NMRPipe: A multidimensional spectral processing system based on UNIX pipes

The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects

Johnson, C. W., Reid, D., Parker, J. A., Salter, S., Knihtila, R., Kuzmic, P., & Mattos, C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778886 · Cited by 133

Dynamic binding mode of a Synaptotagmin-1–SNARE complex in solution

Brewer, K. D., Bacaj, T., Cavalli, A., Camilloni, C., Swarbrick, J. D., Liu, J., Zhou, A., Zhou, P., Barlow, N., Xu, J., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3035 · Cited by 142

The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping

Heras, B., Totsika, M., Peters, K. M., Paxman, J. J., Gee, C. L., Jarrott, R. J., Perugini, M. A., Whitten, A. E., & Schembri, M. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311592111 · Cited by 141

Structural basis of sialyltransferase activity in trypanosomal sialidases

Buschiazzo, A., Tavares, G. A., Campetella, O., Spinelli, S., Cremona, M. L., París, G., Fernanda Amaya, M., Frasch, A. C. C., & Alzari, P. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.16 · Cited by 138

TGFβ2 and TGFβ3 isoforms drive fibrotic disease pathogenesis

Sun, T., Huang, Z., Liang, W.-C., Yin, J., Lin, W. Y., Wu, J., Vernes, J.-M., Lutman, J., Caplazi, P., Jeet, S., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe0407 · Cited by 134

Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2

Pádua, R. A. P., Sun, Y., Marko, I., Pitsawong, W., Stiller, J. B., Otten, R., & Kern, D. (2018) · Nature Communications · doi:10.1038/s41467-018-06814-w · Cited by 133

The Structure of an Interdomain Complex That Regulates Talin Activity

Goult, B. T., Bate, N., Anthis, N. J., Wegener, K. L., Gingras, A. R., Patel, B., Barsukov, I. L., Campbell, I. D., Roberts, G. C. K., & Critchley, D. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900078200 · Cited by 131

Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53

Kostic, M., Matt, T., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.027 · Cited by 128

Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106

Su, D., Hu, Q., Li, Q., Thompson, J. R., Cui, G., Fazly, A., Davies, B. A., Botuyan, M. V., Zhang, Z., & Mer, G. (2012) · Nature · doi:10.1038/nature10861 · Cited by 128

Crystal Structure of the Antioxidant Enzyme Glutathione Reductase Inactivated by Peroxynitrite

Savvides, S. N., Scheiwein, M., Böhme, C. C., Arteel, G. E., Karplus, P. A., Becker, K., & Schirmer, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108190200 · Cited by 127

Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex

Fukai, S., Matern, H. T., Jagath, J. R., Scheller, R. H., & Brunger, A. T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg329 · Cited by 126

Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses 1 1Edited by P. E. Wright

Campos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119

Solution Structure of ERK2 Binding Domain of MAPK Phosphatase MKP-3

Farooq, A., Chaturvedi, G., Mujtaba, S., Plotnikova, O., Zeng, L., Dhalluin, C., Ashton, R., & Zhou, M.-M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00186-1 · Cited by 119

Structure and self-association of the Rous sarcoma virus capsid protein

Kingston, R. L., Fitzon-Ostendorp, T., Eisenmesser, E. Z., Schatz, G. W., Vogt, V. M., Post, C. B., & Rossmann, M. G. (2000) · Structure · doi:10.1016/s0969-2126(00)00148-9 · Cited by 112

Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis

Weiss, A., Murdoch, C. C., Edmonds, K. A., Jordan, M. R., Monteith, A. J., Perera, Y. R., Rodríguez Nassif, A. M., Petoletti, A. M., Beavers, W. N., Munneke, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.011 · Cited by 113

Nicotinamide Riboside Is a Major NAD+ Precursor Vitamin in Cow Milk

Trammell, S. A., Yu, L., Redpath, P., Migaud, M. E., & Brenner, C. (2016) · The Journal of Nutrition · doi:10.3945/jn.116.230078 · Cited by 112

USP7-specific inhibitors target and modify the enzyme’s active site via distinct chemical mechanisms.

Pozhidaeva, A., Valles, G., Wang, F., Wu, J., Sterner, D. E., Nguyen, P., Weinstock, J., Kumar, K. G. S., Kanyo, J., Wright, D., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.004 · Cited by 107

An allosteric interaction links USP7 to deubiquitination and chromatin targeting of UHRF1.

Zhang, Z.-M., Rothbart, S. B., Allison, D. F., Cai, Q., Harrison, J. S., Li, L., Wang, Y., Strahl, B. D., Wang, G. G., & Song, J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.046 · Cited by 99

TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Ma, W., & Goldberg, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605916113 · Cited by 108

Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice

Guo, S., Stevens, C. A., Vance, T. D. R., Olijve, L. L. C., Graham, L. A., Campbell, R. L., Yazdi, S. R., Escobedo, C., Bar-Dolev, M., Yashunsky, V., et al. (2017) · Science Advances · doi:10.1126/sciadv.1701440 · Cited by 107

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06880-0 · Cited by 100

Tyrosyl phosphorylation of KRAS stalls GTPase cycle via alteration of switch I and II conformation

Kano, Y., Gebregiworgis, T., Marshall, C. B., Radulovich, N., Poon, B. P. K., St-Germain, J., Cook, J. D., Valencia-Sama, I., Grant, B. M. M., Herrera, S. G., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08115-8 · Cited by 103

Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin

Kurzbach, D., Platzer, G., Schwarz, T. C., Henen, M. A., Konrat, R., & Hinderberger, D. (2013) · Biochemistry · doi:10.1021/bi400502c · Cited by 105

Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56

Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95

Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus

Bamford, N. C., Snarr, B. D., Gravelat, F. N., Little, D. J., Lee, M. J., Zacharias, C. A., Chabot, J. C., Geller, A. M., Baptista, S. D., Baker, P., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679050 · Cited by 102

Peptide lipidation stabilizes structure to enhance biological function

Ward, B. P., Ottaway, N. L., Perez-Tilve, D., Ma, D., Gelfanov, V. M., Tschöp, M. H., & DiMarchi, R. D. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.08.008 · Cited by 101

Recognition of ERK MAP kinase by PEA‐15 reveals a common docking site within the death domain and death effector domain

Hill, J. M., Vaidyanathan, H., Ramos, J. W., Ginsberg, M. H., & Werner, M. H. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf641 · Cited by 100

Tricyclic Covalent Inhibitors Selectively Target Jak3 through an Active Site Thiol

Goedken, E. R., Argiriadi, M. A., Banach, D. L., Fiamengo, B. A., Foley, S. E., Frank, K. E., George, J. S., Harris, C. M., Hobson, A. D., Ihle, D. C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595181 · Cited by 101

Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-β Pathways

Aragón, E., Goerner, N., Xi, Q., Gomes, T., Gao, S., Massagué, J., & Macias, M. J. (2012) · Structure · doi:10.1016/j.str.2012.07.014 · Cited by 99

Frog Skins Keep Redox Homeostasis by Antioxidant Peptides with Rapid Radical Scavenging Ability

Liu, C., Hong, J., Yang, H., Wu, J., Ma, D., Li, D., Lin, D., & Lai, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.036 · Cited by 97

Structural insights into adeno-associated virus serotype 5

Govindasamy, L., DiMattia, M. A., Gurda, B. L., Halder, S., McKenna, R., Chiorini, J. A., Muzyczka, N., Zolotukhin, S., & Agbandje-McKenna, M. (2013) · Journal of Virology · doi:10.1128/jvi.00867-13 · Cited by 95

The Structural and Dynamic Basis of Ets-1 DNA Binding Autoinhibition

Lee, G. M., Donaldson, L. W., Pufall, M. A., Kang, H.-S., Pot, I., Graves, B. J., & McIntosh, L. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410722200 · Cited by 95

Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting

Saad, J. S., Ablan, S. D., Ghanam, R. H., Kim, A., Andrews, K., Nagashima, K., Soheilian, F., Freed, E. O., & Summers, M. F. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.027 · Cited by 95

Integrated RAS signaling defined by parallel NMR detection of effectors and regulators

Smith, M. J., & Ikura, M. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1435 · Cited by 87

Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site

Fang, Z., Marshall, C. B., Nishikawa, T., Gossert, A. D., Jansen, J. M., Jahnke, W., & Ikura, M. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.07.009 · Cited by 86

PFAS and Dissolved Organic Carbon Enrichment in Surface Water Foams on a Northern U.S. Freshwater Lake

Schwichtenberg, T., Bogdan, D., Carignan, C. C., Reardon, P., Rewerts, J., Wanzek, T., & Field, J. A. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c05697 · Cited by 91

Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase

Durbecq, V., Sainz, G., Oudjama, Y., Clantin, B., Bompard‐Gilles, C., Tricot, C., Caillet, J., Stalon, V., Droogmans, L., & Villeret, V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1530 · Cited by 90

Discovery of small-molecule inhibitors of ubiquitin specific protease 7 (USP7) using integrated NMR and in silico techniques

Di Lello, P., Pastor, R., Murray, J. M., Blake, R. A., Cohen, F., Crawford, T. D., Drobnick, J., Drummond, J., Kategaya, L., Kleinheinz, T., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01293 · Cited by 90

The Structural Basis for RNA Selectivity by the IMP Family of RNA-Binding Proteins

Biswas, J., Patel, V. L., Bhaskar, V., Chao, J. A., Singer, R. H., & Eliscovich, C. (2019) · Nature Communications · doi:10.1038/s41467-019-12193-7 · Cited by 84

Arid5a regulates naive CD4+ T cell fate through selective stabilization of Stat3 mRNA

Masuda, K., Ripley, B., Nyati, K. K., Dubey, P. K., Zaman, M. M.-U., Hanieh, H., Higa, M., Yamashita, K., Standley, D. M., Mashima, T., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151289 · Cited by 88

High Pressure NMR Reveals that Apomyoglobin is an Equilibrium Mixture from the Native to the Unfolded

Kitahara, R., Yamada, H., Akasaka, K., & Wright, P. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00449-7 · Cited by 85

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84

Novel lactoferrampin antimicrobial peptides derived from human lactoferrin

HANEY, E., NAZMI, K., LAU, F., BOLSCHER, J., & VOGEL, H. (2009) · Biochimie · doi:10.1016/j.biochi.2008.04.013 · Cited by 81

Structure of the Brd4 ET domain bound to a C-terminal motif from γ-retroviral integrases reveals a conserved mechanism of interaction

Crowe, B. L., Larue, R. C., Yuan, C., Hess, S., Kvaratskhelia, M., & Foster, M. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516813113 · Cited by 83

Restricted Motion of the Conserved Immunoglobulin G1 N-Glycan Is Essential for Efficient FcγRIIIa Binding

Subedi, G. P., Hanson, Q. M., & Barb, A. W. (2014) · Structure · doi:10.1016/j.str.2014.08.002 · Cited by 81

Eps15 Homology Domain 1-associated Tubules Contain Phosphatidylinositol-4-Phosphate and Phosphatidylinositol-(4,5)-Bisphosphate and Are Required for Efficient Recycling

Jović, M., Kieken, F., Naslavsky, N., Sorgen, P. L., & Caplan, S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-11-1102 · Cited by 81

Rational optimization of a transcription factor activation domain inhibitor

Basu, S., Martínez-Cristóbal, P., Frigolé-Vivas, M., Pesarrodona, M., Lewis, M., Szulc, E., Bañuelos, C. A., Sánchez-Zarzalejo, C., Bielskutė, S., Zhu, J., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01159-5 · Cited by 83

Structural basis of p38α regulation by hematopoietic tyrosine phosphatase

Francis, D. M., Różycki, B., Koveal, D., Hummer, G., Page, R., & Peti, W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.707 · Cited by 79

Development of near-zero water consumption cement materials via the geopolymerization of tektites and its implication for lunar construction

Wang, K.-T., Tang, Q., Cui, X.-M., He, Y., & Liu, L.-P. (2016) · Scientific Reports · doi:10.1038/srep29659 · Cited by 79

High-affinity interaction of the K-Ras4B hypervariable region with the RAS active site

Chavan, T. S., Jang, H., Khavrutskii, L., Abraham, S. J., Banerjee, A., Freed, B. C., Johannessen, L., Tarasov, S. G., Gaponenko, V., Nussinov, R., et al. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.034 · Cited by 79

Solution structure of an informationally complex high-affinity RNA aptamer to GTP

CAROTHERS, J. M., DAVIS, J. H., CHOU, J. J., & SZOSTAK, J. W. (2006) · RNA · doi:10.1261/rna.2251306 · Cited by 78

Atomic resolution mechanism of ligand binding to a solvent inaccessible cavity in T4 lysozyme

(2018) · doi:10.1371/journal.pcbi.1006180 · Cited by 77

Influence of iron and aeration on Staphylococcus aureus growth, metabolism, and transcription

Ledala, N., Zhang, B., Seravalli, J., Powers, R., & Somerville, G. A. (2014) · Journal of Bacteriology · doi:10.1128/jb.01475-14 · Cited by 74

Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor

Eftekharzadeh, B., Banduseela, V. C., Chiesa, G., Martínez-Cristóbal, P., Rauch, J. N., Nath, S. R., Schwarz, D. M. C., Shao, H., Marin-Argany, M., Di Sanza, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11594-y · Cited by 76

Structural and Biochemical Characterization of a Fluorogenic Rhodamine-Labeled Malarial Protease Substrate

Blackman, M. J., Corrie, J. E. T., Croney, J. C., Kelly, G., Eccleston, J. F., & Jameson, D. M. (2002) · Biochemistry · doi:10.1021/bi0263661 · Cited by 73

Altering murine leukemia virus integration through disruption of the integrase and BET protein family interaction

Aiyer, S., Swapna, G. V. T., Malani, N., Aramini, J. M., Schneider, W. M., Plumb, M. R., Ghanem, M., Larue, R. C., Sharma, A., Studamire, B., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku175 · Cited by 72

The N-Terminal Region of Amyloid β Controls the Aggregation Rate and Fibril Stability at Low pH through a Gain of Function Mechanism

Brännström, K., Öhman, A., Nilsson, L., Pihl, M., Sandblad, L., & Olofsson, A. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503535m · Cited by 74

High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded β-Barrel Fold

Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73

An interaction between Scribble and the NADPH oxidase complex controls M1 macrophage polarization and function

Zheng, W., Umitsu, M., Jagan, I., Tran, C. W., Ishiyama, N., BeGora, M., Araki, K., Ohashi, P. S., Ikura, M., & Muthuswamy, S. K. (2016) · Nature Cell Biology · doi:10.1038/ncb3413 · Cited by 60

Rotamer-free protein sequence design based on deep learning and self-consistency

Liu, Y., Zhang, L., Wang, W., Zhu, M., Wang, C., Li, F., Zhang, J., Li, H., Chen, Q., & Liu, H. (2022) · Nature Computational Science · doi:10.1038/s43588-022-00273-6 · Cited by 72

The Mechanism of Hsp90 ATPase Stimulation by Aha1

Wolmarans, A., Lee, B., Spyracopoulos, L., & LaPointe, P. (2016) · Scientific Reports · doi:10.1038/srep33179 · Cited by 72

Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces

Barré, P., & Eliezer, D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.018 · Cited by 69

Correction of the NMR structure of the ETS1/DNA complex

Werner, M. H., Clore, G. M., Fisher, C. L., Fisher, R. J., Trinh, L., Shiloach, J., & Gronenborn, A. M. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018399711996 · Cited by 68

Soluble TREM2 inhibits secondary nucleation of Aβ fibrillization and enhances cellular uptake of fibrillar Aβ

Belsare, K. D., Wu, H., Mondal, D., Bond, A., Castillo, E., Jin, J., Jo, H., Roush, A. E., Pilla, K. B., Sali, A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114486119 · Cited by 68

Diversity in Structure and Function of the Ets Family PNT Domains

Mackereth, C. D., Schärpf, M., Gentile, L. N., MacIntosh, S. E., Slupsky, C. M., & McIntosh, L. P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.094 · Cited by 67

Tadpole-like conformations of Huntingtin Exon 1 are characterized by conformational heterogeneity that persists regardless of polyglutamine length

Newcombe, E. A., Ruff, K. M., Sethi, A., Ormsby, A. R., Ramdzan, Y. M., Fox, A., Purcell, A. W., Gooley, P. R., Pappu, R. V., & Hatters, D. M. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.031 · Cited by 66

Molecular Analysis of the Interaction between the Hematopoietic Master Transcription Factors GATA-1 and PU.1

Liew, C. W., Rand, K. D., Simpson, R. J. Y., Yung, W. W., Mansfield, R. E., Crossley, M., Proetorius-Ibba, M., Nerlov, C., Poulsen, F. M., & Mackay, J. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602830200 · Cited by 63

Structural and biochemical characterization of the yeast exosome component Rrp40

Oddone, A., Lorentzen, E., Basquin, J., Gasch, A., Rybin, V., Conti, E., & Sattler, M. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7400856 · Cited by 62

Different regions of synaptic vesicle membrane regulate VAMP2 conformation for the SNARE assembly

Wang, C., Tu, J., Zhang, S., Cai, B., Liu, Z., Hou, S., Zhong, Q., Hu, X., Liu, W., Li, G., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15270-4 · Cited by 55

Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network

Lopez, A., Dahiya, V., Delhommel, F., Freiburger, L., Stehle, R., Asami, S., Rutz, D., Blair, L., Buchner, J., & Sattler, M. (2021) · Science Advances · doi:10.1126/sciadv.abl7295 · Cited by 59

VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins

Swarbrick, J. D., Shaw, D. J., Chhabra, S., Ghai, R., Valkov, E., Norwood, S. J., Seaman, M. N. J., & Collins, B. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020420 · Cited by 59

The Affinity of Ets-1 for DNA is Modulated by Phosphorylation Through Transient Interactions of an Unstructured Region

Lee, G. M., Pufall, M. A., Meeker, C. A., Kang, H.-S., Graves, B. J., & McIntosh, L. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.064 · Cited by 58

KRASQ61H Preferentially Signals through MAPK in a RAF Dimer-Dependent Manner in Non–Small Cell Lung Cancer

Zhou, Z.-W., Ambrogio, C., Bera, A. K., Li, Q., Li, X.-X., Li, L., Son, J., Gondi, S., Li, J., Campbell, E., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0448 · Cited by 60

Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry

Mealman, T. D., Bagai, I., Singh, P., Goodlett, D. R., Rensing, C., Zhou, H., Wysocki, V. H., & McEvoy, M. M. (2011) · Biochemistry · doi:10.1021/bi102012j · Cited by 53

Computational design of closely related proteins that adopt two well-defined but structurally divergent folds

Wei, K. Y., Moschidi, D., Bick, M. J., Nerli, S., McShan, A. C., Carter, L. P., Huang, P.-S., Fletcher, D. A., Sgourakis, N. G., Boyken, S. E., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914808117 · Cited by 57

Functional Dynamics of Human FKBP12 Revealed by Methyl 13 C Rotating Frame Relaxation Dispersion NMR Spectroscopy

Brath, U., Akke, M., Yang, D., Kay, L. E., & Mulder, F. A. A. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0570279 · Cited by 57

Rac regulates its effector phospholipase Cγ2 through interaction with a split pleckstrin homology domain

Walliser, C., Retlich, M., Harris, R., Everett, K. L., Josephs, M. B., Vatter, P., Esposito, D., Driscoll, P. C., Katan, M., Gierschik, P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803316200 · Cited by 56

Structural insights into the effects of 2’-5’ linkages on the RNA duplex

Sheng, J., Li, L., Engelhart, A. E., Gan, J., Wang, J., & Szostak, J. W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317799111 · Cited by 50

Oxaloacetic acid mediates ADP-dependent inhibition of mitochondrial complex II-driven respiration

Fink, B. D., Bai, F., Yu, L., Sheldon, R. D., Sharma, A., Taylor, E. B., & Sivitz, W. I. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005144 · Cited by 54

Continuous in vivo Metabolism by NMR

Judge, M. T., Wu, Y., Tayyari, F., Hattori, A., Glushka, J., Ito, T., Arnold, J., & Edison, A. S. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00026 · Cited by 53

Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1

Dove, K. K., Olszewski, J. L., Martino, L., Duda, D. M., Wu, X. S., Miller, D. J., Reiter, K. H., Rittinger, K., Schulman, B. A., & Klevit, R. E. (2017) · Structure · doi:10.1016/j.str.2017.04.013 · Cited by 52

Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

Abelein, A., Ciofi-Baffoni, S., Mörman, C., Kumar, R., Giachetti, A., Piccioli, M., & Biverstål, H. (2022) · JACS Au · doi:10.1021/jacsau.2c00438 · Cited by 52

YdiV regulates Escherichia coli ferric uptake by manipulating the DNA-binding ability of Fur in a SlyD-dependent manner

Zhang, F., Li, B., Dong, H., Chen, M., Yao, S., Li, J., Zhang, H., Liu, X., Wang, H., Song, N., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa696 · Cited by 49

Crystal Structure of the Tp34 (TP0971) Lipoprotein of Treponema pallidum

Deka, R. K., Brautigam, C. A., Tomson, F. L., Lumpkins, S. B., Tomchick, D. R., Machius, M., & Norgard, M. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610215200 · Cited by 50

The Q61H mutation decouples KRAS from upstream regulation and renders cancer cells resistant to SHP2 inhibitors

Gebregiworgis, T., Kano, Y., St-Germain, J., Radulovich, N., Udaskin, M. L., Mentes, A., Huang, R., Poon, B. P. K., He, W., Valencia-Sama, I., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26526-y · Cited by 49

New Insights into Histidine Triad Proteins: Solution Structure of a Streptococcus pneumoniae PhtD Domain and Zinc Transfer to AdcAII

Bersch, B., Bougault, C., Roux, L., Favier, A., Vernet, T., & Durmort, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081168 · Cited by 49

Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting

Lenoir, M., Ustunel, C., Rajesh, S., Kaur, J., Moreau, D., Gruenberg, J., & Overduin, M. (2018) · Nature Communications · doi:10.1038/s41467-018-03370-1 · Cited by 49

Domain substructure of HPV E6 oncoprotein: Biophysical characterization of the E6 C-terminal DNA-binding domain

Nominé, Y., Charbonnier, S., Ristriani, T., Stier, G., Masson, M., Cavusoglu, N., Van Dorsselaer, A., Weiss, É., Kieffer, B., & Travé, G. (2003) · Biochemistry · doi:10.1021/bi026980c · Cited by 49

Striatins contain a noncanonical coiled coil that binds protein phosphatase 2A A subunit to form a 2:2 heterotetrameric core of striatin-interacting phosphatase and kinase (STRIPAK) complex

Chen, C., Shi, Z., Zhang, W., Chen, M., He, F., Zhang, Z., Wang, Y., Feng, M., Wang, W., Zhao, Y., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.529297 · Cited by 47

Chemical profiling of complex biochemical mixtures from various seaweeds

Date, Y., Sakata, K., & Kikuchi, J. (2012) · Polymer Journal · doi:10.1038/pj.2012.105 · Cited by 47

Bimodal high-affinity association of Brd4 with murine leukemia virus integrase and mononucleosomes

Larue, R. C., Plumb, M. R., Crowe, B. L., Shkriabai, N., Sharma, A., DiFiore, J., Malani, N., Aiyer, S. S., Roth, M. J., Bushman, F. D., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku135 · Cited by 44

Ubiquitin Interacts with the Tollip C2 and CUE Domains and Inhibits Binding of Tollip to Phosphoinositides

Mitra, S., Traughber, C. A., Brannon, M. K., Gomez, S., & Capelluto, D. G. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.484170 · Cited by 46

Modulating co-translational protein folding by rational design and ribosome engineering

Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45

Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature

Kamatari, Y. O., Smith, L. J., Dobson, C. M., & Akasaka, K. (2011) · Biophysical Chemistry · doi:10.1016/j.bpc.2011.01.009 · Cited by 46

The zinc efflux activator Scz A protects Streptococcus pneumoniae serotype 2 D 39 from intracellular zinc toxicity

Martin, J. E., Edmonds, K. A., Bruce, K. E., Campanello, G. C., Eijkelkamp, B. A., Brazel, E. B., McDevitt, C. A., Winkler, M. E., & Giedroc, D. P. (2017) · Molecular Microbiology · doi:10.1111/mmi.13654 · Cited by 38

Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity.

Kim, R. Q., Geurink, P. P., Mulder, M. P. C., Fish, A., Ekkebus, R., El Oualid, F., van Dijk, W. J., van Dalen, D., Ovaa, H., van Ingen, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08231-5 · Cited by 41

An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling

Kim, S. K., Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768754 · Cited by 43

Lipids Regulate Lck Protein Activity through Their Interactions with the Lck Src Homology 2 Domain

Sheng, R., Jung, D.-J., Silkov, A., Kim, H., Singaram, I., Wang, Z.-G., Xin, Y., Kim, E., Park, M.-J., Thiagarajan-Rosenkranz, P., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.720284 · Cited by 43

Functional and structural characterization of a dense core secretory granule sorting domain from the PC1/3 protease

Dikeakos, J. D., Di Lello, P., Lacombe, M.-J., Ghirlando, R., Legault, P., Reudelhuber, T. L., & Omichinski, J. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809576106 · Cited by 40

Structural and Functional Comparison of the RING Domains of Two p53 E3 Ligases, Mdm2 and Pirh2

Shloush, J., Vlassov, J. E., Engson, I., Duan, S., Saridakis, V., Dhe-paganon, S., Raught, B., Sheng, Y., & Arrowsmith, C. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157669 · Cited by 42