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For: Belsom A, Rappsilber J. Anatomy of a crosslinker. Curr Opin Chem Biol 2021;60:39-46. [PMID: 32829152 DOI: 10.1016/j.cbpa.2020.07.008] [Cited by in Crossref: 8] [Cited by in F6Publishing: 18] [Article Influence: 4.0] [Reference Citation Analysis]
Number Citing Articles
1 Matzinger M, Vasiu A, Madalinski M, Müller F, Stanek F, Mechtler K. Mimicked synthetic ribosomal protein complex for benchmarking crosslinking mass spectrometry workflows. Nat Commun 2022;13:3975. [PMID: 35803948 DOI: 10.1038/s41467-022-31701-w] [Reference Citation Analysis]
2 Wu SY, Wu FG, Chen X. Antibody-Incorporated Nanomedicines for Cancer Therapy. Adv Mater 2022;:e2109210. [PMID: 35142395 DOI: 10.1002/adma.202109210] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
3 Kolbowski L, Lenz S, Fischer L, Sinn LR, O'Reilly FJ, Rappsilber J. Improved Peptide Backbone Fragmentation Is the Primary Advantage of MS-Cleavable Crosslinkers. Anal Chem 2022. [PMID: 35613060 DOI: 10.1021/acs.analchem.1c05266] [Reference Citation Analysis]
4 Karamanos TK, Kalverda AP, Radford SE. Generating Ensembles of Dynamic Misfolding Proteins. Front Neurosci 2022;16:881534. [DOI: 10.3389/fnins.2022.881534] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
5 Sarnowski CP, Bikaki M, Leitner A. Cross-linking and mass spectrometry as a tool for studying the structural biology of ribonucleoproteins. Structure 2022:S0969-2126(22)00084-3. [PMID: 35366400 DOI: 10.1016/j.str.2022.03.003] [Reference Citation Analysis]
6 Yılmaz Ş, Busch F, Nagaraj N, Cox J. Accurate and Automated High-Coverage Identification of Chemically Cross-Linked Peptides with MaxLynx. Anal Chem 2022. [PMID: 35014260 DOI: 10.1021/acs.analchem.1c03688] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
7 Czaplewski C, Gong Z, Lubecka EA, Xue K, Tang C, Liwo A. Recent Developments in Data-Assisted Modeling of Flexible Proteins. Front Mol Biosci 2021;8:765562. [PMID: 35004845 DOI: 10.3389/fmolb.2021.765562] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
8 Klykov O, Kopylov M, Carragher B, Heck AJ, Noble AJ, Scheltema RA. Label-free visual proteomics: Coupling MS- and EM-based approaches in structural biology. Molecular Cell 2022;82:285-303. [DOI: 10.1016/j.molcel.2021.12.027] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
9 Graziadei A, Rappsilber J. Leveraging crosslinking mass spectrometry in structural and cell biology. Structure 2021:S0969-2126(21)00419-6. [PMID: 34895473 DOI: 10.1016/j.str.2021.11.007] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
10 Yugandhar K, Zhao Q, Gupta S, Xiong D, Yu H. Progress in methodologies and quality-control strategies in protein cross-linking mass spectrometry. Proteomics 2021;:e2100145. [PMID: 34647422 DOI: 10.1002/pmic.202100145] [Reference Citation Analysis]
11 Rogawski R, Sharon M. Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry. Chem Rev 2021. [PMID: 34406752 DOI: 10.1021/acs.chemrev.1c00217] [Cited by in Crossref: 2] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
12 Pirklbauer GJ, Stieger CE, Matzinger M, Winkler S, Mechtler K, Dorfer V. MS Annika: A New Cross-Linking Search Engine. J Proteome Res 2021;20:2560-9. [PMID: 33852321 DOI: 10.1021/acs.jproteome.0c01000] [Cited by in F6Publishing: 4] [Reference Citation Analysis]
13 de Jong L, Roseboom W, Kramer G. Towards low false discovery rate estimation for protein-protein interactions detected by chemical cross-linking. Biochim Biophys Acta Proteins Proteom 2021;1869:140655. [PMID: 33812047 DOI: 10.1016/j.bbapap.2021.140655] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
14 Mendes ML, Dittmar G. Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry. Biomolecules 2021;11:505. [PMID: 33801594 DOI: 10.3390/biom11040505] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
15 Kalathiya U, Padariya M, Faktor J, Coyaud E, Alfaro JA, Fahraeus R, Hupp TR, Goodlett DR. Interfaces with Structure Dynamics of the Workhorses from Cells Revealed through Cross-Linking Mass Spectrometry (CLMS). Biomolecules 2021;11:382. [PMID: 33806612 DOI: 10.3390/biom11030382] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
16 Dowling P, Gargan S, Murphy S, Zweyer M, Sabir H, Swandulla D, Ohlendieck K. The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle. Proteomes 2021;9:9. [PMID: 33540575 DOI: 10.3390/proteomes9010009] [Cited by in Crossref: 7] [Cited by in F6Publishing: 9] [Article Influence: 7.0] [Reference Citation Analysis]
17 Mbundi L, González-pérez M, González-pérez F, Juanes-gusano D, Rodríguez-cabello JC. Trends in the Development of Tailored Elastin-Like Recombinamer–Based Porous Biomaterials for Soft and Hard Tissue Applications. Front Mater 2021;7:601795. [DOI: 10.3389/fmats.2020.601795] [Cited by in Crossref: 3] [Cited by in F6Publishing: 7] [Article Influence: 3.0] [Reference Citation Analysis]
18 Matzinger M, Mechtler K. Cleavable Cross-Linkers and Mass Spectrometry for the Ultimate Task of Profiling Protein-Protein Interaction Networks in Vivo. J Proteome Res 2021;20:78-93. [PMID: 33151691 DOI: 10.1021/acs.jproteome.0c00583] [Cited by in Crossref: 8] [Cited by in F6Publishing: 20] [Article Influence: 4.0] [Reference Citation Analysis]