Results 41 to 50 of about 2,230,593 (247)

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

FEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang, Hyo Been Jin, Chang Min Kim, So Yeon Lee, Hyun Ho Park   +4 more
wiley   +1 more source

Zinc-Induced Transposition of Insertion Sequence Elements Contributes to Increased Adaptability of Cupriavidus metallidurans

Frontiers in Microbiology, 2016
Bacteria can respond to adverse environments by increasing their genomic variability and subsequently facilitating adaptive evolution. To demonstrate this, the contribution of Insertion Sequence (IS) elements to the genetic adaptation of Cupriavidus ...
Joachim eVandecraen, Joachim eVandecraen, Pieter eMonsieurs, Max eMergeay, Natalie eLeys, Abram eAertsen, Rob eVan Houdt   +6 more
doaj   +1 more source

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

FEBS Letters, EarlyView.
Proximity‐dependent labeling at the LAMTOR complex revealed the Rho GEF PLEKHG3 as a lysosome‐proximal protein directing the study toward the influence of lysosome positioning on actin dynamics and cell motility. We show that PLEKHG3 colocalizes with lysosomes at focal adhesion sites and observe that forced peripheral dispersion of lysosomes hinders ...
Rainer Ettelt, Ana‐Maria Sandru, Georg Vucak, Sebastian Didusch, Biljana Riemelmoser, Karin Ehrenreiter, Markus Hartl, Lukas A. Huber, Manuela Baccarini   +8 more
wiley   +1 more source

The Rice Annotation Project Database (RAP-DB): 2008 update [PDF]

, 2008
The Rice Annotation Project Database (RAP-DB) was created to provide the genome sequence assembly of the International Rice Genome Sequencing Project (IRGSP), manually curated annotation of the sequence, and other genomics information that could be ...
Raghuvanshi S, Hosokawa, S., SMITH-WHITE, B, Zhao, Q., An, G., Tateno, Y., Imanishi, T., Nobushima, S., SUZUKI, M, NOBUTA, K, Oota, S., Tatusova T, Nakaoka, H., Lu, C., Shinso Y, Takeda, J.-i., Todokoro F, Yamamoto, N., Khurana, J.P., OOta S, Tanaka, T., Kim, H., Sakai, Y., Piegu B, Ito, Y., Hosokawa S, Bruskiewich, R. M., Kubooka H, Harada, E., Messing, J., Lin, Yao-Cheng, HAN, B, Meyers BC, Wei, F-J, Koyanagi, K. O., Sakai, H., Ikeo K, Ohyanagi, H., IKAWA, H, Meyers, B.C., Barrero, R.A., Aono R, Okido, T., Zuccolo, A., HARADA, E, KOYANAGI, KO, Green PJ, Sasaki T, Sato Y, Bureau TE, Nobuta, K., Barrero, R. A., Yamasaki C, Shibata, M., NUMA, H, Zhao Q, Christie, K.R., Lieberherr, D., Kanno M, Panaud O, Bureau, T.E., Souvorov A, MESSING, J, An, G., Messing J, KIM, H, Hsing, Y-i, PIEGU, B, Lonsdale, D., MEYERS, BC, Bin, H., Ito, Y., HABERER, G, Tanino M, BRUSKIEWICH, RM, Aono, R., Namiki, N., Green, P. J., Sanbonmatsu, R., SAKAI, Y, Fujisawa, M., Zuccolo, A., HABARA, T, Shinso, Y., Fujisawa, M., Ohyanagi, H., Yamasaki, C., HOEN, DR, Christie, K. R., Yamaguchi, K., Kramer, M. R., SHIBATA, M, Kubooka, H., Tada, M., Echeverria M., GREEN, PJ, Yamamoto, N., OOta, S., TANAKA, T, Hoen, D. R., Numa H, LONSDALE, D, An, S., Piegu, B., McCombie RW, Echeverria, M., SAKAI, H, Tateno Y, Habara, T., Ikawa, H., TYAGI, AK, Koyanagi, K.O., Itoh T, Gojobori, T., Harada, E., Raghuvanshi, S., Bureau, T. E., Hosokawa, S., Lin YC, Kramer MR, ANTONIO, BA, Yamamoto, M., Apweiler R, Kubooka, H., TATUSOVA, T, Kawahara Y, Suzuki M, TAKEDA, JI, Lonsdale, D., Antonio BA, Sanbonmatsu, R., Shinso, Y., KHURANA, JP, IMANISHI, T, Kanno, M., Tatusova, T., Hsing YI, FUJISAWA, M, Haberer, G., Numa, H., Yamaguchi, K., Ikeo, K., Todokoro, F., Ikeo, K., Chaparro, C., Singh, N. K., ECHEVERRIA, M, Smith-White, B., Ohyanagi H, Nagamura, Y., Wei, F. J., Wing, R. A., Habara T, NAKAOKA, H, PANAUD, O, WEI, FJ, Fujii, Y., Fuks G, Namiki N, Kikuchi, S., KRAMER, MR, MATSUYA, A, KAWASHIMA, H, Tanino, M., Whitfield, E.J., Christie KR, Harada E, Okido T, Todokoro, F., Saichi N, Singh, N.K., Sasaki, T., Numa, H., Sakata K, NOBUSHIMA, S, MCCOMBIE, RW, Kawashima, H., Kawahara, Y., Zhao, Q., Haberer, G., Bruskiewich, R.M., NAMIKI, N, IKEO, K, Ikawa, H., Nobuta K, Nakaoka H, Piegu, B., Tanino, M., Tateno, Y., KUBOOKA, H, Tanaka, T., HSING, YI, Antonio, B. A., Kim, H-R, SATO, Y, An G, Saichi, N., Suzuki, M., CHRISTIE, KR, Fuks, G., Barrero RA, APWEILER, R, Sato, Y., Tyagi, A. K., ITO, Y, YAMASAKI, C, FUKS, G, AONO, R, YAMAMOTO, M, YAMAMOTO, N, TADA, M, O'Donovan, C. C., TODOKORO, F, Kim H, WU, J, ZUCCOLO, A, OKIDO, T, Shibata M, Matsuya, A., McCombie, R. W., Koyanagi KO, HOSOKAWA, S, Apweiler, R., Chaparro C, BARRERO, RA, Tanaka T, Nobuta, K., Fujii, Y., Tyagi AK, SANBONMATSU, R, SAKATA, K, An S, Echeverria, M., Sakai, H., Tatusova, T., Fujisawa M, Sakata, K., Kawashima H, Lin, Y. C., WING, RA, OOTA, S, Wu, J., Habara, T., Whitfield EJ, LU, C, An, S., Lin, Y-C, Wu, J., Hoen DR, O'DONOVAN, CC, Han B, SHINSO, Y, Smith White B, Whitfield, E. J., Okido, T., Green, P.J., TATENO, Y, KIKUCHI, S, Kawahara, Y., Apweiler, R., Wu J, Kramer, M.R., Kikuchi S, Matsumoto, T., Kawashima, H., Hoen, D.R., Ito Y, Nobushima S, ZHAO, Q, SASAKI, T, Souvorov, A., Tada, M., Sakai, Y., LIEBERHERR, D, Sanbonmatsu R, McCombie, R.W., Fujii Y, Matsuya, A., Fuks, G., Lieberherr, D., Lieberherr D, Antonio, B.A., Ikawa H, Sakata, K., Raghuvanshi, S., MATSUMOTO, T, SAICHI, N, Nobushima, S., Yamamoto N, Gojobori T, Sakai Y, Yamamoto M, Singh NK, Hsing, Y. I., Smith-White, B., Lu C, NAGAMURA, Y, Khurana, J. P., AN, S, Tada M, Souvorov, A., Shibata, M., O'Donovan CC, Sakai H, KANNO, M, Nagamura Y, FUJII, Y, KAWAHARA, Y, Kikuchi, S., AN, G, Sasaki, T., Meyers, B. C., YAMAGUCHI, K, Suzuki, M., Han, B., ZUCCOLO, ANDREA, CHAPARRO, C, Bruskiewich RM, Chaparro, C., Aono, R., SOUVOROV, A, Nakaoka, H., O’Donovan, C.C., OHYANAGI, H, Yamasaki, C., Imanishi T, Lonsdale D, TANINO, M, BUREAU, TE, Lu, C., Panaud, O., Yamaguchi K, Kanno, M., Wing, R.A., Sato, Y., Matsumoto T, ITOH, T, GOJOBORI, T, Panaud, O., Messing, J., Haberer G, Saichi, N., Matsuya A, Wing RA, Khurana JP, Tyagi, A.K., Namiki, N., Itoh, T., Itoh, T., Imanishi, T., SINGH, NK, Matsumoto, T., Nagamura, Y., Yamamoto, M., RAGHUVANSHI, S, Takeda, J. I., Wei FJ, Takeda J, WHITFIELD, EJ, Gojobori, T.   +359 more
core   +1 more source

Intracellular Transposition of Mobile Genetic Elements Associated with the Colistin Resistance Gene mcr-1

Microbiology Spectrum, 2023
Mobile colistin resistance (mcr) genes are often located on conjugative plasmids, where their association with insertion sequences enables intercellular and intracellular dissemination throughout bacterial replicons and populations.
Richard N. Goodman, Supathep Tansirichaiya, Michael S. M. Brouwer, Adam P. Roberts   +3 more
doaj   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

FEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang, Ruslana Romaniuk, Hristo L. Svilenov   +2 more
wiley   +1 more source

Deep learning for HGT insertion sites recognition

BMC Genomics, 2020
Background Horizontal Gene Transfer (HGT) refers to the sharing of genetic materials between distant species that are not in a parent-offspring relationship. The HGT insertion sites are important to understand the HGT mechanisms.
Chen Li, Jiaxing Chen, Shuai Cheng Li
doaj   +1 more source

Insertion variants missing in the human reference genome are widespread among human populations

BMC Biology, 2020
Background Structural variants comprise diverse genomic arrangements including deletions, insertions, inversions, and translocations, which can generally be detected in humans through sequence comparison to the reference genome. Among structural variants,
Young-gun Lee, Jin-young Lee, Junhyong Kim, Young-Joon Kim   +3 more
doaj   +1 more source

Golgi enzymes are retrieved from the plasma membrane to the trans‐Golgi network

FEBS Letters, EarlyView.
Golgi enzymes are traditionally considered resident proteins retained within the Golgi apparatus. Here, we demonstrate that a subset transiently reaches the cell surface and is subsequently retrieved to the trans‐Golgi network via retrograde transport. Using a nanobody‐based toolkit, we uncover a dynamic trafficking cycle of several Golgi enzymes.
Dominik P. Buser, Tina Junne
wiley   +1 more source

Summary of insertion position and the sequence of insertion in forms of split compact groups.

, 2022
Summary of insertion position and the sequence of insertion in forms of split compact groups.
Suphakant Phimoltares (5724890), Chidchanok Lursinsap (5724896), Suluk Chaikhan (12354520)   +2 more
core   +1 more source