Viswanathan Chinnusamy

Plant Science · 2003–2018

A researcher in the Science corpus: 10 papers; trusts 24 researchers and is trusted by 25 researchers here, as inferred from the citation graph.

Subfields

Whom Viswanathan Chinnusamy trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

  1. Jian‐Kang Zhu
  2. Ramanjulu Sunkar
  3. Lizhong Xiong
  4. Huazhong Shi
  5. Kazuko Yamaguchi-Shinozaki
  6. Sarah G. Fowler
  7. Kazuo Shinozaki
  8. O. Borsani
  9. Daniel Zilberman
  10. M. Thomashow

Who trusts Viswanathan Chinnusamy overall

  1. Jian‐Kang Zhu
  2. Julia Krasensky
  3. Narendra Kumar Tuteja
  4. M. Thomashow
  5. A. Venkateswarlu
  6. R. Mittler
  7. G. Onaga
  8. Sudesh Kumar Yadav
  9. Leila Heidarvand
  10. Erica E. Benson

Papers from Viswanathan Chinnusamy's perspective

Ordered by how strongly the researchers Viswanathan Chinnusamy trusts endorse each paper. Same corpus, a different order for every researcher.

  1. Arabidopsis basic leucine zipper transcription factors involved in an abscisic acid-dependent signal transduction pathway under drought and high-salinity conditions. (Proceedings of the National Academy of Sciences of the United States of America)
  2. microRNA-directed phasing during trans-acting siRNA biogenesis in plants. (Cell)
  3. CARPEL FACTORY, a Dicer homolog, and HEN1, a novel protein, act in microRNA metabolism in Arabidopsis thaliana. (Current Biology)
  4. Empirical Analysis of Transcriptional Activity in the Arabidopsis Genome (Science)
  5. Transgenic salt-tolerant tomato plants accumulate salt in foliage but not in fruit (Nature Biotechnology)
  6. Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6. (The Plant Journal)
  7. Functional analysis of oxidative stress-activated mitogen-activated protein kinase cascade in plants. (Proceedings of the National Academy of Sciences of the United States of America)
  8. Control of leaf morphogenesis by microRNAs (Nature)
  9. The negative regulator of plant cold responses, HOS1, is a RING E3 ligase that mediates the ubiquitination and degradation of ICE1. (Proceedings of the National Academy of Sciences of the United States of America)
  10. Computational identification of plant microRNAs and their targets, including a stress-induced miRNA. (Molecules and Cells)

Their papers