- Structural Dynamics Associated with Intermediate Formation in an Archetypal Conformational Disease
[作者：Nyon, MP; Segu, L; Cabrita, LD; Levy, GR; Kirkpatrick, J; Roussel, BD; Patschull, AOM; Barrett, TE; Ekeowa, UI; Kerr, R; Waudby, CA; Kalsheker, N; Hil, M; Thalassinos, K; Lomas, DA; Christodoulou, J; Gooptu, B,期刊：Structure, 页码：504-512 , 文章类型： Article，,卷期：2012年20-3]
- In conformational diseases, native protein conformers convert to pathological intermediates that polymerize. Structural characterization of these key intermediates is challenging. They are unstable and minimally populate...
- The Structure of the 26S Proteasome Subunit Rpn2 Reveals Its PC Repeat Domain as a Closed Toroid of Two Concentric alpha-Helical Rings
[作者：He, J; Kulkarni, K; da Fonseca, PCA; Krutauz, D; Glickman, MH; Barford, D; Morris, EP,期刊：Structure, 页码：513-521 , 文章类型： Article，,卷期：2012年20-3]
- The 26S proteasome proteolyses ubiquitylated proteins and is assembled from a 20S proteolytic core and two 19S regulatory particles (19S-RP). The 19S-RP scaffolding subunits Rpn1 and Rpn2 function to engage ubiquitin rec...
- Recognition Pliability Is Coupled to Structural Heterogeneity: A Calmodulin Intrinsically Disordered Binding Region Complex
[作者：Nagulapalli, M; Parigi, G; Yuan, J; Gsponer, J; Deraos, G; Bamm, VV; Harauz, G; Matsoukas, J; de Planque, MRR; Gerothanassis, IP; Babu, MM; Luchinat, C; Tzakos, AG,期刊：Structure, 页码：522-533 , 文章类型： Article，,卷期：2012年20-3]
- Protein interactions within regulatory networks should adapt in a spatiotemporal-dependent dynamic environment, in order to process and respond to diverse and versatile cellular signals. However, the principles governing...
- Cdc6-Induced Conformational Changes in ORC Bound to Origin DNA Revealed by Cryo-Electron Microscopy
[作者：Sun, JC; Kawakami, H; Zech, J; Speck, C; Stillman, B; Li, HL,期刊：Structure, 页码：534-544 , 文章类型： Article，,卷期：2012年20-3]
- The eukaryotic origin recognition complex (ORC) interacts with and remodels origins of DNA replication prior to initiation in S phase. Here, we report a single-particle cryo-EM-derived structure of the supramolecular ass...
- Structure of the Cmr2 Subunit of the CRISPR-Cas RNA Silencing Complex
[作者：Cocozaki, AI; Ramie, NF; Shao, YM; Hale, CR; Terns, RM; Terns, MP; Li, H,期刊：Structure, 页码：545-553 , 文章类型： Article，,卷期：2012年20-3]
- Cmr2 is the largest and an essential subunit of a CRISPR RNA-Cas protein complex (the Cmr complex) that cleaves foreign RNA to protect prokaryotes from invading genetic elements. Cmr2 is thought to be the catalytic subun...
- Architecture of a Dodecameric Bacterial Replicative Helicase
[作者：Stelter, M; Gutsche, I; Kapp, U; Bazin, A; Bajic, G; Goret, G; Jamin, M; Timmins, J; Terradot, L,期刊：Structure, 页码：554-564 , 文章类型： Article，,卷期：2012年20-3]
- Hexameric DnaB helicases are often loaded at DNA replication forks by interacting with the initiator protein DnaA and/or a helicase loader (DnaC in Escherichia coil). These loaders are not universally required, and DnaB ...
- UBAP1: A New ESCRT Member Joins the cl_Ub
[作者：Pashkova, N; Piper, RC,期刊：Structure, 页码：383-385 , 文章类型： Editorial Material，,卷期：2012年20-3]
- The ESCRTs play multiple roles within the cell, including degradation of ubiquitinated membrane proteins by sorting them into multivesicular bodies (MVBs). Two recent studies provide structural and functional insights in...
- The 19S Cap Puzzle: A New Jigsaw Piece
[作者：Huber, EM; Groll, M,期刊：Structure, 页码：387-388 , 文章类型： Editorial Material，,卷期：2012年20-3]
- After elucidation of the atomic details of 20S proteasomes, current research focuses on the regulatory 19S particle. In this issue of Structure, He et al. present the crystal structure of Rpn2 and use electron microscopy...
- Cas Protein Cmr2 Full of Surprises
[作者：Huang, RH,期刊：Structure, 页码：389-390 , 文章类型： Editorial Material，,卷期：2012年20-3]
- The Cmr complex carries out target RNA degradation in organisms possessing the CRISPR-Cas system. In this issue of Structure, Cocozaki et al. present the crystal structure of Cmr2, providing insight into the architecture...
- The Protein Data Bank at 40: Reflecting on the Past to Prepare for the Future
[作者：Berman, HM; Kleywegt, GJ; Nakamura, H; Markley, JL,期刊：Structure, 页码：391-396 , 文章类型： News Item，,卷期：2012年20-3]
- A symposium celebrating the 40th anniversary of the Protein Data Bank archive (PDB), organized by the Worldwide Protein Data Bank, was held at Cold Spring Harbor Laboratory (CSHL) October 28-30, 2011. PDB40's distinguish...
- The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain
[作者：Agromayor, M; Soler, N; Caballe, A; Kueck, T; Freund, SM; Allen, MD; Bycroft, M; Perisic, O; Ye, Y; McDonald, B; Scheel, H; Hofmann, K; Neil, SJD; Martin-Serrano, J; Williams, RL,期刊：Structure, 页码：414-428 , 文章类型： Article，,卷期：2012年20-3]
- The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associa...
- Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin
[作者：Saccoccia, F; Di Micco, P; Boumis, G; Brunori, M; Koutris, I; Miele, AE; Morea, V; Sriratana, P; Williams, DL; Bellelli, A; Angelucci, F,期刊：Structure, 页码：429-439 , 文章类型： Article，,卷期：2012年20-3]
- 2-Cys peroxiredoxins (Prxs) play two different roles depending on the physiological status of the cell. They are thioredoxin-dependent peroxidases under low oxidative stress and ATP-independent chaperones upon exposure t...
- Mechanistic Insights into the Activation of Rad51-Mediated Strand Exchange from the Structure of a Recombination Activator, the Swi5-Sfr1 Complex
[作者：Kuwabara, N; Murayama, Y; Hashimoto, H; Kokabu, Y; Ikeguchi, M; Sato, M; Mayanagi, K; Tsutsui, Y; Iwasaki, H; Shimizu, T,期刊：Structure, 页码：440-449 , 文章类型： Article，,卷期：2012年20-3]
- Rad51 forms a helical filament on single-stranded DNA and promotes strand exchange between two homologous DNA molecules during homologous recombination. The Swi5-Sfr1 complex interacts directly with Rad51 and stimulates ...
|