": "create",
"action": "create",
"user": "Vilas",
"timestamp": "2026-02-20T12:58:36Z",
"comment": "Created page with \"== Citation == M. Schreiber, B. Turo\u0148ov\u00e1, TANGO: Analysis and curation of particles in cryo-electron tomography. Nat Commun 17, 1557 (2026). == Abstract == Cryo-electron tomography (cryo-ET) enables the visualization of cellular structures in near-native environments, but its potential for spatial analysis has been underutilized due to a lack of versatile tools accommodating biological sample diversity. Available solutions often rely on case-specific or hypothesis...\""
},
{
"logid": 3614,
"ns": 0,
"title": "2026JCarrion JDavis insituHet3D",
"pageid": 3113,
"logpage": 3113,
"revid": 5165,
"params": {},
"type": "create",
"action": "create",
"user": "Vilas",
"timestamp": "2026-02-20T12:43:32Z",
"comment": "Created page with \"== Citation == J. Carrion, and J. Davis, \"Resolving structural heterogeneity in situ through cryogenic electron tomography\", Current Opinion in Structural Biology, Volume 96, 103188, 2026 == Abstract == Cryogenic electron tomography (cryoET) has emerged as a powerful tool for studying the structural heterogeneity of proteins and their complexes, offering insights into macromolecular dynamics directly within cells. Driven by recent computational advances, including pow...\""
},
{
"logid": 3613,
"ns": 0,
"title": "2025Balanov Confirmation",
"pageid": 3112,
"logpage": 3112,
"revid": 5163,
"params": {},
"type": "create",
"action": "create",
"user": "WikiSysop",
"timestamp": "2026-02-20T06:35:06Z",
"comment": "Created page with \"== Citation == Balanov, A., Bendory, T. and Huleihel, W. 2025. Confirmation bias in Gaussian mixture models. IEEE Trans. on Information Theory. (2025). == Abstract == Confirmation bias, the tendency to interpret information in a way that aligns with one\u2019s preconceptions, can profoundly impact scientific research, leading to conclusions that reflect the researcher\u2019s hypotheses even when the observational data do not support them. This issue is especially critical i...\""
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{
"logid": 3612,
"ns": 0,
"title": "2026Li Atomic",
"pageid": 3111,
"logpage": 3111,
"revid": 5161,
"params": {},
"type": "create",
"action": "create",
"user": "WikiSysop",
"timestamp": "2026-02-18T07:26:09Z",
"comment": "Created page with \"== Citation == Li, T. and Huang, S.-Y. 2026. Deep learning\u2013based postprocessing and model building for cryo-electron microscopy maps. Current Opinion in Structural Biology. 96, (2026), 103196. == Abstract == Cryo-electron microscopy (cryo-EM) has emerged as one of the most powerful techniques for determining the structures of biological macromolecules. The ultimate goal of cryo-EM is to determine the atomic structure of target molecules, where map postprocessing and...\""
},
{
"logid": 3611,
"ns": 0,
"title": "2026Chen CryoEvoBuild",
"pageid": 3110,
"logpage": 3110,
"revid": 5159,
"params": {},
"type": "create",
"action": "create",
"user": "WikiSysop",
"timestamp": "2026-02-17T04:51:20Z",
"comment": "Created page with \"== Citation == Chen, J., Li, T., He, J. and Huang, S.-Y. 2026. Protein model building for intermediate-resolution cryo-EM maps by integrating evolutionary and experimental information. Structure. 34, (2026), 375\u2013384. == Abstract == Accurate model building in intermediate-resolution cryo-EM maps normally requires flexible fitting of reliable initial structures. However, while deep learning-based methods such as AlphaFold2 can predict highly accurate structures, the p...\""
},
{
"logid": 3610,
"ns": 0,
"title": "2026Urzhumtsev ProjDir",
"pageid": 3109,
"logpage": 3109,
"revid": 5157,
"params": {},
"type": "create",
"action": "create",
"user": "WikiSysop",
"timestamp": "2026-02-17T04:38:34Z",
"comment": "Created page with \"== Citation == Urzhumtsev, A.G. 2026. Quantifying distributions of cryo-EM projections. Biological Crystallography. 82, 2 (2026). == Abstract == In cryo-electron microscopy, a set of two-dimensional projections collected from different viewing directions may complicate image processing and subsequent model building if the distribution of these views is non-uniform. View distributions are traditionally represented as color-coded two-dimensional diagrams. However, such...\""
},
{
"logid": 3609,
"ns": 0,
"title": "2026Barchet NonUniform",
"pageid": 3108,
"logpage": 3108,
"revid": 5155,
"params": {},
"type": "create",
"action": "create",
"user": "WikiSysop",
"timestamp": "2026-02-17T04:30:10Z",
"comment": "Created page with \"== Citation == Barchet, C., von Loeffelholz, O., Bahena-Ceron, R., Klaholz, B.P. and Urzhumtsev, A.G. 2026. Explicit correction of severely non-uniform distributions of cryo-EM views. Biological Crystallography. 82, 2 (2026). == Abstract == The quality of three-dimensional macromolecular image reconstruction by cryo electron microscopy (cryo-EM) strongly depends on the number and the quality of the respective two-dimensional projections and on their angular distributi...\""
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